ID A0A077LJ09_9PSED Unreviewed; 350 AA.
AC A0A077LJ09;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-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=PSCI_3340 {ECO:0000313|EMBL:BAP44042.1};
OS Pseudomonas sp. StFLB209.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1028989 {ECO:0000313|EMBL:BAP44042.1, ECO:0000313|Proteomes:UP000031652};
RN [1] {ECO:0000313|EMBL:BAP44042.1, ECO:0000313|Proteomes:UP000031652}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=StFLB209 {ECO:0000313|EMBL:BAP44042.1,
RC ECO:0000313|Proteomes:UP000031652};
RX PubMed=25323715; DOI=10.1128/genomeA.01037-14;
RA Morohoshi T., Kato T., Someya N., Ikeda T.;
RT "Complete Genome Sequence of N-Acylhomoserine Lactone-Producing Pseudomonas
RT sp. Strain StFLB209, Isolated from Potato Phyllosphere.";
RL Genome Announc. 2:e01037-e01014(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; AP014637; BAP44042.1; -; Genomic_DNA.
DR RefSeq; WP_045489125.1; NZ_AP014637.1.
DR AlphaFoldDB; A0A077LJ09; -.
DR STRING; 1028989.PSCI_3340; -.
DR KEGG; pses:PSCI_3340; -.
DR HOGENOM; CLU_031953_0_1_6; -.
DR OrthoDB; 9767905at2; -.
DR Proteomes; UP000031652; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000031652}.
FT DOMAIN 5..345
FT /note="Isopropylmalate dehydrogenase-like"
FT /evidence="ECO:0000259|SMART:SM01329"
SQ SEQUENCE 350 AA; 37780 MW; 9188194B78CEC589 CRC64;
MSTYKIAAVP GDGIGVEVIA AGVEVLQALA AKSGFELKFG HFDWNSDNYL KNGFYIPEGG
LDELKTFDAI FFGAVGALNV ADHISLWGLR LPICQGFDQY ANVRPARVLP GVKSPLHNGH
EIDWVVVREN SEGEYSGNGG RVHRGLPEEV ATEVSVFTRV GVERIHRFAF ELARSRPRKH
LTLVTKSNAQ RHGMVLWDEV FFEVAKDFPD VRIDKELVDA VTTRMVLKPG TLDVIVATNL
HADILSDLAA ALSGSLGIAP TANLNPNRSF PSMFEPIHGS AFDITGKGVA NPIATFWTAA
MMLEHLGEAA AARTLMSAIE AVTESGLHTP DLGGTATTRQ VTDAVLALIK
//
