ID A0A3E0U1F0_9GAMM Unreviewed; 311 AA.
AC A0A3E0U1F0;
DT 16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT 16-JAN-2019, sequence version 1.
DT 27-MAR-2024, entry version 20.
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=DXX94_08625 {ECO:0000313|EMBL:REL30776.1};
OS Thalassotalea euphylliae.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Colwelliaceae; Thalassotalea.
OX NCBI_TaxID=1655234 {ECO:0000313|EMBL:REL30776.1, ECO:0000313|Proteomes:UP000256899};
RN [1] {ECO:0000313|Proteomes:UP000256899}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H3 {ECO:0000313|Proteomes:UP000256899};
RA Summers S., Rice S.A., Freckelton M.L., Nedved B.T., Hadfield M.G.;
RT "Thalassotalea euphylliae genome.";
RL Submitted (AUG-2018) 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:REL30776.1}.
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DR EMBL; QUOT01000001; REL30776.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3E0U1F0; -.
DR Proteomes; UP000256899; 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|HAMAP-Rule:MF_01516,
KW ECO:0000256|RuleBase:RU003369};
KW Reference proteome {ECO:0000313|Proteomes:UP000256899};
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..308
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; 32039 MW; A4B930D5F4A60614 CRC64;
MKVAVLGAAG GIGQALSLLL KTQLPAGSDL ALYDVAPVVP GVAVDLSHIP TAVNVKGYGA
DDLAPALAGA DIVIIPAGMP RKPGMDRADL FNVNAGIVKT LAEGIVANCP KALVGVITNP
VNGTVPIVAE VFKKAGTYEA GRVFGVTTLD VIRSEAFIAE LKGVDVATVK VPVIGGHSGT
TILPLLSQVE GVEFTEEEVA SLTPRIQNAG TEVVNAKAGG GSATLSMGAA AARFTMSLIK
GLQGEEVVDY AYVAVEDGDA EYFAHPVRLG KNGVEEILSY GELSAFEQKA KEDMLETLNK
DIKEGIDFIN G
//
