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Database: UniProt
Entry: A0A1L6I2Y6_9BURK
LinkDB: A0A1L6I2Y6_9BURK
Original site: A0A1L6I2Y6_9BURK 
ID   A0A1L6I2Y6_9BURK        Unreviewed;       372 AA.
AC   A0A1L6I2Y6;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   24-JAN-2024, entry version 18.
DE   RecName: Full=D-malate dehydrogenase (decarboxylating) {ECO:0000256|ARBA:ARBA00013126};
DE            EC=1.1.1.83 {ECO:0000256|ARBA:ARBA00013126};
GN   ORFNames=BTO02_10160 {ECO:0000313|EMBL:APR37580.1};
OS   Paraburkholderia sp. SOS3.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Paraburkholderia.
OX   NCBI_TaxID=1926494 {ECO:0000313|EMBL:APR37580.1, ECO:0000313|Proteomes:UP000184708};
RN   [1] {ECO:0000313|EMBL:APR37580.1, ECO:0000313|Proteomes:UP000184708}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SOS3 {ECO:0000313|EMBL:APR37580.1,
RC   ECO:0000313|Proteomes:UP000184708};
RA   Song W.-J., Kurnit D.M.;
RL   Submitted (DEC-2016) 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}.
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DR   EMBL; CP018811; APR37580.1; -; Genomic_DNA.
DR   RefSeq; WP_075158754.1; NZ_CP018811.1.
DR   AlphaFoldDB; A0A1L6I2Y6; -.
DR   STRING; 1926494.BTO02_10160; -.
DR   KEGG; para:BTO02_10160; -.
DR   OrthoDB; 5289857at2; -.
DR   Proteomes; UP000184708; Chromosome 1.
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          6..354
FT                   /note="Isopropylmalate dehydrogenase-like"
FT                   /evidence="ECO:0000259|SMART:SM01329"
SQ   SEQUENCE   372 AA;  40893 MW;  AA890D3BEAA111C1 CRC64;
     MTRSYRIAVI PGDGIGVEVM PEGLRVLDAA CQRFGIEIHY RHIEWASCDY YAQHGQMMPD
     DWKAQLEGCD AILFGAVGWP DKVPDHVSLW GSLLKFRREF DQYINLRPAR LFDGVPSPLA
     GRKPGDIDFM IVRENTEGEY SSVGGTMYEG TEREIVMQQA IFSRRGTERA LKFAFDLAAR
     RQKKITVATK SNGISISMPW WDARAAEMAA HYPDVVWDKQ HIDILCARFV LNPDRFDVVV
     ASNLFGDILS DLGPACTGTI GIAPSGNLNP ERRFPSLFEP VHGSAPDIAG KGIANPVAMI
     WSAAMMLDFL GNGEGAERVA HDAMLEAIVQ VLKEGPHTGD LGGKASTREV GMAVAAQLAK
     RAGAADIDRY RD
//
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