ID A0A0A0EK50_9RHOB Unreviewed; 320 AA.
AC A0A0A0EK50;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 24-JAN-2024, entry version 47.
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=ATO9_03360 {ECO:0000313|EMBL:KGM50538.1};
OS Pseudooceanicola atlanticus.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Pseudooceanicola.
OX NCBI_TaxID=1461694 {ECO:0000313|EMBL:KGM50538.1, ECO:0000313|Proteomes:UP000030004};
RN [1] {ECO:0000313|EMBL:KGM50538.1, ECO:0000313|Proteomes:UP000030004}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=22II-s11g {ECO:0000313|EMBL:KGM50538.1,
RC ECO:0000313|Proteomes:UP000030004};
RX PubMed=25663028; DOI=10.1007/s10482-015-0398-2;
RA Lai Q., Li G., Liu X., Du Y., Sun F., Shao Z.;
RT "Pseudooceanicola atlanticus gen. nov. sp. nov., isolated from surface
RT seawater of the Atlantic Ocean and reclassification of Oceanicola
RT batsensis, Oceanicola marinus, Oceanicola nitratireducens, Oceanicola
RT nanhaiensis, Oceanicola antarcticus and Oceanicola flagellatus, as
RT Pseudooceanicola batsensis comb. nov., Pseudooceanicola marinus comb. nov.,
RT Pseudooceanicola nitratireducens comb. nov., Pseudooceanicola nanhaiensis
RT comb. nov., Pseudooceanicola antarcticus comb. nov., and Pseudooceanicola
RT flagellatus comb. nov.";
RL Antonie Van Leeuwenhoek 107:1065-1074(2015).
CC -!- FUNCTION: Catalyzes the reversible oxidation of malate to oxaloacetate.
CC {ECO:0000256|ARBA:ARBA00003966, 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:KGM50538.1}.
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DR EMBL; AQQX01000001; KGM50538.1; -; Genomic_DNA.
DR RefSeq; WP_043744933.1; NZ_CP051248.1.
DR AlphaFoldDB; A0A0A0EK50; -.
DR STRING; 1461694.ATO9_03360; -.
DR eggNOG; COG0039; Bacteria.
DR OrthoDB; 9802969at2; -.
DR Proteomes; UP000030004; 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.
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:UP000030004};
KW Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532, ECO:0000256|HAMAP-
KW Rule:MF_00487}.
FT DOMAIN 5..143
FT /note="Lactate/malate dehydrogenase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00056"
FT DOMAIN 148..307
FT /note="Lactate/malate dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02866"
FT ACT_SITE 176
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00487,
FT ECO:0000256|PIRSR:PIRSR000102-1"
FT BINDING 10..15
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 34
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 83
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00487,
FT ECO:0000256|PIRSR:PIRSR000102-2"
FT BINDING 89
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00487,
FT ECO:0000256|PIRSR:PIRSR000102-2"
FT BINDING 96
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 119..121
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 121
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00487,
FT ECO:0000256|PIRSR:PIRSR000102-2"
FT BINDING 152
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00487,
FT ECO:0000256|PIRSR:PIRSR000102-2"
SQ SEQUENCE 320 AA; 33520 MW; DD355AC8101D63BC CRC64;
MARPKIALIG AGQIGGTLAH LVALKELGDV VLFDIAEGTP EGKALDIAES GPSEGFDATL
KGTQDYADIA GADVCIVTAG VPRKPGMSRD DLLGINLKVM KAVGEGIKAN APDAFVICIT
NPLDAMVWAL QKFSGLPTNK VCGMAGVLDS ARFRHFLSVE FGVSMKDVSG FVLGGHGDTM
VPSVRYSTVA GIPLPDLVKM GWTTQEKLDA IVQRTRDGGA EIVGLLKTGS AFYAPATSAI
EMAEAYLKDQ KRVLPCAAYC DGEIGVKDMY VGVPTVIGAG GIEKVVNIKL NKEEQEMFDK
SVDAVKGLVE ACKGIDDSLA
//