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Database: UniProt
Entry: D0FF33_9VIBR
LinkDB: D0FF33_9VIBR
Original site: D0FF33_9VIBR 
ID   D0FF33_9VIBR            Unreviewed;       141 AA.
AC   D0FF33;
DT   24-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   24-NOV-2009, sequence version 1.
DT   24-JAN-2024, entry version 59.
DE   RecName: Full=Malate dehydrogenase {ECO:0000256|ARBA:ARBA00020382, ECO:0000256|RuleBase:RU000422};
DE            EC=1.1.1.37 {ECO:0000256|ARBA:ARBA00012995, ECO:0000256|RuleBase:RU000422};
DE   Flags: Fragment;
GN   Name=mdh {ECO:0000313|EMBL:ACX60916.1};
OS   Vibrio sp. 9CS101.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=677631 {ECO:0000313|EMBL:ACX60916.1};
RN   [1] {ECO:0000313|EMBL:ACX60916.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=9CS101 {ECO:0000313|EMBL:ACX60916.1};
RX   PubMed=20819104; DOI=10.1111/j.1462-2920.2010.02328.x;
RA   Preheim S.P., Boucher Y., Wildschutte H., David L.A., Veneziano D.,
RA   Alm E.J., Polz M.F.;
RT   "Metapopulation structure of Vibrionaceae among coastal marine
RT   invertebrates.";
RL   Environ. Microbiol. 13:265-275(2011).
CC   -!- FUNCTION: Catalyzes the reversible oxidation of malate to oxaloacetate.
CC       {ECO:0000256|ARBA:ARBA00003966}.
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|RuleBase:RU000422};
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC   -!- SIMILARITY: Belongs to the LDH/MDH superfamily. MDH type 1 family.
CC       {ECO:0000256|ARBA:ARBA00008824}.
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DR   EMBL; GQ993417; ACX60916.1; -; Genomic_DNA.
DR   AlphaFoldDB; D0FF33; -.
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; Lactate dehydrogenase/glycoside hydrolase, family 4, C-terminal; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 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; 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   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|RuleBase:RU000422};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU003369};
KW   Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532,
KW   ECO:0000256|RuleBase:RU000422}.
FT   DOMAIN          3..94
FT                   /note="Lactate/malate dehydrogenase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00056"
FT   DOMAIN          96..139
FT                   /note="Lactate/malate dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02866"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:ACX60916.1"
FT   NON_TER         141
FT                   /evidence="ECO:0000313|EMBL:ACX60916.1"
SQ   SEQUENCE   141 AA;  14646 MW;  61A759F05450C501 CRC64;
     PVSIKGYAGE DPTPALEGAD VVLISAGVAR KPGMDRADLF NVNAGIVKSL AEKIAVTCPT
     ACVGIITNPV NTTVPIAAEV LKKAGVYDKR RLFGITTLDV IRSETFVAEL KDKDPGDVRV
     PVIGGHSGVT ILPLLSQVEG V
//
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