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Database: UniProt
Entry: A0A0W8J8K2_9VIBR
LinkDB: A0A0W8J8K2_9VIBR
Original site: A0A0W8J8K2_9VIBR 
ID   A0A0W8J8K2_9VIBR        Unreviewed;       311 AA.
AC   A0A0W8J8K2;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   24-JAN-2024, entry version 44.
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=VRK_42610 {ECO:0000313|EMBL:KUI96566.1};
OS   Vibrio sp. MEBiC08052.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=1761910 {ECO:0000313|EMBL:KUI96566.1, ECO:0000313|Proteomes:UP000054473};
RN   [1] {ECO:0000313|EMBL:KUI96566.1, ECO:0000313|Proteomes:UP000054473}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MEBiC08052 {ECO:0000313|EMBL:KUI96566.1,
RC   ECO:0000313|Proteomes:UP000054473};
RA   Kim Y.J., Lee J.-H., Kwon K.K.;
RT   "Genome sequence of Vibrio sp. MEBiC08052.";
RL   Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
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:KUI96566.1}.
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DR   EMBL; LQIY01000043; KUI96566.1; -; Genomic_DNA.
DR   RefSeq; WP_059123288.1; NZ_KQ947477.1.
DR   AlphaFoldDB; A0A0W8J8K2; -.
DR   STRING; 1761910.VRK_42610; -.
DR   PATRIC; fig|1761910.3.peg.4312; -.
DR   OrthoDB; 9802969at2; -.
DR   Proteomes; UP000054473; 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   NCBIfam; TIGR01772; MDH_euk_gproteo; 1.
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   PROSITE; PS00068; MDH; 1.
PE   3: Inferred from homology;
KW   NAD {ECO:0000256|HAMAP-Rule:MF_01516, ECO:0000256|PIRSR:PIRSR000102-3};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW   Rule:MF_01516};
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                   ECO:0000256|PIRSR:PIRSR000102-3"
FT   BINDING         34
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01516,
FT                   ECO:0000256|PIRSR:PIRSR000102-3"
FT   BINDING         81
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01516,
FT                   ECO:0000256|PIRSR:PIRSR000102-2"
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                   ECO:0000256|PIRSR:PIRSR000102-3"
FT   BINDING         117..119
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01516,
FT                   ECO:0000256|PIRSR:PIRSR000102-3"
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,
FT                   ECO:0000256|PIRSR:PIRSR000102-3"
SQ   SEQUENCE   311 AA;  32155 MW;  C5DA2F4DDCDF259B CRC64;
     MKVAVIGAAG GIGQALALLL KNHLPAGSDL ALYDIAPVTP GVAKDLSHIP TPVSINGYSG
     EDPTPALEGA DVVLISAGVA RKPGMDRSDL FNVNAGIVKS LAEKIAVVCP EACIGIITNP
     VNTTVPIAAE VLKKAGVYNK RKLFGITTLD VIRSETFVSE LKGKNPLDVN VPVIGGHSGV
     TILPLLSQVK DVTFSDEEVA ALTHRIQNAG TEVVEAKAGG GSATLSMGQA ACRFGLSLVK
     ALQGEANVIE CAYIESDGGL APFFAQPVRL GKDGIEEVLS YGELNSFEQK ALEGMLDTLN
     GDIQLGVDFA S
//
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