LEU11_CALS4
ID LEU11_CALS4 Reviewed; 397 AA.
AC Q8RDK3;
DT 26-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 25-MAY-2022, entry version 102.
DE RecName: Full=2-isopropylmalate synthase 1;
DE EC=2.3.3.13;
DE AltName: Full=Alpha-IPM synthase 1;
DE AltName: Full=Alpha-isopropylmalate synthase 1;
GN Name=leuA1; OrderedLocusNames=TTE0016;
OS Caldanaerobacter subterraneus subsp. tengcongensis (strain DSM 15242 / JCM
OS 11007 / NBRC 100824 / MB4) (Thermoanaerobacter tengcongensis).
OC Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales;
OC Thermoanaerobacteraceae; Caldanaerobacter.
OX NCBI_TaxID=273068;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15242 / JCM 11007 / NBRC 100824 / MB4;
RX PubMed=11997336; DOI=10.1101/gr.219302;
RA Bao Q., Tian Y., Li W., Xu Z., Xuan Z., Hu S., Dong W., Yang J., Chen Y.,
RA Xue Y., Xu Y., Lai X., Huang L., Dong X., Ma Y., Ling L., Tan H., Chen R.,
RA Wang J., Yu J., Yang H.;
RT "A complete sequence of the T. tengcongensis genome.";
RL Genome Res. 12:689-700(2002).
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 -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the alpha-IPM synthase/homocitrate synthase
CC family. LeuA type 1 subfamily. {ECO:0000305}.
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DR EMBL; AE008691; AAM23333.1; -; Genomic_DNA.
DR RefSeq; WP_011024550.1; NC_003869.1.
DR AlphaFoldDB; Q8RDK3; -.
DR SMR; Q8RDK3; -.
DR STRING; 273068.TTE0016; -.
DR EnsemblBacteria; AAM23333; AAM23333; TTE0016.
DR KEGG; tte:TTE0016; -.
DR eggNOG; COG0119; Bacteria.
DR HOGENOM; CLU_022158_3_1_9; -.
DR OMA; NTMRMLV; -.
DR OrthoDB; 840579at2; -.
DR UniPathway; UPA00048; UER00070.
DR Proteomes; UP000000555; 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; IPR000891; PYR_CT.
DR Pfam; PF00682; HMGL-like; 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..397
FT /note="2-isopropylmalate synthase 1"
FT /id="PRO_0000140393"
FT DOMAIN 6..268
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01151"
SQ SEQUENCE 397 AA; 44026 MW; A93AA8742F75E777 CRC64;
MGVKRVIVFD TTLRDGEQTP GVNFNSRDKL EIAYQLAKLG VDVIEAGFPA ASNGDFEAVK
NIADYVKGVT IAAMGRAVKE DIDRASSALK NAEKSRLHVF IATSDIHLQY KLKMTRDEVL
KKAVEMVKYA RGKFDEIEFS AEDASRTDWD FLVKVFSEVI DAGAHIINVP DTVGYAMPRE
YGELIRYIRN NVPNIDGVTI SAHCHNDLGL AVANSLSAIE NGATQVEVTV NGIGERAGNA
AMEEVIMALN TRKDYFGLVH GINTKEIYNT SKLVSELTGI KLQPNKAIVG ANAFRHQSGI
HQHGVINNRL TYEIMRPEDI GVVPDTFALG KLSGRNAFEL KVRQLGYNLS PGEISEAFRK
FKDLADRKKT IVEEDIRFVV EETIEEFRGF REGEAWA
