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MDH_VIBCH
ID   MDH_VIBCH               Reviewed;         311 AA.
AC   Q9KUT3; Q8GN36; Q8GN37; Q8GN38; Q8GN39; Q99PZ5; Q99Q77; Q99QN5; Q9AG49;
AC   Q9AG50; Q9AIU2; Q9R3N1; Q9R3N2; Q9R3N3; Q9S4R7; Q9XCZ8;
DT   01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 2.
DT   03-AUG-2022, entry version 138.
DE   RecName: Full=Malate dehydrogenase;
DE            EC=1.1.1.37;
GN   Name=mdh; OrderedLocusNames=VC_0432;
OS   Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=243277;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=M535, M536, M548, M549, M550, M551, M553, M554, M555, M556, M557,
RC   M558, M559, M560, M561, M562, M563, M645, and M793;
RX   PubMed=10024551; DOI=10.1128/iai.67.3.1116-1124.1999;
RA   Byun R., Elbourne L.D., Lan R., Reeves P.R.;
RT   "Evolutionary relationships of pathogenic clones of Vibrio cholerae by
RT   sequence analysis of four housekeeping genes.";
RL   Infect. Immun. 67:1116-1124(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX   PubMed=10952301; DOI=10.1038/35020000;
RA   Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA   Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R.,
RA   Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D.,
RA   Vamathevan J.J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.A.,
RA   Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L.,
RA   Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.;
RT   "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT   cholerae.";
RL   Nature 406:477-483(2000).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 26-248.
RC   STRAIN=151 / Serotype O37, 208 / Serotype O11,
RC   ATCC 25870 / Classical Inaba 569B / Serotype O1, CO130 / Serotype O37,
RC   V46 / Serotype O141, and V52 / Serotype O37;
RX   PubMed=10986258; DOI=10.1128/jb.182.19.5530-5538.2000;
RA   Boyd E.F., Heilpern A.J., Waldor M.K.;
RT   "Molecular analyses of a putative CTXphi precursor and evidence for
RT   independent acquisition of distinct CTXphis by toxigenic Vibrio cholerae.";
RL   J. Bacteriol. 182:5530-5538(2000).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 38-201.
RC   STRAIN=25872, 329 / Serotype O139, 653/36 / Serotype O139,
RC   BO1 / Serotype O139, BO2 / Serotype O139, BO4 / Serotype O139,
RC   CO391 / Serotype O139, CO396 / Serotype O139, CO402 / Serotype O139,
RC   CO403 / Serotype O139, CO404 / Serotype O139, CO406 / Serotype O139,
RC   CO407 / Serotype O139, CO414 / Serotype O139, CO415 / Serotype O139,
RC   CO418 / Serotype O139, CO487 / Serotype O1, MDO90 / Serotype O139,
RC   MOD084 / Serotype O139, NPO388 / Serotype O139, NPO390 / Serotype O139,
RC   NT329 / Serotype O139, NT330 / Serotype O139, NT638 / Serotype O139,
RC   NT642 / Serotype O139, NT648 / Serotype O139, SG24 / Serotype O139,
RC   SO19 / Serotype O139, SO29 / Serotype O139, SO30 / Serotype O139, and
RC   VO6 / Serotype O139;
RX   PubMed=11844759; DOI=10.1128/jb.184.5.1304-1313.2002;
RA   Farfan M., Minana-Galbis D., Fuste M.C., Loren J.G.;
RT   "Allelic diversity and population structure in Vibrio cholerae O139 Bengal
RT   based on nucleotide sequence analysis.";
RL   J. Bacteriol. 184:1304-1313(2002).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 111-310.
RC   STRAIN=GD64313 / Serotype O1, GD9512 / Serotype O139,
RC   GD98200 / Serotype O139, and GD98224 / Serotype O1;
RA   Yongyu R., Biao K., Shouyi G.;
RT   "Housekeeping genes of strains of Vibrio cholerae isolated from Guangdong
RT   province.";
RL   Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the reversible oxidation of malate to oxaloacetate.
CC       {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(S)-malate + NAD(+) = H(+) + NADH + oxaloacetate;
CC         Xref=Rhea:RHEA:21432, ChEBI:CHEBI:15378, ChEBI:CHEBI:15589,
CC         ChEBI:CHEBI:16452, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.37;
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the LDH/MDH superfamily. MDH type 1 family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAF93605.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AF117859; AAD23488.1; -; Genomic_DNA.
DR   EMBL; AF117860; AAD23489.1; -; Genomic_DNA.
