ID H0QK86_ARTGO Unreviewed; 362 AA.
AC H0QK86;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=Putative 3-isopropylmalate dehydrogenase {ECO:0000313|EMBL:GAB13326.1};
GN ORFNames=ARGLB_037_01770 {ECO:0000313|EMBL:GAB13326.1};
OS Arthrobacter globiformis NBRC 12137.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Arthrobacter.
OX NCBI_TaxID=1077972 {ECO:0000313|EMBL:GAB13326.1, ECO:0000313|Proteomes:UP000003828};
RN [1] {ECO:0000313|EMBL:GAB13326.1, ECO:0000313|Proteomes:UP000003828}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 12137 {ECO:0000313|EMBL:GAB13326.1,
RC ECO:0000313|Proteomes:UP000003828};
RA Miyazawa S., Hosoyama A., Tsuchikane K., Katsumata H., Yamazaki S.,
RA Fujita N.;
RT "Whole genome shotgun sequence of Arthrobacter globiformis NBRC 12137.";
RL Submitted (DEC-2011) 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:GAB13326.1}.
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DR EMBL; BAEG01000037; GAB13326.1; -; Genomic_DNA.
DR RefSeq; WP_003800467.1; NZ_BAEG01000037.1.
DR AlphaFoldDB; H0QK86; -.
DR STRING; 1077972.ARGLB_037_01770; -.
DR eggNOG; COG0473; Bacteria.
DR OrthoDB; 5289857at2; -.
DR Proteomes; UP000003828; 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:UP000003828}.
FT DOMAIN 8..353
FT /note="Isopropylmalate dehydrogenase-like"
FT /evidence="ECO:0000259|SMART:SM01329"
SQ SEQUENCE 362 AA; 38058 MW; 229C4BF630562F7E CRC64;
MTESKQYQLA VLNGDGIGPE IVPASVKILD AAMAAAGAPA IAWTELPLGR SAIDTHGTAV
PAETLEALNN VDGWLLGPHD SASYPEPHKS ALNPSGTIRK HFGLFANIRP SKAFPGGNAI
VEGTDLVIVR ENTEGFYADR NTFAGTGEFM PTPDVAIMHG IITRAATERI AHSAFQLARS
RSKQLTIVHK ANVLKMTTGL FRDVCKEVAA QYPDVSVNDF HIDAMTVHLV RRANKFDVIV
TENMFGDILS DLAGEVAGSL GIAPSINSSD THAMAQASHG SAPDIAGKNI ANPIAMILSS
AMLLRWLGAK FGDEKVLAAA ELVEKAIEAT VLDGTATKDM GGTSGTSEFA DAVAAHITIR
GV
//