data/structure/seqwords.seq

ID   ACEA_ECOLI     STANDARD;      PRT;   434 AA.
AC   P05313;
DT   01-NOV-1988 (Rel. 09, Created)
DT   01-NOV-1988 (Rel. 09, Last sequence update)
DT   15-DEC-1998 (Rel. 37, Last annotation update)
DE   ISOCITRATE LYASE (EC 4.1.3.1) (ISOCITRASE) (ISOCITRATASE) (ICL).
GN   ACEA OR ICL.
OS   Escherichia coli.
OC   Bacteria; Proteobacteria; gamma subdivision; Enterobacteriaceae;
OC   Escherichia.
RN   [1]
RP   SEQUENCE FROM N.A.
RC   STRAIN=K12;
RX   MEDLINE; 89083515.
RA   Byrne C.R., Stokes H.W., Ward K.A.;
RT   "Nucleotide sequence of the aceB gene encoding malate synthase A in
RT   Escherichia coli.";
RL   Nucleic Acids Res. 16:10924-10924(1988).
RN   [2]
RP   SEQUENCE FROM N.A.
RC   STRAIN=K12;
RX   MEDLINE; 88262573.
RA   Rieul C., Bleicher F., Duclos B., Cortay J.-C., Cozzone A.J.;
RT   "Nucleotide sequence of the aceA gene coding for isocitrate lyase in
RT   Escherichia coli.";
RL   Nucleic Acids Res. 16:5689-5689(1988).
RN   [3]
RP   SEQUENCE FROM N.A.
RX   MEDLINE; 89008064.
RA   Matsuoka M., McFadden B.A.;
RT   "Isolation, hyperexpression, and sequencing of the aceA gene encoding
RT   isocitrate lyase in Escherichia coli.";
RL   J. Bacteriol. 170:4528-4536(1988).
RN   [4]
RP   SEQUENCE FROM N.A.
RC   STRAIN=K12 / MG1655;
RX   MEDLINE; 94089392.
RA   Blattner F.R., Burland V.D., Plunkett G. III, Sofia H.J.,
RA   Daniels D.L.;
RT   "Analysis of the Escherichia coli genome. IV. DNA sequence of the
RT   region from 89.2 to 92.8 minutes.";
RL   Nucleic Acids Res. 21:5408-5417(1993).
RN   [5]
RP   SEQUENCE OF 293-434 FROM N.A.
RX   MEDLINE; 88227861.
RA   Klumpp D.J., Plank D.W., Bowdin L.J., Stueland C.S., Chung T.,
RA   Laporte D.C.;
RT   "Nucleotide sequence of aceK, the gene encoding isocitrate
RT   dehydrogenase kinase/phosphatase.";
RL   J. Bacteriol. 170:2763-2769(1988).
RN   [6]
RP   PHOSPHORYLATION.
RX   MEDLINE; 88115398.
RA   Robertson E.F., Hoyt J.C., Reeves H.C.;
RT   "Evidence of histidine phosphorylation in isocitrate lyase from
RT   Escherichia coli.";
RL   J. Biol. Chem. 263:2477-2488(1988).
RN   [7]
RP   CHARACTERIZATION.
RX   MEDLINE; 88269580.
RA   Hoyt J.C., Robertson E.F., Berlyn K.A., Reeves H.C.;
RT   "Escherichia coli isocitrate lyase: properties and comparisons.";
RL   Biochim. Biophys. Acta 966:30-35(1988).
RN   [8]
RP   MUTAGENESIS OF CYS-195.
RC   STRAIN=ML308;
RX   MEDLINE; 95126911.
RA   Robertson A.G., Nimmo H.G.;
RT   "Site-directed mutagenesis of cysteine-195 in isocitrate lyase from
RT   Escherichia coli ML308.";
RL   Biochem. J. 305:239-244(1995).
CC   -!- CATALYTIC ACTIVITY: ISOCITRATE = SUCCINATE + GLYOXYLATE.
CC   -!- COFACTOR: REQUIRES DIVALENT CATIONS.
CC   -!- ENZYME REGULATION: IS ACTIVATED BY PHOSPHORYLATION (ON HISTIDINE)
CC       AND IS INHIBITED BY PEP, 3-PHOSPHOGLYCERATE AND SUCCINATE.
CC   -!- PATHWAY: FIRST STEP IN GLYOXYLATE BYPASS, AN ALTERNATIVE TO THE
CC       TRICARBOXYLIC ACID CYCLE (IN BACTERIA, PLANTS, AND FUNGI).
CC   -!- SUBUNIT: HOMOTETRAMER.
CC   -!- SUBCELLULAR LOCATION: CYTOPLASMIC.
CC   -!- SIMILARITY: BELONGS TO THE ISOCITRATE LYASE FAMILY.
