ID A0A177Y1N1_9VIBR Unreviewed; 310 AA. AC A0A177Y1N1; DT 07-SEP-2016, integrated into UniProtKB/TrEMBL. DT 07-SEP-2016, sequence version 1. DT 22-FEB-2023, entry version 40. DE RecName: Full=Malate dehydrogenase {ECO:0000256|ARBA:ARBA00020382, ECO:0000256|HAMAP-Rule:MF_01516}; DE EC=1.1.1.37 {ECO:0000256|ARBA:ARBA00012995, ECO:0000256|HAMAP-Rule:MF_01516}; 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; LLEI02000026; OAJ94395.1; -; Genomic_DNA. DR RefSeq; WP_049844370.1; NZ_LLEI02000026.1. DR AlphaFoldDB; A0A177Y1N1; -. DR EnsemblBacteria; OAJ94395; OAJ94395; APB76_10005. DR Proteomes; UP000078406; Unassembled WGS sequence. DR GO; GO:0030060; F:L-malate dehydrogenase activity; IEA:UniProtKB-UniRule. 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; Lactate dehydrogenase/glycoside hydrolase, family 4, C-terminal; 1. DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 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; MALATE AND LACTATE DEHYDROGENASE; 1. DR PANTHER; PTHR11540:SF16; MALATE DEHYDROGENASE, MITOCHONDRIAL; 1. DR Pfam; PF02866; Ldh_1_C; 1. DR Pfam; PF00056; Ldh_1_N; 1. DR PIRSF; PIRSF000102; Lac_mal_DH; 1. DR SUPFAM; SSF56327; LDH C-terminal domain-like; 1. DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 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}. FT DOMAIN 1..145 FT /note="Lactate/malate dehydrogenase N-terminal" FT /evidence="ECO:0000259|Pfam:PF00056" FT DOMAIN 147..309 FT /note="Lactate/malate dehydrogenase C-terminal" FT /evidence="ECO:0000259|Pfam:PF02866" FT ACT_SITE 177 FT /note="Proton acceptor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01516, FT ECO:0000256|PIRSR:PIRSR000102-1" FT BINDING 7..13 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01516" FT BINDING 34 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01516" FT BINDING 81 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01516" FT BINDING 87 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01516, FT ECO:0000256|PIRSR:PIRSR000102-2" FT BINDING 94 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01516" FT BINDING 117..119 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01516" FT BINDING 119 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01516, FT ECO:0000256|PIRSR:PIRSR000102-2" FT BINDING 153 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01516, FT ECO:0000256|PIRSR:PIRSR000102-2" FT BINDING 227 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" 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 //