LEU12_CALS4
ID LEU12_CALS4 Reviewed; 384 AA.
AC Q8RCF9;
DT 26-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 25-MAY-2022, entry version 103.
DE RecName: Full=2-isopropylmalate synthase 2;
DE EC=2.3.3.13;
DE AltName: Full=Alpha-IPM synthase 2;
DE AltName: Full=Alpha-isopropylmalate synthase 2;
GN Name=leuA2; OrderedLocusNames=TTE0472;
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE008691; AAM23753.1; -; Genomic_DNA.
DR RefSeq; WP_011024905.1; NC_003869.1.
DR AlphaFoldDB; Q8RCF9; -.
DR SMR; Q8RCF9; -.
DR STRING; 273068.TTE0472; -.
DR EnsemblBacteria; AAM23753; AAM23753; TTE0472.
DR KEGG; tte:TTE0472; -.
DR eggNOG; COG0119; Bacteria.
DR HOGENOM; CLU_022158_4_2_9; -.
DR OMA; SNMFAHE; -.
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 CDD; cd07939; DRE_TIM_NifV; 1.
DR Gene3D; 3.20.20.70; -; 1.
DR InterPro; IPR002034; AIPM/Hcit_synth_CS.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR013477; NifV/FrbC.
DR InterPro; IPR000891; PYR_CT.
DR Pfam; PF00682; HMGL-like; 1.
DR TIGRFAMs; TIGR02660; nifV_homocitr; 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..384
FT /note="2-isopropylmalate synthase 2"
FT /id="PRO_0000140394"
FT DOMAIN 9..260
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01151"
SQ SEQUENCE 384 AA; 42404 MW; 095310F2C0E4A4DD CRC64;
MAFKKDKPVY IVDTTLRDGE QTAGVVFANN EKIRIAQMLD EIGIDQLEVG IPTMGGDEKE
TVAKIAKLGL KASIMAWNRA VVKDVQESLE CGVDAVAISI STSDIHIEHK LKKTRQWVLD
SMTEAVRFAK KEGVYVSVNA EDASRTDMNF LIEFARCAKQ AGADRLRFCD TVGFLDPFKT
YEMVKAIKDA VDIEIEMHTH NDFGMATANA LAGVKAGAKF VGVTVNGLGE RAGNAALEEV
VMALKYVYKM DLGIDTSRFR EISEYVALAS GRPLPPSKAI VGKNVFAHES GIHVDGALKN
PYTYEVFDPQ EVGLERQIVI GKHSGTAALI NKFKEYGRVL TEEEANLLLP HVRKMAIQLK
RPLFDKELMY LYEDVIVKGK AKAI