CC   --------------------------------------------------------------------------
CC   This SWISS-PROT entry is copyright. It is produced through a collaboration
CC   between  the Swiss Institute of Bioinformatics  and the  EMBL outstation -
CC   the European Bioinformatics Institute.  There are no  restrictions on  its
CC   use  by  non-profit  institutions as long  as its content  is  in  no  way
CC   modified and this statement is not removed.  Usage  by  and for commercial
CC   entities requires a license agreement (See http://www.isb-sib.ch/announce/
CC   or send an email to license@isb-sib.ch).
CC   --------------------------------------------------------------------------
DR   EMBL; X12431; CAA30974.1; -.
DR   EMBL; X07543; CAA30416.1; -.
DR   EMBL; M20714; AAA24009.1; -.
DR   EMBL; U00006; AAC43109.1; -.
DR   EMBL; AE000474; AAC76985.1; -.
DR   EMBL; M22621; AAC13650.1; -.
DR   PIR; S05692; WZECIC.
DR   SWISS-2DPAGE; P05313; COLI.
DR   ECOGENE; EG10022; ACEA.
DR   INTERPRO; IPR000918; -.
DR   PFAM; PF00463; ICL; 2.
DR   PROSITE; PS00161; ISOCITRATE_LYASE; 1.
KW   Glyoxylate bypass; Tricarboxylic acid cycle; Lyase; Phosphorylation.
FT   ACT_SITE    195    195       PROBABLE.
FT   MUTAGEN     195    195       C->A: LARGE DECREASE IN ACTIVITY.
FT   MUTAGEN     195    195       C->S: LARGE DECREASE IN ACTIVITY.
FT   CONFLICT    101    117       LAASMYPDQSLYPANSV -> WRPACIRISRSIRQTRC
FT                                (IN REF. 2).
FT   CONFLICT    215    215       A -> P (IN REF. 2).
FT   CONFLICT    293    293       P -> R (IN REF. 5).
FT   CONFLICT    338    338       Q -> E (IN REF. 2).
FT   CONFLICT    419    434       TSSVTALTGSTEESQF -> DVFSHRADRLH
FT                                (IN REF. 3).
SQ   SEQUENCE   434 AA;  47521 MW;  F66449CCD1E168E9 CRC64;
     MKTRTQQIEE LQKEWTQPRW EGITRPYSAE DVVKLRGSVN PECTLAQLGA AKMWRLLHGE
     SKKGYINSLG ALTGGQALQQ AKAGIEAVYL SGWQVAADAN LAASMYPDQS LYPANSVPAV
     VERINNTFRR ADQIQWSAGI EPGDPRYVDY FLPIVADAEA GFGGVLNAFE LMKAMIEAGA
     AAVHFEDQLA SVKKCGHMGG KVLVPTQEAI QKLVAARLAA DVTGVPTLLV ARTDADAADL
     ITSDCDPYDS EFITGERTSE GFFRTHAGIE QAISRGLAYA PYADLVWCET STPDLELARR
     FAQAIHAKYP GKLLAYNCSP SFNWQKNLDD KTIASFQQQL SDMGYKFQFI TLAGIHSMWF
     NMFDLANAYA QGEGMKHYVE KVQQPEFAAA KDGYTFVSHQ QEVGTGYFDK VTTIIQGGTS
     SVTALTGSTE ESQF
//
ID   ALR1_YEAST     STANDARD;      PRT;   859 AA.
AC   Q08269; Q02811;
DT   01-NOV-1997 (Rel. 35, Created)
DT   01-NOV-1997 (Rel. 35, Last sequence update)
DT   15-DEC-1998 (Rel. 37, Last annotation update)
DE   ALUMINIUM RESISTANCE PROTEIN 1.
GN   ALR1 OR YOL130W.
OS   Saccharomyces cerevisiae (Baker's yeast).
OC   Eukaryota; Fungi; Ascomycota; Saccharomycetes; Saccharomycetales;
OC   Saccharomycetaceae; Saccharomyces.
RN   [1]
RP   SEQUENCE FROM N.A.
RC   STRAIN=S288C / FY1679;
RX   MEDLINE; 97051588.
RA   Casamayor A., Khalid H., Balcells L., Aldea M., Casas C.,
RA   Herrero E., Arino J.;
RT   "Sequence analysis of a 13.4 kbp fragment from the left arm of
RT   chromosome XV reveals a malate dehydrogenase gene, a putative Ser/Thr
RT   protein kinase, the ribosomal L25 gene and four new open reading
RT   frames.";
RL   Yeast 12:1013-1020(1996).
RN   [2]
RP   IDENTIFICATION.
RA   McDiarmid C.W., Gardner R.C.;
RL   Unpublished observations (XXX-1995).
CC   -!- SIMILARITY: STRONG, TO YEAST ALR2. AND ALSO SIMILAR TO MNR2.
CC   -!- SIMILARITY: SOME, TO E.COLI CORA.
