LEU1_IGNH4
ID LEU1_IGNH4 Reviewed; 399 AA.
AC A8AB61;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-OCT-2007, sequence version 1.
DT 25-MAY-2022, entry version 71.
DE RecName: Full=Probable 2-isopropylmalate synthase;
DE EC=2.3.3.13;
DE AltName: Full=Alpha-IPM synthase;
DE AltName: Full=Alpha-isopropylmalate synthase;
GN Name=leuA; OrderedLocusNames=Igni_0983;
OS Ignicoccus hospitalis (strain KIN4/I / DSM 18386 / JCM 14125).
OC Archaea; Crenarchaeota; Thermoprotei; Desulfurococcales;
OC Desulfurococcaceae; Ignicoccus.
OX NCBI_TaxID=453591;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KIN4/I / DSM 18386 / JCM 14125;
RX PubMed=19000309; DOI=10.1186/gb-2008-9-11-r158;
RA Podar M., Anderson I., Makarova K.S., Elkins J.G., Ivanova N., Wall M.A.,
RA Lykidis A., Mavromatis K., Sun H., Hudson M.E., Chen W., Deciu C.,
RA Hutchison D., Eads J.R., Anderson A., Fernandes F., Szeto E., Lapidus A.,
RA Kyrpides N.C., Saier M.H. Jr., Richardson P.M., Rachel R., Huber H.,
RA Eisen J.A., Koonin E.V., Keller M., Stetter K.O.;
RT "A genomic analysis of the archaeal system Ignicoccus hospitalis-
RT Nanoarchaeum equitans.";
RL Genome Biol. 9:R158.1-R158.18(2008).
CC -!- FUNCTION: Catalyzes the condensation of the acetyl group of acetyl-CoA
CC with 3-methyl-2-oxobutanoate (2-oxoisovalerate) to form 3-carboxy-3-
CC hydroxy-4-methylpentanoate (2-isopropylmalate). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-methyl-2-oxobutanoate + acetyl-CoA + H2O = (2S)-2-
CC isopropylmalate + CoA + H(+); Xref=Rhea:RHEA:21524, ChEBI:CHEBI:1178,
CC ChEBI:CHEBI:11851, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288; EC=2.3.3.13;
CC -!- PATHWAY: Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine
CC from 3-methyl-2-oxobutanoate: step 1/4.
CC -!- SIMILARITY: Belongs to the alpha-IPM synthase/homocitrate synthase
CC family. {ECO:0000305}.
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DR EMBL; CP000816; ABU82163.1; -; Genomic_DNA.
DR RefSeq; WP_012123127.1; NC_009776.1.
DR AlphaFoldDB; A8AB61; -.
DR SMR; A8AB61; -.
DR STRING; 453591.Igni_0983; -.
DR EnsemblBacteria; ABU82163; ABU82163; Igni_0983.
DR GeneID; 5563127; -.
DR KEGG; iho:Igni_0983; -.
DR eggNOG; arCOG02092; Archaea.
DR HOGENOM; CLU_022158_4_2_2; -.
DR OMA; NTMRMLV; -.
DR OrthoDB; 26145at2157; -.
DR PhylomeDB; A8AB61; -.
DR UniPathway; UPA00048; UER00070.
DR Proteomes; UP000000262; Chromosome.
DR GO; GO:0003852; F:2-isopropylmalate synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0009098; P:leucine biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.20.20.70; -; 1.
DR InterPro; IPR002034; AIPM/Hcit_synth_CS.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR011830; LEU1_arch.
DR InterPro; IPR000891; PYR_CT.
DR Pfam; PF00682; HMGL-like; 1.
DR TIGRFAMs; TIGR02090; LEU1_arch; 1.
DR PROSITE; PS00815; AIPM_HOMOCIT_SYNTH_1; 1.
DR PROSITE; PS00816; AIPM_HOMOCIT_SYNTH_2; 1.
DR PROSITE; PS50991; PYR_CT; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis; Branched-chain amino acid biosynthesis;
KW Leucine biosynthesis; Reference proteome; Transferase.
FT CHAIN 1..399
FT /note="Probable 2-isopropylmalate synthase"
FT /id="PRO_1000149211"
FT DOMAIN 20..272
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01151"
SQ SEQUENCE 399 AA; 43687 MW; 15A69674A4FD3A8E CRC64;
MLIVEGVRIA EELENLPKEV RIFDTTLRDG EQTPGISFTK EQKLMIARQL AKLGVASIEA
GFPAVSQGEF EAVKAIAREG LGPEIVALAR ANKRDIDKAL DADVDAIHVF IAASDIHLKY
KLRMTREEAL RRAVEAVEYA KSHGVTVEFS PEDGTRADLN YLYTMVEAVV DAGADRVDIP
DTVGVMTPTR MKYLIKFILP AAKGRIVSVH CHNDFGLAVA NSIAGIEAGA RQAHVTVNGI
GERAGNAALE EVVAALEFLL NVRTGVNTKL LYETSLLVSK ITGIPIPPNK PIVGENVFSH
ESGIHVHGVI NNPFTYEPIQ PEMVGQRRRI VLGKHSGRHG VEYALKTLGY PTDPDVVLRV
LDEVKRLGDM GIRVTEDKLR EIVEKVLEER ERAKEAATS
