ID B2TAT0_PARPJ Unreviewed; 360 AA.
AC B2TAT0;
DT 01-JUL-2008, integrated into UniProtKB/TrEMBL.
DT 01-JUL-2008, sequence version 1.
DT 27-MAR-2024, entry version 79.
DE RecName: Full=D-malate dehydrogenase (decarboxylating) {ECO:0000256|ARBA:ARBA00013126};
DE EC=1.1.1.83 {ECO:0000256|ARBA:ARBA00013126};
GN OrderedLocusNames=Bphyt_6098 {ECO:0000313|EMBL:ACD20430.1};
OS Paraburkholderia phytofirmans (strain DSM 17436 / LMG 22146 / PsJN)
OS (Burkholderia phytofirmans).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Paraburkholderia.
OX NCBI_TaxID=398527 {ECO:0000313|EMBL:ACD20430.1, ECO:0000313|Proteomes:UP000001739};
RN [1] {ECO:0000313|EMBL:ACD20430.1, ECO:0000313|Proteomes:UP000001739}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17436 / LMG 22146 / PsJN
RC {ECO:0000313|Proteomes:UP000001739};
RX PubMed=21551308; DOI=10.1128/JB.05055-11;
RA Weilharter A., Mitter B., Shin M.V., Chain P.S., Nowak J., Sessitsch A.;
RT "Complete genome sequence of the plant growth-promoting endophyte
RT Burkholderia phytofirmans strain PsJN.";
RL J. Bacteriol. 193:3383-3384(2011).
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; CP001053; ACD20430.1; -; Genomic_DNA.
DR RefSeq; WP_012427938.1; NC_010676.1.
DR AlphaFoldDB; B2TAT0; -.
DR STRING; 398527.Bphyt_6098; -.
DR KEGG; bpy:Bphyt_6098; -.
DR eggNOG; COG0473; Bacteria.
DR HOGENOM; CLU_031953_0_1_4; -.
DR OrthoDB; 5289857at2; -.
DR Proteomes; UP000001739; Chromosome 2.
DR GO; GO:0046553; F:D-malate dehydrogenase (decarboxylating) activity; IEA:UniProtKB-EC.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
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 Lyase {ECO:0000313|EMBL:ACD20430.1};
KW Manganese {ECO:0000256|ARBA:ARBA00023211}.
FT DOMAIN 6..355
FT /note="Isopropylmalate dehydrogenase-like"
FT /evidence="ECO:0000259|SMART:SM01329"
SQ SEQUENCE 360 AA; 39565 MW; E339C56C99B2F364 CRC64;
MSKKYRIAVI PGDGIGVEVM PEAIRALEAV KTRFGIELEY QHIEWASCDY YAKHGKMMPD
DWKAQLQSAD AILFGAVGWP DTVPDHISLW GSLLKFRREF DQYINLRPAR LFAGVPSPLA
GRRAGDIDFW IVRENTEGEY SSVGGVMFEG TEREFVLQES VFTRHGSERV LKFAFDLAQR
RERKKITVAT KSNGIAISMP WWDKVAAGIA AQYPDVTWDK QHIDILCARF VLSPDRFDVV
VATNLFGDIL SDLGPACTGT IGLAPSGNLN PDRKFPSLFE PVHGSAPDIA GKNIANPIAM
IWSAAMMLDF LGNHEGKERE AHDAILAAIE ATLVEGPHTG DLGGKANTTE VGQAIAARLA
//