CC   --------------------------------------------------------------------------
CC   This SWISS-PROT entry is copyright. It is produced through a collaboration
CC   between  the Swiss Institute of Bioinformatics  and the  EMBL outstation -
CC   the European Bioinformatics Institute.  There are no  restrictions on  its
CC   use  by  non-profit  institutions as long  as its content  is  in  no  way
CC   modified and this statement is not removed.  Usage  by  and for commercial
CC   entities requires a license agreement (See http://www.isb-sib.ch/announce/
CC   or send an email to license@isb-sib.ch).
CC   --------------------------------------------------------------------------
DR   EMBL; Z74872; CAA99150.1; -.
DR   EMBL; Z74871; CAA99149.1; -.
DR   EMBL; U41293; AAC49462.1; -.
DR   SGD; L0002887; ALR1.
DR   INTERPRO; IPR002523; -.
DR   PFAM; PF01544; CorA; 1.
KW   Transmembrane.
FT   TRANSMEM    744    764       POTENTIAL.
FT   TRANSMEM    773    793       POTENTIAL.
FT   CONFLICT     13     13       N -> Y (IN AAC49462).
SQ   SEQUENCE   859 AA;  95869 MW;  6DA44CA70EFA2693 CRC64;
     MSSSSSSSES SPNLSRSNSL ANTMVSMKTE DHTGLYDHRQ HPDSLPVRHQ PPTLKNKEIA
     KSTKPSIPKE QKSATRYNSH VDVGSVPSRG RMDFEDEGQG MDETVAHHQL RASAILTSNA
     RPSRLAHSMP HQRQLYVESN IHTPPKDVGV KRDYTMSSST ASSGNKSKLS ASSSASPITK
     VRKSSLVSPV LEIPHESKSD THSKLAKPKK RTYSTTSAHS SINPAVLLTK STSQKSDADD
     DTLERKPVRM NTRASFDSDV SQASRDSQET EEDVCFPMPP QLHTRVNGID FDELEEYAQF
     ANAEKSQFLA SLQVPNEQKY SNVSQDIGFT SSTSTSGSSA ALKYTPRVSQ TGEKSESTNE
     TEIHEKKEDE HEKIKPSLHP GISFGKNKVE GEENENIPSN DPAYCSYQGT DFQIPNRFSF
     FCSESDETVH ASDIPSLVSE GQTFYELFRG GEPTWWLDCS CPTDDEMRCI AKAFGIHPLT
     AEDIRMQETR EKVELFKSYY FVCFHTFEND KESEDFLEPI NVYIVVCRSG VLTFHFGPIS
     HCANVRRRVR QLRDYVNVNS DWLCYALIDD ITDSFAPVIQ SIEYEADAIE DSVFMARDMD
     FAAMLQRIGE SRRKTMTLMR LLSGKADVIK MFAKRCQDEA NGIGPALTSQ INIANLQARQ
     DNASHIKNNS STTVPNNYAP TTSQPRGDIA LYLGDIQDHL LTMFQNLLAY EKIFSRSHTN
     YLAQLQVESF NSNNKVTEML GKVTMIGTML VPLNVITGLF GMNVKVPGEN SSIAWWFGIL
     GVLLLLAVLG WFLASYWIKR IDPPATLNEA AESGAKSVIS SFLPKRNKRF NDRSKNINVR
     AGPSNKSVAS LPSRYSRYD
//
ID   GOX_SPIOL      STANDARD;      PRT;   369 AA.
AC   P05414;
DT   01-NOV-1988 (Rel. 09, Created)
DT   01-NOV-1988 (Rel. 09, Last sequence update)
DT   15-DEC-1998 (Rel. 37, Last annotation update)
DE   (S)-2-HYDROXY-ACID OXIDASE, PEROXISOMAL (EC 1.1.3.15) (GLYCOLATE
DE   OXIDASE) (GOX) (SHORT CHAIN ALPHA-HYDROXY ACID OXIDASE).
OS   Spinacia oleracea (Spinach).
OC   Eukaryota; Viridiplantae; Embryophyta; Tracheophyta; Spermatophyta;
OC   Magnoliophyta; eudicotyledons; Caryophyllidae; Caryophyllales;
OC   Chenopodiaceae; Spinacia.
RN   [1]
RP   SEQUENCE FROM N.A.
RX   MEDLINE; 88058933.
RA   Volokita M., Somerville C.R.;
RT   "The primary structure of spinach glycolate oxidase deduced from the
RT   DNA sequence of a cDNA clone.";
RL   J. Biol. Chem. 262:15825-15828(1987).
RN   [2]
RP   SEQUENCE.
RX   MEDLINE; 88225066.
RA   Cederlund E., Lindqvist Y., Soederlund G., Braenden C.-I.,
RA   Joernvall H.;
RT   "Primary structure of glycolate oxidase from spinach.";
RL   Eur. J. Biochem. 173:523-530(1988).
RN   [3]
RP   X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
RX   MEDLINE; 90040713.
RA   Lindqvist Y.;
RT   "Refined structure of spinach glycolate oxidase at 2-A resolution.";
RL   J. Mol. Biol. 209:151-166(1989).
