ID LEU1_CAMFF Reviewed; 506 AA.
AC A0RQK7;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 1.
DT 01-MAY-2013, entry version 49.
DE RecName: Full=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=CFF8240_1344;
OS Campylobacter fetus subsp. fetus (strain 82-40).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Campylobacteraceae; Campylobacter.
OX NCBI_TaxID=360106;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=82-40;
RA Fouts D.E., Nelson K.E.;
RT "Sequence of Campylobacter fetus subsp. fetus 82-40.";
RL Submitted (NOV-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the condensation of the acetyl group of
CC acetyl-CoA with 3-methyl-2-oxobutanoate (2-oxoisovalerate) to form
CC 3-carboxy-3-hydroxy-4-methylpentanoate (2-isopropylmalate) (By
CC similarity).
CC -!- CATALYTIC ACTIVITY: Acetyl-CoA + 3-methyl-2-oxobutanoate + H(2)O =
CC (2S)-2-isopropylmalate + CoA.
CC -!- PATHWAY: Amino-acid biosynthesis; L-leucine biosynthesis; L-
CC leucine from 3-methyl-2-oxobutanoate: step 1/4.
CC -!- SUBUNIT: Homotetramer (By similarity).
CC -!- SIMILARITY: Belongs to the alpha-IPM synthase/homocitrate synthase
CC family. LeuA type 1 subfamily.
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DR EMBL; CP000487; ABK82096.1; -; Genomic_DNA.
DR RefSeq; YP_892490.1; NC_008599.1.
DR ProteinModelPortal; A0RQK7; -.
DR STRING; 360106.CFF8240_1344; -.
DR EnsemblBacteria; ABK82096; ABK82096; CFF8240_1344.
DR GeneID; 4539073; -.
DR KEGG; cff:CFF8240_1344; -.
DR PATRIC; 20037206; VBICamFet25865_1308.
DR eggNOG; COG0119; -.
DR HOGENOM; HOG000046859; -.
DR KO; K01649; -.
DR OMA; VWSVHCH; -.
DR ProtClustDB; PRK00915; -.
DR BioCyc; CFET360106:GHTH-1359-MONOMER; -.
DR UniPathway; UPA00048; UER00070.
DR GO; GO:0003852; F:2-isopropylmalate synthase activity; IEA:HAMAP.
DR GO; GO:0009098; P:leucine biosynthetic process; IEA:HAMAP.
DR Gene3D; 3.20.20.70; -; 1.
DR HAMAP; MF_01025; LeuA_type1; 1; -.
DR InterPro; IPR013709; 2-isopropylmalate_synth_dimer.
DR InterPro; IPR002034; AIPM/Hcit_synth_CS.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR005671; LeuA_bact_synth.
DR InterPro; IPR000891; PYR_CT.
DR Pfam; PF00682; HMGL-like; 1.
DR Pfam; PF08502; LeuA_dimer; 1.
DR SMART; SM00917; LeuA_dimer; 1.
DR SUPFAM; SSF110921; 2-isopropylmalate_synth_dimer; 1.
DR TIGRFAMs; TIGR00973; leuA_bact; 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 Complete proteome; Leucine biosynthesis; Transferase.
FT CHAIN 1 506 2-isopropylmalate synthase.
FT /FTId=PRO_1000149159.
SQ SEQUENCE 506 AA; 54896 MW; EA0FBEE7E49F01E2 CRC64;
MDNNKIIVFD TTLRDGEQSP GASMNTEEKI QIALQLERLG VDVMEAGFAA ASPGDFDAIN
QIAKQIHSIR IASLARALEK DIKAAGEAIS PAKNRRIHTF IATSPIHMEH KLKMTPDEVI
KRAVEAVKYA KTFVDDVEFS CEDAGRSDIV FLKEICAAVV EAGARTLNLP DTVGFRMPDE
IYNMVKSMVD FIGDRAIISV HNHNDLGLAV ANTLASIKAG ARQVECTING LGERAGNAAL
EEIVMTIRTR SDEFAPLYTD IVTKEIYATS RLVASITGIE PQPNKAIVGK NAFAHESGIH
QDGMLKCAQT YEIIKAEDIG AEKNSLVLGK HSGRHAFKDK LINLGFDLDD NEINEAFIKF
KELCDKKKEI FDDDIRALVS HEIIKIPEIY SIQTLSTSSC NAGHSSAAVS IKFSDNIISD
AALGNGTADA IFKVIDRISG ISGELKDYKV NAVSQGKDAL AKITVKVVFE GSSCATIGHG
LDIDTMMASA KAYVSALNSY LSMKNR
//
