ID I5CL45_9BURK Unreviewed; 360 AA.
AC I5CL45;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=D-malate dehydrogenase (decarboxylating) {ECO:0000256|ARBA:ARBA00013126};
DE EC=1.1.1.83 {ECO:0000256|ARBA:ARBA00013126};
GN ORFNames=WQE_33166 {ECO:0000313|EMBL:EIM96613.1};
OS Paraburkholderia hospita BS001.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Paraburkholderia.
OX NCBI_TaxID=1171375 {ECO:0000313|EMBL:EIM96613.1};
RN [1] {ECO:0000313|EMBL:EIM96613.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BS001 {ECO:0000313|EMBL:EIM96613.1};
RX PubMed=22843604; DOI=10.1128/JB.00725-12;
RA Nazir R., Hansen M.A., Sorensen S., van Elsas J.D.;
RT "Draft Genome Sequence of the Soil Bacterium Burkholderia terrae Strain
RT BS001, Which Interacts with Fungal Surface Structures.";
RL J. Bacteriol. 194:4480-4481(2012).
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:EIM96613.1}.
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DR EMBL; AKAU01000188; EIM96613.1; -; Genomic_DNA.
DR AlphaFoldDB; I5CL45; -.
DR PATRIC; fig|1171375.3.peg.6868; -.
DR Proteomes; UP000004980; 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..349
FT /note="Isopropylmalate dehydrogenase-like"
FT /evidence="ECO:0000259|SMART:SM01329"
SQ SEQUENCE 360 AA; 39193 MW; DD4D9CB67FDC724B CRC64;
MNTYRIATIP GDGIGKEVVP AGKEVLEALA RTSNSFKFEF ENFDWGADYY REHGVMMPAD
GLDAIRNKDA ILFGSAGDPD VPDHVTLWGL RLKICQGFDQ YANVRPTRIL PGIDAPLKRC
TPEDLNWVIV RENSEGEYSG VGGRVHQGHP IEAATDVSIM TRAGVERIMR FAFRLAQSRP
RKLLTVITKS NAQRHAMVMW DEIALQISKE FPDVKWDKEL VDASTARMIN RPASLDTIVA
TNLHADILSD LAAALAGSLG IAPTGNIDPE RRYPSMFEPI HGSAFDIMGK GLANPIGTFW
SVVMLLEHLG EFEAAKRVMS AVETVTADPS LHTGDLGGKA TTAQVTAAVC ALVEKVPVAA
//