RN   [4]
RP   ACTIVE SITE.
RX   MEDLINE; 89123500.
RA   Lindqvist Y., Braenden C.-I.;
RT   "The active site of spinach glycolate oxidase.";
RL   J. Biol. Chem. 264:3624-3628(1989).
CC   -!- CATALYTIC ACTIVITY: (S)-2-HYDROXY-ACID + O(2) = 2-OXO ACID +
CC       H(2)O(2).
CC   -!- COFACTOR: FMN.
CC   -!- PATHWAY: SECOND REACTION OF THE PHOTORESPIRATORY PATHWAY
CC       (GLYCOLATE PATHWAY).
CC   -!- SUBUNIT: HOMOTETRAMER OR HOMOOCTAMER.
CC   -!- SUBCELLULAR LOCATION: PEROXISOMAL.
CC   -!- SIMILARITY: BELONGS TO THE FMN-DEPENDENT ALPHA-HYDROXY ACID
CC       DEHYDROGENASES FAMILY.
CC   --------------------------------------------------------------------------
CC   This SWISS-PROT entry is copyright. It is produced through a collaboration
CC   between  the Swiss Institute of Bioinformatics  and the  EMBL outstation -
CC   the European Bioinformatics Institute.  There are no  restrictions on  its
CC   use  by  non-profit  institutions as long  as its content  is  in  no  way
CC   modified and this statement is not removed.  Usage  by  and for commercial
CC   entities requires a license agreement (See http://www.isb-sib.ch/announce/
CC   or send an email to license@isb-sib.ch).
CC   --------------------------------------------------------------------------
DR   EMBL; J03492; AAA34030.1; -.
DR   PIR; A28496; OXSPH.
DR   PIR; S00621; S00621.
DR   PDB; 1GOX; 15-OCT-89.
DR   PDB; 1AL7; 12-NOV-97.
DR   PDB; 1AL8; 17-SEP-97.
DR   PDB; 1GYL; 31-MAR-95.
DR   INTERPRO; IPR000262; -.
DR   PFAM; PF01070; FMN_dh; 1.
DR   PROSITE; PS00342; MICROBODIES_CTER; 1.
DR   PROSITE; PS00557; FMN_HYDROXY_ACID_DH; 1.
KW   Oxidoreductase; Flavoprotein; FMN; Peroxisome; Glycolate pathway;
KW   Photorespiration; 3D-structure; Acetylation.
FT   MOD_RES       1      1       ACETYLATION.
FT   SIMILAR     159    186       WITH CUCUMBER MALATE SYNTHETASE AND
FT                                SOYBEAN NODULIN 35.
FT   ACT_SITE     24     24       SUBSTRATE BINDING.
FT   ACT_SITE    129    129       SUBSTRATE BINDING.
FT   ACT_SITE    254    254       REMOVES THE SUBSTRATE ALPHA-PROTON AS THE
FT                                FIRST STEP IN CATALYSIS.
FT   ACT_SITE    257    257       SUBSTRATE BINDING.
FT   SITE        367    369       MICROBODY TARGETING SIGNAL (POTENTIAL).
FT   TURN          6      7
FT   HELIX         8     16
FT   HELIX        19     26
FT   TURN         30     31
FT   HELIX        33     44
FT   STRAND       45     47
FT   STRAND       59     59
FT   STRAND       62     64
FT   TURN         65     66
FT   STRAND       67     69
FT   STRAND       73     75
FT   HELIX        81     83
FT   TURN         84     84
FT   TURN         86     87
FT   HELIX        88     98
FT   TURN         99    100
FT   STRAND      103    105
FT   TURN        107    108
FT   HELIX       113    117
FT   TURN        118    119
FT   STRAND      124    128
FT   STRAND      131    131
FT   HELIX       134    146
FT   TURN        147    148
FT   STRAND      151    155
FT   HELIX       165    169
FT   TURN        170    171
FT   TURN        176    177
FT   HELIX       181    183
FT   HELIX       199    205
FT   TURN        206    206
FT   STRAND      207    207
FT   TURN        209    210
FT   HELIX       213    222
FT   STRAND      227    230
FT   HELIX       235    243
FT   TURN        244    245
FT   STRAND      248    251
FT   HELIX       254    256
FT   TURN        257    257
FT   TURN        260    261
FT   HELIX       265    275
FT   TURN        276    278
FT   STRAND      282    285
FT   HELIX       291    300
FT   TURN        301    301
FT   STRAND      304    307
FT   HELIX       309    341
FT   TURN        342    342
FT   STRAND      345    345
FT   TURN        346    348
FT   HELIX       351    353
FT   STRAND      354    356
FT   TURN        357    358
SQ   SEQUENCE   369 AA;  40285 MW;  892F1B3D0C1B48E0 CRC64;
     MEITNVNEYE AIAKQKLPKM VYDYYASGAE DQWTLAENRN AFSRILFRPR ILIDVTNIDM
     TTTILGFKIS MPIMIAPTAM QKMAHPEGEY ATARAASAAG TIMTLSSWAT SSVEEVASTG
     PGIRFFQLYV YKDRNVVAQL VRRAERAGFK AIALTVDTPR LGRREADIKN RFVLPPFLTL
     KNFEGIDLGK MDKANDSGLS SYVAGQIDRS LSWKDVAWLQ TITSLPILVK GVITAEDARL
     AVQHGAAGII VSNHGARQLD YVPATIMALE EVVKAAQGRI PVFLDGGVRR GTDVFKALAL
     GAAGVFIGRP VVFSLAAEGE AGVKKVLQMM RDEFELTMAL SGCRSLKEIS RSHIAADWDG
     PSSRAVARL
//
ID   ICLR_ECOLI     STANDARD;      PRT;   274 AA.
