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 27-MAR-2024, entry version 107.
DE RecName: Full=2-isopropylmalate synthase 1 {ECO:0000250|UniProtKB:Q9JZG1};
DE EC=2.3.3.13 {ECO:0000250|UniProtKB:Q9JZG1};
DE AltName: Full=Alpha-IPM synthase 1 {ECO:0000250|UniProtKB:Q9JZG1};
DE AltName: Full=Alpha-isopropylmalate synthase 1 {ECO:0000250|UniProtKB:Q9JZG1};
GN Name=leuA1 {ECO:0000303|PubMed:11997336}; OrderedLocusNames=TTE0016;
OS Caldanaerobacter subterraneus subsp. tengcongensis (strain DSM 15242 / JCM
OS 11007 / NBRC 100824 / MB4) (Thermoanaerobacter tengcongensis).
OC Bacteria; Bacillota; 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-ketoisovalerate) to form 3-carboxy-3-
CC hydroxy-4-methylpentanoate (2-isopropylmalate).
CC {ECO:0000250|UniProtKB:Q9JZG1}.
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 Evidence={ECO:0000250|UniProtKB:Q9JZG1};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:Q9JZG1};
CC -!- PATHWAY: Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine
CC from 3-methyl-2-oxobutanoate: step 1/4. {ECO:0000250|UniProtKB:Q9JZG1}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q9JZG1}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9JZG1}.
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; NZ_JANUCV010000001.1.
DR AlphaFoldDB; Q8RDK3; -.
DR SMR; Q8RDK3; -.
DR STRING; 273068.TTE0016; -.
DR KEGG; tte:TTE0016; -.
DR eggNOG; COG0119; Bacteria.
DR HOGENOM; CLU_022158_3_1_9; -.
DR OrthoDB; 9804858at2; -.
DR UniPathway; UPA00048; UER00070.
DR Proteomes; UP000000555; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003852; F:2-isopropylmalate synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0009098; P:leucine biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd07940; DRE_TIM_IPMS; 1.
DR Gene3D; 1.10.238.260; -; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR InterPro; IPR002034; AIPM/Hcit_synth_CS.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR000891; PYR_CT.
DR PANTHER; PTHR10277:SF9; 2-ISOPROPYLMALATE SYNTHASE 1, CHLOROPLASTIC-RELATED; 1.
DR PANTHER; PTHR10277; HOMOCITRATE SYNTHASE-RELATED; 1.
DR Pfam; PF00682; HMGL-like; 1.
DR SUPFAM; SSF51569; Aldolase; 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; Cytoplasm;
KW Leucine biosynthesis; Manganese; Metal-binding; Reference proteome;
KW 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"
FT BINDING 15
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:Q9JZG1"
FT BINDING 203
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:Q9JZG1"
FT BINDING 205
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:Q9JZG1"
FT BINDING 239
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:Q9JZG1"
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
//
