ID A0A0W7W6U5_9MICO Unreviewed; 353 AA.
AC A0A0W7W6U5;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=3-isopropylmalate dehydrogenase {ECO:0000313|EMBL:KUF06331.1};
GN ORFNames=AUL38_13490 {ECO:0000313|EMBL:KUF06331.1};
OS Leucobacter sp. G161.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Leucobacter.
OX NCBI_TaxID=663704 {ECO:0000313|EMBL:KUF06331.1, ECO:0000313|Proteomes:UP000053012};
RN [1] {ECO:0000313|EMBL:KUF06331.1, ECO:0000313|Proteomes:UP000053012}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=G161 {ECO:0000313|EMBL:KUF06331.1,
RC ECO:0000313|Proteomes:UP000053012};
RA Ge S., Dong X.;
RT "High quality draft genome sequence of Leucobacter sp. G161, a distinct and
RT effective chromium reducer.";
RL Submitted (DEC-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:KUF06331.1}.
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DR EMBL; LOHP01000071; KUF06331.1; -; Genomic_DNA.
DR RefSeq; WP_059062629.1; NZ_LOHP01000071.1.
DR AlphaFoldDB; A0A0W7W6U5; -.
DR STRING; 663704.AUL38_13490; -.
DR OrthoDB; 5289857at2; -.
DR Proteomes; UP000053012; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000053012}.
FT DOMAIN 6..345
FT /note="Isopropylmalate dehydrogenase-like"
FT /evidence="ECO:0000259|SMART:SM01329"
SQ SEQUENCE 353 AA; 37225 MW; CDD3014EE13B6E9C CRC64;
MTRTIKLAVI PGDGIGPEVI EQANRVVDAV VAGGDIVVER TEFKLGAERF LATGDTLPEI
EQAAIASHDA ILFGAVGGVP GDERLRFANI ERGLLLKLRF DFEHYANVRP CVLFPGVEST
LANPGTVDFV VVREGTEGPY VGNGGRLRPG TPAEVATEVS VNTAFGVERV VRYAFETAMA
RPRKKLTWVH KTNVLVHAGQ TWQGVVEAVR AEYPDIAVDY MHVDAATIHM VQNPAQFDVI
VTDNLFGDIL TDLAGAIGGG IGLAASGNIN PDGSFPSMFE PVHGSAPDIA GQQKADPTAA
ILSAGLMLDH LGLSAEADRL RAAVRADRAT HGSAARATAE VGDAIIAQIP ARS
//