AC   P16528; P76782;
DT   01-AUG-1990 (Rel. 15, Created)
DT   01-AUG-1990 (Rel. 15, Last sequence update)
DT   01-NOV-1997 (Rel. 35, Last annotation update)
DE   ACETATE OPERON REPRESSOR.
GN   ICLR.
OS   Escherichia coli.
OC   Bacteria; Proteobacteria; gamma subdivision; Enterobacteriaceae;
OC   Escherichia.
RN   [1]
RP   SEQUENCE FROM N.A.
RX   MEDLINE; 90236928.
RA   Sunnarborg A., Klumpp D.J., Chung T., Laporte D.C.;
RT   "Regulation of the glyoxylate bypass operon: cloning and
RT   characterization of iclR.";
RL   J. Bacteriol. 172:2642-2649(1990).
RN   [2]
RP   SEQUENCE FROM N.A.
RC   STRAIN=K12;
RX   MEDLINE; 91138983.
RA   Negre D., Cortay J.-C., Old I.G., Galinier A., Richaud C.,
RA   Saint-Girons I., Cozzone A.J.;
RT   "Overproduction and characterization of the iclR gene product of
RT   Escherichia coli K-12 and comparison with that of Salmonella
RT   typhimurium LT2.";
RL   Gene 97:29-37(1991).
RN   [3]
RP   SEQUENCE FROM N.A.
RC   STRAIN=K12 / MG1655;
RX   MEDLINE; 94089392.
RA   Blattner F.R., Burland V.D., Plunkett G. III, Sofia H.J.,
RA   Daniels D.L.;
RT   "Analysis of the Escherichia coli genome. IV. DNA sequence of the
RT   region from 89.2 to 92.8 minutes.";
RL   Nucleic Acids Res. 21:5408-5417(1993).
RN   [4]
RP   SEQUENCE OF 262-274 FROM N.A.
RX   MEDLINE; 91138981.
RA   Galinier A., Bleicher F., Negre D., Perriere G., Duclos B.,
RA   Cozzone A.J., Cortay J.-C.;
RT   "Primary structure of the intergenic region between aceK and iclR in
RT   the Escherichia coli chromosome.";
RL   Gene 97:149-150(1991).
CC   -!- FUNCTION: REGULATION OF THE GLYOXYLATE BYPASS OPERON (ACEBAK),
CC       WHICH ENCODES ISOCITRATE LYASE, MALATE SYNTHASE AS WELL AS
CC       ISOCITRATE DEHYDROGENASE KINASE/PHOSPHORYLASE.
CC   -!- SIMILARITY: BELONGS TO THE ICLR FAMILY OF TRANSCRIPTIONAL
CC       REGULATORS.
CC   --------------------------------------------------------------------------
CC   This SWISS-PROT entry is copyright. It is produced through a collaboration
CC   between  the Swiss Institute of Bioinformatics  and the  EMBL outstation -
CC   the European Bioinformatics Institute.  There are no  restrictions on  its
CC   use  by  non-profit  institutions as long  as its content  is  in  no  way
CC   modified and this statement is not removed.  Usage  by  and for commercial
CC   entities requires a license agreement (See http://www.isb-sib.ch/announce/
CC   or send an email to license@isb-sib.ch).
CC   --------------------------------------------------------------------------
DR   EMBL; M31761; AAA24008.1; -.
DR   EMBL; M63914; AAA50561.1; ALT_INIT.
DR   EMBL; U00006; AAC43112.1; ALT_INIT.
DR   EMBL; AE000475; AAC76988.1; ALT_INIT.
DR   EMBL; M63497; AAA73003.1; -.
DR   PIR; A35267; RPECIR.
DR   PIR; JQ0871; JQ0871.
DR   ECOGENE; EG10491; ICLR.
DR   INTERPRO; IPR000285; -.
DR   PFAM; PF01614; IclR; 1.
DR   PROSITE; PS01051; HTH_ICLR_FAMILY; 1.
KW   Transcription regulation; Glyoxylate bypass; DNA-binding;
KW   Repressor.