DR   EMBL; AF117861; AAD23490.1; -; Genomic_DNA.
DR   EMBL; AF117862; AAD23491.1; -; Genomic_DNA.
DR   EMBL; AF117863; AAD23492.1; -; Genomic_DNA.
DR   EMBL; AF117864; AAD23493.1; -; Genomic_DNA.
DR   EMBL; AF117865; AAD23494.1; -; Genomic_DNA.
DR   EMBL; AF117866; AAD23495.1; -; Genomic_DNA.
DR   EMBL; AF117867; AAD23496.1; -; Genomic_DNA.
DR   EMBL; AF117868; AAD23497.1; -; Genomic_DNA.
DR   EMBL; AF117869; AAD23498.1; -; Genomic_DNA.
DR   EMBL; AF117870; AAD23499.1; -; Genomic_DNA.
DR   EMBL; AF117871; AAD23500.1; -; Genomic_DNA.
DR   EMBL; AF117872; AAD23501.1; -; Genomic_DNA.
DR   EMBL; AF117873; AAD23502.1; -; Genomic_DNA.
DR   EMBL; AF117874; AAD23503.1; -; Genomic_DNA.
DR   EMBL; AF117875; AAD23504.1; -; Genomic_DNA.
DR   EMBL; AF117876; AAD23505.1; -; Genomic_DNA.
DR   EMBL; AF117877; AAD23506.1; -; Genomic_DNA.
DR   EMBL; AE003852; AAF93605.1; ALT_INIT; Genomic_DNA.
DR   EMBL; AF238329; AAK15054.1; -; Genomic_DNA.
DR   EMBL; AF238330; AAK15055.1; -; Genomic_DNA.
DR   EMBL; AF238331; AAK15056.1; -; Genomic_DNA.
DR   EMBL; AF238332; AAK15057.1; -; Genomic_DNA.
DR   EMBL; AF238333; AAK15058.1; -; Genomic_DNA.
DR   EMBL; AF238334; AAK15059.1; -; Genomic_DNA.
DR   EMBL; AF343280; AAK30532.1; -; Genomic_DNA.
DR   EMBL; AF343281; AAK30533.1; -; Genomic_DNA.
DR   EMBL; AF343282; AAK30534.1; -; Genomic_DNA.
DR   EMBL; AF343283; AAK30535.1; -; Genomic_DNA.
DR   EMBL; AF343284; AAK30536.1; -; Genomic_DNA.
DR   EMBL; AF343285; AAK30537.1; -; Genomic_DNA.
DR   EMBL; AF343286; AAK30538.1; -; Genomic_DNA.
DR   EMBL; AF343287; AAK30539.1; -; Genomic_DNA.
DR   EMBL; AF343288; AAK30540.1; -; Genomic_DNA.
DR   EMBL; AF343289; AAK30541.1; -; Genomic_DNA.
DR   EMBL; AF343290; AAK30542.1; -; Genomic_DNA.
DR   EMBL; AF343291; AAK30543.1; -; Genomic_DNA.
DR   EMBL; AF343292; AAK30544.1; -; Genomic_DNA.
DR   EMBL; AF343293; AAK30545.1; -; Genomic_DNA.
DR   EMBL; AF343294; AAK30546.1; -; Genomic_DNA.
DR   EMBL; AF343295; AAK30547.1; -; Genomic_DNA.
DR   EMBL; AF343296; AAK30548.1; -; Genomic_DNA.
DR   EMBL; AF343297; AAK30549.1; -; Genomic_DNA.
DR   EMBL; AF343298; AAK30550.1; -; Genomic_DNA.
DR   EMBL; AF343299; AAK30551.1; -; Genomic_DNA.
DR   EMBL; AF343300; AAK30552.1; -; Genomic_DNA.
DR   EMBL; AF343301; AAK30553.1; -; Genomic_DNA.
DR   EMBL; AF343302; AAK30554.1; -; Genomic_DNA.
DR   EMBL; AF343303; AAK30555.1; -; Genomic_DNA.
DR   EMBL; AF343304; AAK30556.1; -; Genomic_DNA.
DR   EMBL; AF343305; AAK30557.1; -; Genomic_DNA.
DR   EMBL; AF343306; AAK30558.1; -; Genomic_DNA.
DR   EMBL; AF343307; AAK30559.1; -; Genomic_DNA.
DR   EMBL; AF343308; AAK30560.1; -; Genomic_DNA.
