ID A0A0Q8AZ80_9PSED Unreviewed; 351 AA.
AC A0A0Q8AZ80;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, 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=ASD60_26620 {ECO:0000313|EMBL:KQZ87826.1};
OS Pseudomonas sp. Root562.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1736561 {ECO:0000313|EMBL:KQZ87826.1, ECO:0000313|Proteomes:UP000051426};
RN [1] {ECO:0000313|EMBL:KQZ87826.1, ECO:0000313|Proteomes:UP000051426}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root562 {ECO:0000313|EMBL:KQZ87826.1,
RC ECO:0000313|Proteomes:UP000051426};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQZ87826.1, ECO:0000313|Proteomes:UP000051426}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root562 {ECO:0000313|EMBL:KQZ87826.1,
RC ECO:0000313|Proteomes:UP000051426};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) 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:KQZ87826.1}.
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DR EMBL; LMGK01000010; KQZ87826.1; -; Genomic_DNA.
DR RefSeq; WP_056853775.1; NZ_LMGK01000010.1.
DR AlphaFoldDB; A0A0Q8AZ80; -.
DR OrthoDB; 9767905at2; -.
DR Proteomes; UP000051426; 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}.
FT DOMAIN 5..345
FT /note="Isopropylmalate dehydrogenase-like"
FT /evidence="ECO:0000259|SMART:SM01329"
SQ SEQUENCE 351 AA; 38113 MW; EE4C23AE4AC4F805 CRC64;
MSAYKIAAVP GDGIGVEVIA AGVEVLQALS KKTGFELDFK HFDWNSDNYL KNGYYIPEGG
LEELKTFDAI FFGAVGALNV PDHISLWGLR LPICQGFDQY ANVRPARVLP GVKSPLHNGD
QIDWVVVREN SEGEYSGNGG RVHRGLPEEV ATEVSVFTRA GVERIHRFAF ELAQSRPRKH
LTMVTKSNAQ RHGMVLWDEI FYEVAKDFPD VKIDKELVDA VTTRMVLKPS TLDVIVATNL
HADILSDLAA ALSGSLGIAP TANLNPSRKF PSMFEPIHGS AFDITGKGVA NPIATFWTAA
MMLEHLGEAA AAKHLMSAIE AVTESGLHTP DLGGNATTRQ ITDAVLALIN R
//
