ID A0A0H2M9U5_VARPD Unreviewed; 362 AA.
AC A0A0H2M9U5;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=D-malate dehydrogenase (decarboxylating) {ECO:0000256|ARBA:ARBA00013126};
DE EC=1.1.1.83 {ECO:0000256|ARBA:ARBA00013126};
GN Name=dmlA1 {ECO:0000313|EMBL:KLN57422.1};
GN ORFNames=VPARA_15020 {ECO:0000313|EMBL:KLN57422.1};
OS Variovorax paradoxus.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Variovorax.
OX NCBI_TaxID=34073 {ECO:0000313|EMBL:KLN57422.1, ECO:0000313|Proteomes:UP000035170};
RN [1] {ECO:0000313|EMBL:KLN57422.1, ECO:0000313|Proteomes:UP000035170}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TBEA6 {ECO:0000313|EMBL:KLN57422.1,
RC ECO:0000313|Proteomes:UP000035170};
RA Poehlein A., Schuldes J., Wuebbeler J.H., Hiessl S., Steinbuechel A.,
RA Daniel R.;
RT "Genome sequence of Variovorax paradoxus TBEA6.";
RL Submitted (MAR-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:KLN57422.1}.
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DR EMBL; JZWI01000007; KLN57422.1; -; Genomic_DNA.
DR RefSeq; WP_047783951.1; NZ_JZWI01000007.1.
DR AlphaFoldDB; A0A0H2M9U5; -.
DR PATRIC; fig|34073.19.peg.1532; -.
DR Proteomes; UP000035170; 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 Oxidoreductase {ECO:0000313|EMBL:KLN57422.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000035170}.
FT DOMAIN 6..355
FT /note="Isopropylmalate dehydrogenase-like"
FT /evidence="ECO:0000259|SMART:SM01329"
SQ SEQUENCE 362 AA; 39569 MW; 1EB244F6141F117D CRC64;
MTPTFRIALI AGDGIGKEVM PEGLRVVQAA AERFGFELDC RTIDWASCDY HAQHGQMMPD
DWKEQLQGVD ALYFGAVGWP ATVPDHVSLW GSLLKFRREF DQYINLRPVR LFEGVPCPLA
GRRPGDIDYV VVRENTEGEY TSLGGVMYEG TEREIVIQES VFSRHGTDRV LRYACELANS
RARKHLTVAT KSNGIAISMP WWDGRADAIG RDYPEVTVDK QHIDILSARF VLQPTRFDVV
VASNLFGDIL SDLGPATTGT IGLAPSANLN PERRFPSLFE PVHGSAPDIY GQNIANPIAM
IWSGALMLDF LTQGQGAGRA AHDAILGAIE AVLRDGPRTR DLGGTASTTE LGMAIAERVA
AA
//
