ID A0A167JEA4_9FLAO Unreviewed; 308 AA.
AC A0A167JEA4;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 32.
DE RecName: Full=Malate dehydrogenase {ECO:0000256|HAMAP-Rule:MF_00487};
DE EC=1.1.1.37 {ECO:0000256|HAMAP-Rule:MF_00487};
GN Name=mdh {ECO:0000256|HAMAP-Rule:MF_00487};
GN ORFNames=ULVI_01970 {ECO:0000313|EMBL:OAB80587.1};
OS Cochleicola gelatinilyticus.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Cochleicola.
OX NCBI_TaxID=1763537 {ECO:0000313|EMBL:OAB80587.1, ECO:0000313|Proteomes:UP000077013};
RN [1] {ECO:0000313|EMBL:OAB80587.1, ECO:0000313|Proteomes:UP000077013}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LPB0005 {ECO:0000313|EMBL:OAB80587.1,
RC ECO:0000313|Proteomes:UP000077013};
RA Shin S.-K., Yi H.;
RT "Ulvibacter sp. LPB0005, isolated from Thais luteostoma.";
RL Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the reversible oxidation of malate to oxaloacetate.
CC {ECO:0000256|HAMAP-Rule:MF_00487}.
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|HAMAP-Rule:MF_00487};
CC -!- SIMILARITY: Belongs to the LDH/MDH superfamily. MDH type 3 family.
CC {ECO:0000256|HAMAP-Rule:MF_00487}.
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:OAB80587.1}.
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DR EMBL; LRXL01000026; OAB80587.1; -; Genomic_DNA.
DR RefSeq; WP_068591300.1; NZ_LRXL01000026.1.
DR AlphaFoldDB; A0A167JEA4; -.
DR STRING; 1763537.ULVI_01970; -.
DR OrthoDB; 9802969at2; -.
DR Proteomes; UP000077013; Unassembled WGS sequence.
DR GO; GO:0030060; F:L-malate dehydrogenase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0019752; P:carboxylic acid metabolic process; IEA:InterPro.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-UniRule.
DR CDD; cd01339; LDH-like_MDH; 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_00487; Malate_dehydrog_3; 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; IPR011275; Malate_DH_type3.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR NCBIfam; TIGR01763; MalateDH_bact; 1.
DR PANTHER; PTHR43128; L-2-HYDROXYCARBOXYLATE DEHYDROGENASE (NAD(P)(+)); 1.
DR PANTHER; PTHR43128:SF16; L-LACTATE DEHYDROGENASE; 1.
DR Pfam; PF02866; Ldh_1_C; 1.
DR Pfam; PF00056; Ldh_1_N; 1.
DR PIRSF; PIRSF000102; Lac_mal_DH; 1.
DR PRINTS; PR00086; LLDHDRGNASE.
DR SUPFAM; SSF56327; LDH C-terminal domain-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|HAMAP-Rule:MF_00487};
KW Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_00487,
KW ECO:0000256|RuleBase:RU003369};
KW Reference proteome {ECO:0000313|Proteomes:UP000077013};
KW Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532, ECO:0000256|HAMAP-
KW Rule:MF_00487}.
FT DOMAIN 1..142
FT /note="Lactate/malate dehydrogenase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00056"
FT DOMAIN 147..297
FT /note="Lactate/malate dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02866"
FT ACT_SITE 175
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00487,
FT ECO:0000256|PIRSR:PIRSR000102-1"
FT BINDING 7..12
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00487,
FT ECO:0000256|PIRSR:PIRSR000102-3"
FT BINDING 32
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00487,
FT ECO:0000256|PIRSR:PIRSR000102-3"
FT BINDING 82
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00487,
FT ECO:0000256|PIRSR:PIRSR000102-2"
FT BINDING 88
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00487,
FT ECO:0000256|PIRSR:PIRSR000102-2"
FT BINDING 95
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00487,
FT ECO:0000256|PIRSR:PIRSR000102-3"
FT BINDING 118..120
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00487,
FT ECO:0000256|PIRSR:PIRSR000102-3"
FT BINDING 120
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00487,
FT ECO:0000256|PIRSR:PIRSR000102-2"
FT BINDING 151
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00487,
FT ECO:0000256|PIRSR:PIRSR000102-2"
SQ SEQUENCE 308 AA; 32583 MW; D72406046298DD9C CRC64;
MKVTVVGAGA VGASCAEYIA IKNFASEVVL VDIKEGYAEG KAMDLMQTAS LNGFDTRVVG
TTGDYTKTAD SDICVITSGI PRKPGMTREE LIGINAGIVK DVSSSLVKHS PNTIIIVVSN
PMDTMTYLVH KTTNLPKNRI IGMGGALDSA RFKYRLAEAL EAPISDVDGM VIGGHSDKGM
VPLTRLATRN SVPVTAFISE ERLNQVKEDT KVGGATLTKL LGTSAWYAPG AAVSGLVQAI
ACDQKKIFPC STFLEGEYGL NDLCIGVPVV LGKDGIEKIV ELELTDAEKD HMKESAEGVS
KTNGLLEL
//