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Database: UniProt
Entry: W8QEP4_9PSED
LinkDB: W8QEP4_9PSED
Original site: W8QEP4_9PSED 
ID   W8QEP4_9PSED            Unreviewed;       359 AA.
AC   W8QEP4;
DT   14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT   14-MAY-2014, sequence version 1.
DT   24-JAN-2024, entry version 29.
DE   RecName: Full=D-malate dehydrogenase (decarboxylating) {ECO:0000256|ARBA:ARBA00013126};
DE            EC=1.1.1.83 {ECO:0000256|ARBA:ARBA00013126};
GN   ORFNames=CD58_18165 {ECO:0000313|EMBL:AHL34705.1};
OS   Pseudomonas brassicacearum.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=930166 {ECO:0000313|EMBL:AHL34705.1, ECO:0000313|Proteomes:UP000019521};
RN   [1] {ECO:0000313|EMBL:AHL34705.1, ECO:0000313|Proteomes:UP000019521}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DF41 {ECO:0000313|EMBL:AHL34705.1,
RC   ECO:0000313|Proteomes:UP000019521};
RX   PubMed=24812222;
RA   Loewen P.C., Switala J., Fernando W.G., de Kievit T.;
RT   "Genome Sequence of Pseudomonas brassicacearum DF41.";
RL   Genome Announc. 2:e00390-14(2014).
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}.
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DR   EMBL; CP007410; AHL34705.1; -; Genomic_DNA.
DR   RefSeq; WP_025214295.1; NZ_CP007410.1.
DR   AlphaFoldDB; W8QEP4; -.
DR   KEGG; pbc:CD58_18165; -.
DR   PATRIC; fig|930166.5.peg.3539; -.
DR   eggNOG; COG0473; Bacteria.
DR   OrthoDB; 9767905at2; -.
DR   Proteomes; UP000019521; Chromosome.
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}.
FT   DOMAIN          7..355
FT                   /note="Isopropylmalate dehydrogenase-like"
FT                   /evidence="ECO:0000259|SMART:SM01329"
SQ   SEQUENCE   359 AA;  39315 MW;  8309B5342E747A5A CRC64;
     MSRTQYKIAV IPGDGIGKEV MPEGVRVLDA VAARFNLELQ WDWFDFASAD YYLAHGKMMP
     DDWFDTLKGY DAIYFGAVGW PDVVPDHISL WDSLLQFRRE FDQYVNLRPC RLMPGVKAPL
     ANRKPGDIDF WVVRENTEGE YSSVGGKMFP GTDREIVLQE TVMTRVGVDR ILKFAYDLAQ
     SRPKKHLTSA TKSNGIAITM PYWDERVAEM GNKYPDVNVD KYHIDILTAN FVLHPDWFDV
     VVASNLFGDI LSDLGPACTG TIGIAPSANI NPERNFPSLF EPVHGSAPDI AGKGIANPIG
     QIWCGAMMLE HLGHPEAGAA VLTAIESVLA MGPENAPLTA DIGGTGNTES LGKAIAAAV
//
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