ID W7WFC2_9BURK Unreviewed; 372 AA.
AC W7WFC2;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE RecName: Full=D-malate dehydrogenase (decarboxylating) {ECO:0000256|ARBA:ARBA00013126};
DE EC=1.1.1.83 {ECO:0000256|ARBA:ARBA00013126};
GN Name=dmlA {ECO:0000313|EMBL:EWS55480.1};
GN ORFNames=X551_01682 {ECO:0000313|EMBL:EWS55480.1};
OS Methylibium sp. T29.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Sphaerotilaceae; Methylibium.
OX NCBI_TaxID=1430884 {ECO:0000313|EMBL:EWS55480.1, ECO:0000313|Proteomes:UP000019361};
RN [1] {ECO:0000313|Proteomes:UP000019361}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=T29 {ECO:0000313|Proteomes:UP000019361};
RA Szabo Z., Gyula P., Robotka H., Bihari Z.;
RT "Genome sequencing of the MTBE-degrading Methylibium sp. T29.";
RL Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EWS55480.1, ECO:0000313|Proteomes:UP000019361}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=T29 {ECO:0000313|EMBL:EWS55480.1,
RC ECO:0000313|Proteomes:UP000019361};
RX PubMed=26221420; DOI=10.1186/s40793-015-0023-z;
RA Szabo Z., Gyula P., Robotka H., Bato E., Galik B., Pach P., Pekker P.,
RA Papp I., Bihari Z.;
RT "Draft genome sequence of Methylibium sp. strain T29, a novel fuel
RT oxygenate-degrading bacterial isolate from Hungary.";
RL Stand. Genomic Sci. 10:39-39(2015).
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:EWS55480.1}.
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DR EMBL; AZND01000042; EWS55480.1; -; Genomic_DNA.
DR RefSeq; WP_036248060.1; NZ_AZND01000042.1.
DR AlphaFoldDB; W7WFC2; -.
DR PATRIC; fig|1430884.4.peg.1698; -.
DR Proteomes; UP000019361; 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:EWS55480.1}.
FT DOMAIN 5..363
FT /note="Isopropylmalate dehydrogenase-like"
FT /evidence="ECO:0000259|SMART:SM01329"
SQ SEQUENCE 372 AA; 40901 MW; 35F74796032B5DD5 CRC64;
MKPHRIAVIP GDGIGQEVMP EGLRVLEVAA QRFELPLQFD HFDWACAAYW QRTGQMLPND
WFATLSGYDA IYFGAVGWPA VVPDHVSLWG SLLKFRREFD QYVNLRPVRL FDGVPCPLVD
RDGRPRKPGD IDFFVVRENT EGEYTHLGGR LFEGTEREIV IQESVFSRHG TDRVMKFAFE
LAQSRPRKHL TVATKSNGIA ISMPWWDERA EAMAQGYPEV TVDKQHIDIL SARFVLQPTR
FDVVVASNLF GDILSDLGPA CTGTIGLAPS ANLNPQRHFP SLFEPVHGSA PDIFGRAIAN
PVAMIWSGAL MLDFLGGAIG ADTARHLQAH DAIVAAIERV LVTGPRTPDL GGHASTTVMG
RAIAEQVAAG AP
//
