ID A0A117I6V7_9MYCO Unreviewed; 160 AA.
AC A0A117I6V7;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=Tartrate dehydrogenase/decarboxylase/D-malate dehydrogenase {ECO:0000313|EMBL:GAS90695.1};
GN ORFNames=RMCB_4791 {ECO:0000313|EMBL:GAS90695.1};
OS Mycolicibacterium brisbanense.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=146020 {ECO:0000313|EMBL:GAS90695.1, ECO:0000313|Proteomes:UP000069620};
RN [1] {ECO:0000313|EMBL:GAS90695.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM15654 {ECO:0000313|EMBL:GAS90695.1};
RA Katahira K., Ogura Y., Gotoh Y., Hayashi T.;
RT "Draft Genome Sequences of Five Rapidly Growing Mycobacterium Species, M.
RT thermoresistibile, M. fortuitum subsp. acetamidolyticum, M. canariasense,
RT M. brisbanense, and M. novocastrense.";
RL Genome Announc. 4:e00322-16(2016).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2R,3S)-3-isopropylmalate + NAD(+) = 4-methyl-2-oxopentanoate
CC + CO2 + NADH; Xref=Rhea:RHEA:32271, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:17865, ChEBI:CHEBI:35121, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945; EC=1.1.1.85;
CC Evidence={ECO:0000256|ARBA:ARBA00000624};
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 -!- 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:GAS90695.1}.
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DR EMBL; BCSX01000041; GAS90695.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A117I6V7; -.
DR STRING; 146020.RMCB_4791; -.
DR Proteomes; UP000069620; Unassembled WGS sequence.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR GO; GO:0009098; P:leucine biosynthetic process; IEA:UniProtKB-KW.
DR Gene3D; 3.40.718.10; Isopropylmalate Dehydrogenase; 1.
DR InterPro; IPR019818; IsoCit/isopropylmalate_DH_CS.
DR InterPro; IPR024084; IsoPropMal-DH-like_dom.
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 4: Predicted;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022430};
KW Branched-chain amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023304};
KW Leucine biosynthesis {ECO:0000256|ARBA:ARBA00022430};
KW Manganese {ECO:0000256|ARBA:ARBA00023211}.
FT DOMAIN 1..154
FT /note="Isopropylmalate dehydrogenase-like"
FT /evidence="ECO:0000259|SMART:SM01329"
SQ SEQUENCE 160 AA; 16776 MW; DEBA23021F712EE8 CRC64;
MPFWDEIVAE RARGYPSVQW RAEHIDALAA KVVLDPASFD VIVASNLFGD ILSDLAAAVA
GSIGMAPSAN LNPTGELPSM FEPVHGSAPD IACDGIANPI GAIWSAAMML EHLGGHPEAT
AEVLTAIRQC LKSKQTLTRD LGGTASTAEL TKSVIEQIRA
//
