ID W1N509_9GAMM Unreviewed; 358 AA.
AC W1N509;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 24-JAN-2024, entry version 32.
DE RecName: Full=D-malate dehydrogenase (decarboxylating) {ECO:0000256|ARBA:ARBA00013126};
DE EC=1.1.1.83 {ECO:0000256|ARBA:ARBA00013126};
GN ORFNames=BJB45_02490 {ECO:0000313|EMBL:ERL50015.1};
OS Halomonas huangheensis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Halomonadaceae; Halomonas.
OX NCBI_TaxID=1178482 {ECO:0000313|EMBL:ERL50015.1, ECO:0000313|Proteomes:UP000019113};
RN [1] {ECO:0000313|EMBL:ERL50015.1, ECO:0000313|Proteomes:UP000019113}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BJGMM-B45 {ECO:0000313|EMBL:ERL50015.1,
RC ECO:0000313|Proteomes:UP000019113};
RA Miao C., Wan Y., Jin W.;
RT "draft genome of Halomonas huanghegensis, strain BJGMM-B45T.";
RL Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-malate + NAD(+) = CO2 + NADH + pyruvate;
CC Xref=Rhea:RHEA:18365, ChEBI:CHEBI:15361, ChEBI:CHEBI:15588,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.83;
CC Evidence={ECO:0000256|ARBA:ARBA00001361};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|ARBA:ARBA00001936};
CC -!- SIMILARITY: Belongs to the isocitrate and isopropylmalate
CC dehydrogenases family. {ECO:0000256|ARBA:ARBA00007769}.
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:ERL50015.1}.
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DR EMBL; AVBC01000039; ERL50015.1; -; Genomic_DNA.
DR RefSeq; WP_021820063.1; NZ_CP013106.1.
DR AlphaFoldDB; W1N509; -.
DR STRING; 1178482.AR456_03985; -.
DR KEGG; hhu:AR456_03985; -.
DR PATRIC; fig|1178482.3.peg.3106; -.
DR eggNOG; COG0473; Bacteria.
DR OrthoDB; 9806254at2; -.
DR Proteomes; UP000019113; Unassembled WGS sequence.
DR GO; GO:0046553; F:D-malate dehydrogenase (decarboxylating) activity; IEA:UniProtKB-EC.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR Gene3D; 3.40.718.10; Isopropylmalate Dehydrogenase; 1.
DR InterPro; IPR019818; IsoCit/isopropylmalate_DH_CS.
DR InterPro; IPR024084; IsoPropMal-DH-like_dom.
DR InterPro; IPR011829; TTC_DH.
DR NCBIfam; TIGR02089; TTC; 1.
DR PANTHER; PTHR43275; D-MALATE DEHYDROGENASE [DECARBOXYLATING]; 1.
DR PANTHER; PTHR43275:SF1; D-MALATE DEHYDROGENASE [DECARBOXYLATING]; 1.
DR Pfam; PF00180; Iso_dh; 1.
DR SMART; SM01329; Iso_dh; 1.
DR SUPFAM; SSF53659; Isocitrate/Isopropylmalate dehydrogenase-like; 1.
DR PROSITE; PS00470; IDH_IMDH; 1.
PE 3: Inferred from homology;
KW Manganese {ECO:0000256|ARBA:ARBA00023211};
KW Reference proteome {ECO:0000313|Proteomes:UP000019113}.
FT DOMAIN 4..351
FT /note="Isopropylmalate dehydrogenase-like"
FT /evidence="ECO:0000259|SMART:SM01329"
SQ SEQUENCE 358 AA; 39414 MW; 5D2BFC103355426D CRC64;
MTYRIAVLAG DGIGTEVMPE GVRALEATAR RFNIDIELTH FDFACCDYYL EHGKMLPDDW
HQTLIEFDAI YYGAIGWPEK VPDHISLWGS LLKFRREFDQ YVNLRPCRLL PGIKSPLANR
VPGDIDFYVV RENTEGEYSS VGGTMFEGTE REVVIQETVM TRHGVDRVLK YAFELAQQRP
RQKLTSATKS NGIAITMPWW DKRVAEMSEQ YPEVSVDKFH IDILTANFVM HPDWFDVVVA
SNLFGDILSD LGPACTGTIG VAPSANINPE GKFPSLFEPV HGSAPDIAGK GIANPIGQIW
SGAMMLEHLG HKDAGDAILA AIEAVLEEAD SNVVTPDVGG TGTTASLGQA ISERIEKG
//