FT   DNA_BIND     46     65       H-T-H MOTIF (POTENTIAL).
SQ   SEQUENCE   274 AA;  29739 MW;  7C8A7E9FD2841D0C CRC64;
     MVAPIPAKRG RKPAVATAPA TGQVQSLTRG LKLLEWIAES NGSVALTELA QQAGLPNSTT
     HRLLTTMQQQ GFVRQVGELG HWAIGAHAFM VGSSFLQSRN LLAIVHPILR NLMEESGETV
     NMAVLDQSDH EAIIIDQVQC THLMRMSAPI GGKLPMHASG AGKAFLAQLS EEQVTKLLHR
     KGLHAYTHAT LVSPVHLKED LAQTRKRGYS FDDEEHALGL RCLAACIFDE HREPFAAISI
     SGPISRITDD RVTEFGAMVI KAAKEVTLAY GGMR
//
ID   MDH_ECOLI      STANDARD;      PRT;   312 AA.
AC   P06994; Q59343; Q59344; Q59345; Q59346; Q59347; Q59348; Q60133;
AC   Q60150; O30401; O30402; O30403;
DT   01-APR-1988 (Rel. 07, Created)
DT   01-NOV-1995 (Rel. 32, Last sequence update)
DT   30-MAY-2000 (Rel. 39, Last annotation update)
DE   MALATE DEHYDROGENASE (EC 1.1.1.37).
GN   MDH.
OS   Escherichia coli.
OC   Bacteria; Proteobacteria; gamma subdivision; Enterobacteriaceae;
OC   Escherichia.
RN   [1]
RP   SEQUENCE FROM N.A.
RX   MEDLINE; 87259981.
RA   McAlister-Henn L., Blaber M., Bradshaw R.A., Nisco S.J.;
RT   "Complete nucleotide sequence of the Escherichia coli gene encoding
RT   malate dehydrogenase.";
RL   Nucleic Acids Res. 15:4993-4993(1987).
RN   [2]
RP   SEQUENCE FROM N.A.
RX   MEDLINE; 88105815.
RA   Vogel R.F., Entian K.-D., Mecke D.;
RT   "Cloning and sequence of the mdh structural gene of Escherichia coli
RT   coding for malate dehydrogenase.";
RL   Arch. Microbiol. 149:36-42(1987).
RN   [3]
RP   SEQUENCE FROM N.A.
RC   STRAIN=K12 / MG1655;
RX   MEDLINE; 97426617.
RA   Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA   Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA   Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J.,
RA   Mau B., Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1474(1997).
RN   [4]
RP   SEQUENCE OF 1-40 FROM N.A.
RX   MEDLINE; 85288979.
RA   Sutherland P., McAlister-Henn L.;
RT   "Isolation and expression of the Escherichia coli gene encoding
RT   malate dehydrogenase.";
RL   J. Bacteriol. 163:1074-1079(1985).
RN   [5]
RP   SEQUENCE OF 1-36.
RX   MEDLINE; 82047078.
RA   Fernley R.T., Lentz S.R., Bradshaw R.A.;
RT   "Malate dehydrogenase: isolation from E. coli and comparison with the
RT   eukaryotic mitochondrial and cytoplasmic forms.";
RL   Biosci. Rep. 1:497-507(1981).
RN   [6]
RP   SEQUENCE OF 1-16.
RX   MEDLINE; 93281685.
RA   Henzel W.J., Billeci T.M., Stults J.T., Wong S.C., Grimley C.,
RA   Watanabe C.;
RT   "Identifying proteins from two-dimensional gels by molecular mass
RT   searching of peptide fragments in protein sequence databases.";
RL   Proc. Natl. Acad. Sci. U.S.A. 90:5011-5015(1993).
RN   [7]
RP   SEQUENCE OF 1-26.
RC   STRAIN=K12 / EMG2;
RX   MEDLINE; 97443975.
RA   Link A.J., Robison K., Church G.M.;
RT   "Comparing the predicted and observed properties of proteins encoded
RT   in the genome of Escherichia coli K-12.";
RL   Electrophoresis 18:1259-1313(1997).
RN   [8]
RP   SEQUENCE OF 1-26.
RA   Charnock C.;
RL   Submitted (JAN-1996) to the SWISS-PROT data bank.
RN   [9]
RP   SEQUENCE OF 1-11.
RC   STRAIN=K12 / W3110;
RA   Frutiger S., Hughes G.J., Pasquali C., Hochstrasser D.F.;
RL   Submitted (FEB-1996) to the SWISS-PROT data bank.
RN   [10]
RP   SEQUENCE OF 1-13.
RX   MEDLINE; 96283620.
RA   Nystroem T., Larsson C., Gustafsson L.;
RT   "Bacterial defense against aging: role of the Escherichia coli ArcA
RT   regulator in gene expression, readjusted energy flux and survival
RT   during stasis.";
RL   EMBO J. 15:3219-3228(1996).
