ID I7LLC2_METBM Unreviewed; 373 AA.
AC I7LLC2;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE SubName: Full=3-isopropylmalate dehydrogenase {ECO:0000313|EMBL:CCJ35239.1};
DE EC=1.1.1.85 {ECO:0000313|EMBL:CCJ35239.1};
GN Name=leuB1 {ECO:0000313|EMBL:CCJ35239.1};
GN OrderedLocusNames=BN140_0316 {ECO:0000313|EMBL:CCJ35239.1};
OS Methanoculleus bourgensis (strain ATCC 43281 / DSM 3045 / OCM 15 / MS2)
OS (Methanogenium bourgense).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanomicrobiales; Methanomicrobiaceae; Methanoculleus.
OX NCBI_TaxID=1201294 {ECO:0000313|EMBL:CCJ35239.1, ECO:0000313|Proteomes:UP000009007};
RN [1] {ECO:0000313|Proteomes:UP000009007}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43281 / DSM 3045 / OCM 15 / MS2
RC {ECO:0000313|Proteomes:UP000009007};
RX PubMed=22965103; DOI=10.1128/JB.01292-12;
RA Maus I., Wibberg D., Stantscheff R., Eikmeyer F.G., Seffner A., Boelter J.,
RA Szczepanowski R., Blom J., Jaenicke S., Konig H., Puhler A., Schluter A.;
RT "Complete genome sequence of the hydrogenotrophic, methanogenic archaeon
RT Methanoculleus bourgensis strain MS2T, isolated from a sewage sludge
RT digester.";
RL J. Bacteriol. 194:5487-5488(2012).
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};
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DR EMBL; HE964772; CCJ35239.1; -; Genomic_DNA.
DR RefSeq; WP_014866216.1; NC_018227.2.
DR AlphaFoldDB; I7LLC2; -.
DR STRING; 1201294.BN140_0316; -.
DR GeneID; 13355091; -.
DR KEGG; mbg:BN140_0316; -.
DR PATRIC; fig|1201294.9.peg.341; -.
DR HOGENOM; CLU_031953_0_1_2; -.
DR BioCyc; MBOU1201294:BN140_RS01585-MONOMER; -.
DR Proteomes; UP000009007; Chromosome.
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 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 Manganese {ECO:0000256|ARBA:ARBA00023211};
KW Oxidoreductase {ECO:0000313|EMBL:CCJ35239.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000009007}.
FT DOMAIN 4..366
FT /note="Isopropylmalate dehydrogenase-like"
FT /evidence="ECO:0000259|SMART:SM01329"
SQ SEQUENCE 373 AA; 40758 MW; BD2684FE8218CE3B CRC64;
MQHQVAAIGG DGIGPEIIAA GKEVLDAAGE RFGFDIAWTD FDVGAERYLS TGELLTEEDL
RELSKFRAIY FGAIGDERVK PGILEKGILL AIRFHFDQFV NLRPIKLLEG APTPLANKGP
EDVDFVVVRE NTEDFYVGIG SRFTGAREQK TLEVVRDLYN IKFGLDVETD ADEIAYQIGV
VTRPGAERVI RYAFDLAAAR ERKVTSVDKA NVLSDVYGLW RDVFNQVATG YPDVATEFTF
VDAVTMWFVK NPEWFDVVVT PNMFGDIITD LGAMIQGGLG LAPGGNINPA GTSMFEPIHG
SAPKYRGQDV ANPLATIWAG SMLLDHIGER EAARAVLSAI EQSILDGFVT RDMGGAKKTS
EVGRYVASLV KRA
//