ID U2FS12_9BURK Unreviewed; 361 AA.
AC U2FS12;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE RecName: Full=D-malate dehydrogenase (decarboxylating) {ECO:0000256|ARBA:ARBA00013126};
DE EC=1.1.1.83 {ECO:0000256|ARBA:ARBA00013126};
GN ORFNames=L810_4081 {ECO:0000313|EMBL:ERJ33567.1};
OS Burkholderia sp. AU4i.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia.
OX NCBI_TaxID=1335308 {ECO:0000313|EMBL:ERJ33567.1, ECO:0000313|Proteomes:UP000016616};
RN [1] {ECO:0000313|EMBL:ERJ33567.1, ECO:0000313|Proteomes:UP000016616}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AU4i {ECO:0000313|EMBL:ERJ33567.1,
RC ECO:0000313|Proteomes:UP000016616};
RA Devi U., Khatri I., Kumar N., Kumar L., Singh D., Sharma D.,
RA Subramanian S., Saini A.K.;
RT "Genome Assembly of Burkholderia vietnamiensis AU4i.";
RL Submitted (MAY-2013) 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:ERJ33567.1}.
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DR EMBL; ASSI01000252; ERJ33567.1; -; Genomic_DNA.
DR RefSeq; WP_021163712.1; NZ_ASSI01000252.1.
DR AlphaFoldDB; U2FS12; -.
DR PATRIC; fig|1335308.3.peg.8198; -.
DR Proteomes; UP000016616; 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 7..355
FT /note="Isopropylmalate dehydrogenase-like"
FT /evidence="ECO:0000259|SMART:SM01329"
SQ SEQUENCE 361 AA; 39615 MW; 0B62CB1267C7C8D0 CRC64;
MTDRTYRIAV IPGDGIGREV MPEGLRALEA VTARFGIRFD FVQIDWASCD YYAQHGKMMP
DDWKAQLSGM DAILFGAVGW PATVPDHVSL WGSLLKFRRE FDQYINLRPA RLFDGVPSPL
AGRRAGDIDF MIVRENTEGE YSSVGGTMFE GTDREIVMQQ AIFTRHGTER VLKFAFELAQ
RRAKRLTVAT KSNGIAISMP WWDARTAEMA ERYPDIAVDK QHIDILCARF VLQPDRFDVV
VASNLFGDIL SDLGPACTGT IGIAPSANLN PDRTFPSLFE PVHGSAPDIT GQYIANPVAM
IWSAALMLDF LGNGAGRERE AHDAIVAAIE DVLRTGPHTR DLGGNAGTQE VGEAIAARIA
G
//
