ID A0A0R2PFE0_9ACTN Unreviewed; 344 AA.
AC A0A0R2PFE0;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=3-isopropylmalate dehydrogenase {ECO:0000313|EMBL:KRO36623.1};
DE EC=1.1.1.85 {ECO:0000313|EMBL:KRO36623.1};
GN ORFNames=ABR54_00865 {ECO:0000313|EMBL:KRO36623.1};
OS Actinobacteria bacterium BACL15 MAG-120619-bin91.
OC Bacteria; Actinomycetota; Actinomycetes; Actinomycetes incertae sedis;
OC ac1 cluster.
OX NCBI_TaxID=1655562 {ECO:0000313|EMBL:KRO36623.1, ECO:0000313|Proteomes:UP000053274};
RN [1] {ECO:0000313|EMBL:KRO36623.1, ECO:0000313|Proteomes:UP000053274}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BACL15 MAG-120619-bin91 {ECO:0000313|EMBL:KRO36623.1};
RA Hugerth L.W., Larsson J., Alneberg J., Lindh M.V., Legrand C., Pinhassi J.,
RA Andersson A.F.;
RT "Metagenome-Assembled Genomes uncover a global brackish microbiome.";
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
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:KRO36623.1}.
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DR EMBL; LIAM01000003; KRO36623.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0R2PFE0; -.
DR Proteomes; UP000053274; Unassembled WGS sequence.
DR GO; GO:0003862; F:3-isopropylmalate dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0051287; F:NAD binding; 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};
KW Oxidoreductase {ECO:0000313|EMBL:KRO36623.1}.
FT DOMAIN 5..340
FT /note="Isopropylmalate dehydrogenase-like"
FT /evidence="ECO:0000259|SMART:SM01329"
SQ SEQUENCE 344 AA; 36647 MW; BACD40F3A41167A0 CRC64;
MRTINLAVIA GDGIGPEVVH EGLKVLDIVA KRYSVEFKKT SYDLGAAFWH RTGEVLPDAT
LAELAKADVI LLGAVGDPTV PSGVLERGLL LKLRFAFDHY INLRPARLMP GVTGPLATKA
PIDFVVVREG TEGPYVGAGG VLAEGTAAEI ATEESLNTRR GAERVIRDAF ERASQRERKK
LTLVHKNNVL TRAGGLWTRT FNEVAKEYPA ITTDYLHVDA ASMFFVTNPE RFDVVVTDNL
FGDILTDIAA AICGGIGLAA SGNINPTGKF PSMFEPVHGS APDIAGKNLA DPTATVMSVA
MMLDHLGLND AARDVETVVA ADLLSRGDKK RSTTEIGDAL ASAL
//
