ID E7RI97_9BACL Unreviewed; 357 AA.
AC E7RI97;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 24-JAN-2024, entry version 40.
DE RecName: Full=D-malate dehydrogenase (decarboxylating) {ECO:0000256|ARBA:ARBA00013126};
DE EC=1.1.1.83 {ECO:0000256|ARBA:ARBA00013126};
GN ORFNames=GPDM_11025 {ECO:0000313|EMBL:EGA89272.1};
OS Planococcus donghaensis MPA1U2.
OC Bacteria; Bacillota; Bacilli; Bacillales; Planococcaceae; Planococcus.
OX NCBI_TaxID=933115 {ECO:0000313|EMBL:EGA89272.1, ECO:0000313|Proteomes:UP000003052};
RN [1] {ECO:0000313|EMBL:EGA89272.1, ECO:0000313|Proteomes:UP000003052}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MPA1U2 {ECO:0000313|EMBL:EGA89272.1,
RC ECO:0000313|Proteomes:UP000003052};
RX PubMed=21994932; DOI=10.1128/JB.05983-11;
RA Pearson M.D., Noller H.F.;
RT "The Draft Genome of Planococcus donghaensis MPA1U2 Reveals Nonsporulation
RT Pathways Controlled by a Conserved Spo0A Regulon.";
RL J. Bacteriol. 193:6106-6106(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}.
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:EGA89272.1}.
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DR EMBL; AEPB01000036; EGA89272.1; -; Genomic_DNA.
DR RefSeq; WP_008431307.1; NZ_AEPB01000036.1.
DR AlphaFoldDB; E7RI97; -.
DR eggNOG; COG0473; Bacteria.
DR OrthoDB; 9806254at2; -.
DR Proteomes; UP000003052; 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 5..347
FT /note="Isopropylmalate dehydrogenase-like"
FT /evidence="ECO:0000259|SMART:SM01329"
SQ SEQUENCE 357 AA; 39250 MW; 6E755994B66318D5 CRC64;
MTAYKIAVLP GDGIGPDVTK EAVKVLEALK EQDPTFDIAF EQFEWGSEYY LANGYIMPED
GLDQLKNFDA ILFGAVGDKR VPDEITIWEL IMPIRKNFQQ YVNMRPIKRL AGIESPLKNE
QPIDFMVFRE NAEGEYSNIG GRLYQQHSQE MAIQNTVITK QGVERIAKYA FEYAQKNNKS
KVTSATKSNA IIHSMKLWDE VVELVAKDYK DIELESNFID ALAAYFVLRP ESFEVVIASN
LFGDILTDLG AALVGGLGVS PSGNINPEGN FPSMFEAIHG SAPDIAGKGI ANPVAQIWSA
ALMLNHLGRE DLSTAIVDAI EQVIQEGKVL TPDLGGTSTT QEVGSAIAEK VLMLVKN
//