RN   [11]
RP   SEQUENCE OF 12-299 FROM N.A.
RC   STRAIN=VARIOUS STRAINS;
RX   MEDLINE; 94151313.
RA   Boyd E.F., Nelson K., Wang F.S., Whittam T.S., Selander R.K.;
RT   "Molecular genetic basis of allelic polymorphism in malate
RT   dehydrogenase (mdh) in natural populations of Escherichia coli and
RT   Salmonella enterica.";
RL   Proc. Natl. Acad. Sci. U.S.A. 91:1280-1284(1994).
RN   [12]
RP   SEQUENCE OF 12-299 FROM N.A.
RC   STRAIN=VARIOUS STRAINS;
RX   MEDLINE; 97342740.
RA   Pupo G.M., Karaolis D.K., Lan R., Reeves P.R.;
RT   "Evolutionary relationships among pathogenic and nonpathogenic
RT   Escherichia coli strains inferred from multilocus enzyme
RT   electrophoresis and mdh sequence studies.";
RL   Infect. Immun. 65:2685-2692(1997).
RN   [13]
RP   X-RAY CRYSTALLOGRAPHY (1.87 ANGSTROMS).
RX   MEDLINE; 92373767.
RA   Hall M.D., Levitt D.G., Banaszak L.J.;
RT   "Crystal structure of Escherichia coli malate dehydrogenase. A
RT   complex of the apoenzyme and citrate at 1.87-A resolution.";
RL   J. Mol. Biol. 226:867-882(1992).
CC   -!- CATALYTIC ACTIVITY: L-MALATE + NAD(+) = OXALOACETATE + NADH.
CC   -!- SUBUNIT: HOMODIMER.
CC   -!- SIMILARITY: BELONGS TO THE LDH FAMILY. MDH SUBFAMILY.
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CC   the European Bioinformatics Institute.  There are no  restrictions on  its
CC   use  by  non-profit  institutions as long  as its content  is  in  no  way
CC   modified and this statement is not removed.  Usage  by  and for commercial
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DR   EMBL; M10417; AAA24147.1; -.
DR   EMBL; M24777; AAA16107.1; -.
DR   EMBL; U18997; AAA58038.1; -.
DR   EMBL; AE000403; AAC76268.1; -.
DR   EMBL; Y00129; CAA68326.1; -.
DR   EMBL; U04742; AAC43730.1; -.
DR   EMBL; U04743; AAC43731.1; -.
DR   EMBL; U04744; AAC43732.1; -.
DR   EMBL; U04745; AAC43733.1; -.
DR   EMBL; U04746; AAC43734.1; -.
DR   EMBL; U04747; AAC43735.1; -.
DR   EMBL; U04748; AAC43736.1; -.
DR   EMBL; U04749; AAC43737.1; -.
DR   EMBL; U04750; AAC43738.1; -.
DR   EMBL; U04751; AAC43739.1; -.
DR   EMBL; U04752; AAC43740.1; -.
DR   EMBL; U04753; AAC43741.1; -.
DR   EMBL; U04754; AAC43742.1; -.
DR   EMBL; U04755; AAC43743.1; -.
DR   EMBL; U04756; AAC43744.1; -.
DR   EMBL; U04757; AAC43745.1; -.
DR   EMBL; U04758; AAC43746.1; -.
DR   EMBL; U04759; AAC43747.1; -.
DR   EMBL; U04760; AAC43748.1; -.
DR   EMBL; U04770; AAC43758.1; -.
DR   EMBL; AF004170; AAB87003.1; -.
DR   EMBL; AF004171; AAB87004.1; -.
DR   EMBL; AF004172; AAB87005.1; -.
DR   EMBL; AF004173; AAB87006.1; -.
DR   EMBL; AF004174; AAB87007.1; -.
DR   EMBL; AF004175; AAB87008.1; -.
DR   EMBL; AF004176; AAB87009.1; -.
DR   EMBL; AF004177; AAB87010.1; -.
DR   EMBL; AF004179; AAB87012.1; -.
DR   EMBL; AF004180; AAB87013.1; -.
DR   EMBL; AF004182; AAB87015.1; -.
DR   EMBL; AF004183; AAB87016.1; -.
DR   EMBL; AF004184; AAB87017.1; -.
DR   EMBL; AF004186; AAB87019.1; -.
DR   EMBL; AF004187; AAB87020.1; -.
DR   EMBL; AF004188; AAB87021.1; -.
DR   EMBL; AF004190; AAB87023.1; -.
DR   EMBL; AF004191; AAB87024.1; -.
DR   EMBL; AF004195; AAB87028.1; -.
DR   EMBL; AF004196; AAB87029.1; -.
DR   EMBL; AF004199; AAB87032.1; -.
DR   EMBL; AF004200; AAB87033.1; -.
DR   EMBL; AF004201; AAB87034.1; -.
DR   EMBL; AF004202; AAB87035.1; -.
