ID   MDH_VIBMI               Reviewed;         222 AA.
AC   Q9L8F6; Q99PX6; Q9AIU1;
DT   07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 90.
DE   RecName: Full=Malate dehydrogenase;
DE            EC=1.1.1.37;
DE   Flags: Fragment;
GN   Name=mdh;
OS   Vibrio mimicus.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=674;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=PT5;
RX   PubMed=10678967; DOI=10.1128/iai.68.3.1507-1513.2000;
RA   Boyd E.F., Moyer K.E., Shi L., Waldor M.K.;
RT   "Infectious CTXPhi and the Vibrio pathogenicity island prophage in Vibrio
RT   mimicus: evidence for recent horizontal transfer between V. mimicus and V.
RT   cholerae.";
RL   Infect. Immun. 68:1507-1513(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 19-222.
RC   STRAIN=523-80, PT48, and PT5;
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).
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         Evidence={ECO:0000255|PROSITE-ProRule:PRU10004};
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the LDH/MDH superfamily. MDH type 1 family.
CC       {ECO:0000305}.
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DR   EMBL; AF207856; AAF40141.1; -; Genomic_DNA.
DR   EMBL; AF238335; AAK15060.1; -; Genomic_DNA.
DR   EMBL; AF238336; AAK15061.1; -; Genomic_DNA.
DR   EMBL; AF238337; AAK15062.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9L8F6; -.
DR   SMR; Q9L8F6; -.
DR   STRING; 674.VM_13250; -.
DR   eggNOG; COG0039; Bacteria.
DR   GO; GO:0030060; F:L-malate dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006108; P:malate metabolic process; IEA:InterPro.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-KW.
DR   Gene3D; 3.90.110.10; -; 1.
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; IPR036291; NAD(P)-bd_dom_sf.
DR   Pfam; PF02866; Ldh_1_C; 1.
DR   Pfam; PF00056; Ldh_1_N; 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; Tricarboxylic acid cycle.
FT   CHAIN           <1..>222
FT                   /note="Malate dehydrogenase"
FT                   /id="PRO_0000113331"
FT   ACT_SITE        170
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         1..6
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         27
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         74
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10004"
FT   BINDING         80
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10004"
FT   BINDING         87
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         110..112
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         112
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10004"
FT   BINDING         146
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10004"
FT   BINDING         220
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   VARIANT         194
FT                   /note="A -> V (in strain: 523-80)"
FT   CONFLICT        211
FT                   /note="A -> R (in Ref. 2; AAK15060/AAK15061/AAK15062)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        218
FT                   /note="F -> L (in Ref. 2; AAK15060/AAK15061/AAK15062)"
FT                   /evidence="ECO:0000305"
FT   NON_TER         1
FT   NON_TER         222
SQ   SEQUENCE   222 AA;  22601 MW;  593BDCAFBEAE464A CRC64;
     AAGGIGQALA LLLKNRLPAG SDLALYDIAP VTPGVAADLS HIPTPVTIKG YAGEDPTPAL
     EGADVVLVSA GVARKPGMDR ADLFNVNAGI VKALAETIAV VCPKACVGII TNPVNTTVPI
     AAEVLKKAGV YDKRKLFGVT TLDVIRSETF VAALKDKDPG QVRVPVIGGH SGVTILPLLS
     QVEGVTFTDE EVAALTKRIQ NAGTEVVEAK AGGGSATFSM GQ