DR   EMBL; AF343309; AAK30561.1; -; Genomic_DNA.
DR   EMBL; AF343310; AAK30562.1; -; Genomic_DNA.
DR   EMBL; AF540657; AAN23136.1; -; Genomic_DNA.
DR   EMBL; AF540658; AAN23137.1; -; Genomic_DNA.
DR   EMBL; AF540659; AAN23138.1; -; Genomic_DNA.
DR   EMBL; AF540660; AAN23139.1; -; Genomic_DNA.
DR   PIR; G82324; G82324.
DR   RefSeq; NP_230086.2; NC_002505.1.
DR   RefSeq; WP_000861563.1; NZ_LT906614.1.
DR   AlphaFoldDB; Q9KUT3; -.
DR   SMR; Q9KUT3; -.
DR   STRING; 243277.VC_0432; -.
DR   DNASU; 2615693; -.
DR   EnsemblBacteria; AAF93605; AAF93605; VC_0432.
DR   GeneID; 57739170; -.
DR   GeneID; 66938865; -.
DR   KEGG; vch:VC_0432; -.
DR   PATRIC; fig|243277.26.peg.406; -.
DR   eggNOG; COG0039; Bacteria.
DR   HOGENOM; CLU_047181_1_0_6; -.
DR   OMA; MGWTSQA; -.
DR   Proteomes; UP000000584; Chromosome 1.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0030060; F:L-malate dehydrogenase activity; IBA:GO_Central.
DR   GO; GO:0006108; P:malate metabolic process; IEA:InterPro.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-UniRule.
DR   CDD; cd01337; MDH_glyoxysomal_mitochondrial; 1.
DR   Gene3D; 3.90.110.10; -; 1.
DR   HAMAP; MF_01516; Malate_dehydrog_1; 1.
DR   InterPro; IPR001557; L-lactate/malate_DH.
DR   InterPro; IPR022383; Lactate/malate_DH_C.
DR   InterPro; IPR001236; Lactate/malate_DH_N.
DR   InterPro; IPR015955; Lactate_DH/Glyco_Ohase_4_C.
DR   InterPro; IPR001252; Malate_DH_AS.
DR   InterPro; IPR010097; Malate_DH_type1.
DR   InterPro; IPR023958; Malate_DH_type1_bac.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   Pfam; PF02866; Ldh_1_C; 1.
DR   Pfam; PF00056; Ldh_1_N; 1.
DR   PIRSF; PIRSF000102; Lac_mal_DH; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   SUPFAM; SSF56327; SSF56327; 1.
DR   TIGRFAMs; TIGR01772; MDH_euk_gproteo; 1.
DR   PROSITE; PS00068; MDH; 1.
PE   3: Inferred from homology;
KW   NAD; Oxidoreductase; Reference proteome; Tricarboxylic acid cycle.
FT   CHAIN           1..311
FT                   /note="Malate dehydrogenase"
FT                   /id="PRO_0000113328"
FT   ACT_SITE        177
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         7..13
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         34
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         81
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         87
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         94
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         117..119
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         119
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         153
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         227
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   VARIANT         63
FT                   /note="P -> T (in strain: M551)"
FT   VARIANT         171
FT                   /note="V -> L (in strain: M553, M535, CO391, CO407 and 653/
FT                   36)"
FT   VARIANT         204
FT                   /note="K -> N (in strain: M548)"
FT   VARIANT         223
FT                   /note="A -> T (in strain: 569B)"
FT   VARIANT         277
FT                   /note="A -> E (in strain: M550, M551, M554, M557, M558 and
FT                   GD98200)"
SQ   SEQUENCE   311 AA;  32015 MW;  5AD037C0E548BE9C CRC64;
     MKVAVIGAAG GIGQALALLL KNRLPAGSDL ALYDIAPVTP GVAADLSHIP TPVTIKGYAG
     EDPTPALEGA DVVLVSAGVA RKPGMDRADL FNVNAGIVKA LAEKIAVVCP KACVGIITNP
     VNTTVPIAAE VLKKAGVYDK RKLFGVTTLD VIRSETFVAA LKDKDPGQVR VPVIGGHSGV
     TILPLLSQVE GVSFTDEEVA ALTKRIQNAG TEVVEAKAGG GSATLSMGQA ACRFGLALVK
     ALQGESDVVE YAYVEGEGEY APFFAQPIKL GKNGVEALLD IGKLSAYEQA ALDGMLDTLK
     GDIQIGVEFV K
 
 
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