ID   A0A177Y1N1_9VIBR        Unreviewed;       310 AA.
AC   A0A177Y1N1;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   02-DEC-2020, entry version 32.
DE   RecName: Full=Malate dehydrogenase {ECO:0000256|ARBA:ARBA00020382, ECO:0000256|HAMAP-Rule:MF_01516, ECO:0000256|RuleBase:RU000422};
DE            EC=1.1.1.37 {ECO:0000256|ARBA:ARBA00012995, ECO:0000256|HAMAP-Rule:MF_01516, ECO:0000256|RuleBase:RU000422};
GN   Name=mdh {ECO:0000256|HAMAP-Rule:MF_01516};
GN   ORFNames=APB76_10005 {ECO:0000313|EMBL:OAJ94395.1};
OS   Vibrio bivalvicida.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio; Vibrio oreintalis group.
OX   NCBI_TaxID=1276888 {ECO:0000313|EMBL:OAJ94395.1, ECO:0000313|Proteomes:UP000078406};
RN   [1] {ECO:0000313|EMBL:OAJ94395.1, ECO:0000313|Proteomes:UP000078406}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=605 {ECO:0000313|EMBL:OAJ94395.1,
RC   ECO:0000313|Proteomes:UP000078406};
RX   PubMed=26654527; DOI=10.1016/j.syapm.2015.10.006;
RA   Dubert J., Romalde J.L., Prado S., Barja J.L.;
RT   "Vibrio bivalvicida sp. nov., a novel larval pathogen for bivalve molluscs
RT   reared in a hatchery.";
RL   Syst. Appl. Microbiol. 39:8-13(2016).
CC   -!- FUNCTION: Catalyzes the reversible oxidation of malate to oxaloacetate.
CC       {ECO:0000256|ARBA:ARBA00003966, ECO:0000256|HAMAP-Rule:MF_01516}.
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:0000256|ARBA:ARBA00000774, ECO:0000256|HAMAP-
CC         Rule:MF_01516, ECO:0000256|RuleBase:RU000422};
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738, ECO:0000256|HAMAP-
CC       Rule:MF_01516}.
CC   -!- SIMILARITY: Belongs to the LDH/MDH superfamily. MDH type 1 family.
CC       {ECO:0000256|ARBA:ARBA00008824, ECO:0000256|HAMAP-Rule:MF_01516}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OAJ94395.1}.
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DR   EMBL; LLEI02000026; OAJ94395.1; -; Genomic_DNA.
DR   RefSeq; WP_049844370.1; NZ_LLEI02000026.1.
DR   EnsemblBacteria; OAJ94395; OAJ94395; APB76_10005.
DR   OrthoDB; 870724at2; -.
DR   Proteomes; UP000078406; Unassembled WGS sequence.
DR   GO; GO:0030060; F:L-malate dehydrogenase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
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   PANTHER; PTHR11540:SF22; PTHR11540:SF22; 1.
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 {ECO:0000256|HAMAP-Rule:MF_01516, ECO:0000256|RuleBase:RU000422};
KW   Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_01516,
KW   ECO:0000256|RuleBase:RU003369};
KW   Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532, ECO:0000256|HAMAP-
KW   Rule:MF_01516, ECO:0000256|RuleBase:RU000422}.
FT   DOMAIN          1..145
FT                   /note="Ldh_1_N"
FT                   /evidence="ECO:0000259|Pfam:PF00056"
FT   DOMAIN          147..309
FT                   /note="Ldh_1_C"
FT                   /evidence="ECO:0000259|Pfam:PF02866"
FT   NP_BIND         7..13
FT                   /note="NAD"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01516"
FT   NP_BIND         117..119
FT                   /note="NAD"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01516"
FT   ACT_SITE        177
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01516,
FT                   ECO:0000256|PIRSR:PIRSR000102-1"
FT   BINDING         34
FT                   /note="NAD"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01516"
FT   BINDING         81
FT                   /note="Substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01516"
FT   BINDING         87
FT                   /note="Substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01516,
FT                   ECO:0000256|PIRSR:PIRSR000102-2"
FT   BINDING         94
FT                   /note="NAD"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01516"
FT   BINDING         119
FT                   /note="Substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01516,
FT                   ECO:0000256|PIRSR:PIRSR000102-2"
FT   BINDING         153
FT                   /note="Substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01516,
FT                   ECO:0000256|PIRSR:PIRSR000102-2"
FT   BINDING         227
FT                   /note="NAD"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01516"
SQ   SEQUENCE   310 AA;  32158 MW;  A225EECD194B1EEB CRC64;
     MKVAVIGAAG GIGQALALLL KNRLPAGSDL ALYDIAPVTP GVAADLSHIP TPVSIKGYAG
     EDPTPALEGA DVVLISAGVA RKPGMDRADL FNVNAGIVKS LAQRIADVCP KALVGIITNP
     VNTTVPIAAE VLKQAGVYDK RRLFGVTTLD VIRSETFVAD LKDKDPGDVR VPVIGGHSGV
     TILPLLSQVE GVEFSDEEVA ALTKRIQNAG TEVVEAKAGG GSATLSMGQA ACRFGLALVK
     ALQGEEVIEY AYVEGDGEHA PFFAQPVKLG KEGVEEVLSY GELSDFEKSA LDGMLETLNG
     DIQTGVDFVK
//