ID LEU1_CLOCE Reviewed; 508 AA.
AC B8I1T7;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 01-MAY-2013, entry version 34.
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=Ccel_3434;
OS Clostridium cellulolyticum (strain ATCC 35319 / DSM 5812 / JCM 6584 /
OS H10).
OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=394503;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35319 / DSM 5812 / JCM 6584 / H10;
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
RA Tice H., Bruce D., Goodwin L., Pitluck S., Chertkov O., Saunders E.,
RA Brettin T., Detter J.C., Han C., Larimer F., Land M., Hauser L.,
RA Kyrpides N., Ivanova N., Zhou J., Richardson P.;
RT "Complete sequence of Clostridium cellulolyticum H10.";
RL Submitted (JAN-2009) 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; CP001348; ACL77722.1; -; Genomic_DNA.
DR RefSeq; YP_002507702.1; NC_011898.1.
DR ProteinModelPortal; B8I1T7; -.
DR STRING; 394503.Ccel_3434; -.
DR EnsemblBacteria; ACL77722; ACL77722; Ccel_3434.
DR GeneID; 7311996; -.
DR KEGG; cce:Ccel_3434; -.
DR PATRIC; 19437887; VBICloCel57783_3513.
DR eggNOG; COG0119; -.
DR HOGENOM; HOG000046859; -.
DR KO; K01649; -.
DR OMA; VWSVHCH; -.
DR ProtClustDB; CLSK854269; -.
DR BioCyc; CCEL394503:GJET-3509-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 1 508 2-isopropylmalate synthase.
FT /FTId=PRO_1000149169.
SQ SEQUENCE 508 AA; 55525 MW; 684601A469C533E7 CRC64;
MARTIKIFDT TLRDGEQTPG VNLNLQEKLE IAKQLVRLGV DVIEGGFAIA SPGDFESIMT
LSRNLKGVTI ASLCRSVEKD IDRAWEAVQY AESPRIHTFI ATSDIHMKYK LKMTEEEVLE
RAVSMVKRAK GYCSNVEFSA EDASRTREEF LYRVVEAVIK AGATTVNIPD TVGYSTPLEF
GRLIRNIRNN VPNIDKADIS VHCHNDLGLA VANSLAAVEN GAVQVECTIN GLGERAGNAA
LEEIIMGINT RKDYYDITHR IDTTQIYRAS RLVSSLTGVN VQPNKAIVGA NAFAHESGIH
QHGVLSEKTT YEIMTPESVG MGTNRMVLGK LSGRHAFEDR LKEMGYSLSD EEVKTAFAKF
KDLADKKKVV TDKDIEALVD ENIAVPEIFV IDSFQINSGN KMISTSTVSV RKDEEIITEA
ATGDGPVDAA FNAVERATGV NAELVHYRIK AVTEGKDALG EVTVKISNNN SIFMGKGVST
DIIEASVKAY LNAINRSISE IGESIISQ
//