DR   EMBL; AF004203; AAB87036.1; -.
DR   EMBL; AF004204; AAB87037.1; -.
DR   EMBL; AF004205; AAB87038.1; -.
DR   EMBL; AF004206; AAB87039.1; -.
DR   EMBL; AF004207; AAB87040.1; -.
DR   EMBL; AF004208; AAB87041.1; -.
DR   EMBL; AF004209; AAB87042.1; -.
DR   PIR; A26525; DEECM.
DR   PDB; 2CMD; 31-OCT-93.
DR   PDB; 1CME; 31-JAN-94.
DR   PDB; 1EMD; 31-OCT-93.
DR   SWISS-2DPAGE; P06994; COLI.
DR   ECO2DBASE; F030.2; 6TH EDITION.
DR   ECOGENE; EG10576; MDH.
DR   INTERPRO; IPR001236; -.
DR   INTERPRO; IPR001252; -.
DR   PFAM; PF00056; ldh; 1.
DR   PROSITE; PS00068; MDH; 1.
KW   Oxidoreductase; Tricarboxylic acid cycle; NAD; 3D-structure.
FT   ACT_SITE    150    150       PROTON-RELAY.
FT   BINDING     153    153       SUBSTRATE CARBOXYL GROUP.
FT   ACT_SITE    177    177       PROTON-RELAY.
FT   VARIANT      71     71       D -> N (IN STRAINS EC47, EC49 AND EC50).
FT   VARIANT     106    106       A -> S (IN STRAIN ECOR27).
FT   VARIANT     218    218       A -> R (IN STRAINS A8190, E2666-74,
FT                                E830587, E851819, E3406, EC10, EC14,
FT                                EC32, EC35, EC38, EC40, EC44, EC46, EC47,
FT                                EC49, EC50, EC52, EC58, E64 AND EC70).
FT   VARIANT     232    232       A -> T (IN STRAIN ECOR37).
FT   VARIANT     289    289       Q -> K (IN STRAINS EC35, EC38, EC40,
FT                                EC44, EC46 AND EC47).
FT   VARIANT     290    290       N -> S (IN STRAINS E2666-74, ECOR27 AND
FT                                ECOR45).
FT   VARIANT     291    291       A -> S (IN STRAIN EC35).
FT   VARIANT     294    294       G -> A (IN STRAIN ECOR45).
FT   VARIANT     297    297       D -> N (IN STRAIN E830587).
FT   CONFLICT     37     37       P -> S (IN REF. 4).
FT   CONFLICT     70     70       A -> R (IN REF. 2).
FT   CONFLICT     80     80       A -> R (IN REF. 1 AND 2).
FT   CONFLICT    116    116       I -> N (IN REF. 2).
FT   CONFLICT    144    144       F -> L (IN REF. 1).
FT   CONFLICT    305    312       LGEEFVNK -> WAKSSLISN (IN REF. 2).
FT   CONFLICT    307    307       E -> Q (IN REF. 1).
FT   STRAND        2      6
FT   TURN          7      9
FT   HELIX        11     23
FT   TURN         26     27
FT   STRAND       28     33
FT   TURN         37     38
FT   HELIX        39     47
FT   TURN         48     48
FT   STRAND       53     58
FT   HELIX        64     67
FT   TURN         68     69
FT   STRAND       72     75
FT   TURN         83     84
FT   HELIX        87    108
FT   TURN        110    111
FT   STRAND      113    116
FT   HELIX       121    134
FT   TURN        135    136
FT   TURN        140    141
FT   STRAND      143    145
FT   HELIX       148    162
FT   TURN        163    163
FT   HELIX       166    168
FT   STRAND      173    175
FT   TURN        179    181
FT   STRAND      182    184
FT   HELIX       186    188
FT   TURN        190    191
FT   HELIX       196    217
FT   TURN        218    219
FT   HELIX       225    242
FT   TURN        243    244
FT   STRAND      248    255
FT   STRAND      263    271
FT   TURN        272    273
FT   STRAND      274    278
FT   HELIX       286    311
SQ   SEQUENCE   312 AA;  32337 MW;  17741A3B5AD068BA CRC64;
     MKVAVLGAAG GIGQALALLL KTQLPSGSEL SLYDIAPVTP GVAVDLSHIP TAVKIKGFSG
     EDATPALEGA DVVLISAGVA RKPGMDRSDL FNVNAGIVKN LVQQVAKTCP KACIGIITNP
     VNTTVAIAAE VLKKAGVYDK NKLFGVTTLD IIRSNTFVAE LKGKQPGEVE VPVIGGHSGV
     TILPLLSQVP GVSFTEQEVA DLTKRIQNAG TEVVEAKAGG GSATLSMGQA AARFGLSLVR
     ALQGEQGVVE CAYVEGDGQY ARFFSQPLLL GKNGVEERKS IGTLSAFEQN ALEGMLDTLK
     KDIALGEEFV NK
//