ID LEU1_XANCP Reviewed; 520 AA.
AC P58901;
DT 26-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT 26-JUL-2002, sequence version 1.
DT 01-MAY-2013, entry version 72.
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=XCC3327;
OS Xanthomonas campestris pv. campestris (strain ATCC 33913 / NCPPB 528 /
OS LMG 568).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Xanthomonas.
OX NCBI_TaxID=190485;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33913 / NCPPB 528 / LMG 568;
RX PubMed=12024217; DOI=10.1038/417459a;
RA da Silva A.C.R., Ferro J.A., Reinach F.C., Farah C.S., Furlan L.R.,
RA Quaggio R.B., Monteiro-Vitorello C.B., Van Sluys M.A.,
RA Almeida N.F. Jr., Alves L.M.C., do Amaral A.M., Bertolini M.C.,
RA Camargo L.E.A., Camarotte G., Cannavan F., Cardozo J., Chambergo F.,
RA Ciapina L.P., Cicarelli R.M.B., Coutinho L.L., Cursino-Santos J.R.,
RA El-Dorry H., Faria J.B., Ferreira A.J.S., Ferreira R.C.C.,
RA Ferro M.I.T., Formighieri E.F., Franco M.C., Greggio C.C., Gruber A.,
RA Katsuyama A.M., Kishi L.T., Leite R.P., Lemos E.G.M., Lemos M.V.F.,
RA Locali E.C., Machado M.A., Madeira A.M.B.N., Martinez-Rossi N.M.,
RA Martins E.C., Meidanis J., Menck C.F.M., Miyaki C.Y., Moon D.H.,
RA Moreira L.M., Novo M.T.M., Okura V.K., Oliveira M.C., Oliveira V.R.,
RA Pereira H.A., Rossi A., Sena J.A.D., Silva C., de Souza R.F.,
RA Spinola L.A.F., Takita M.A., Tamura R.E., Teixeira E.C., Tezza R.I.D.,
RA Trindade dos Santos M., Truffi D., Tsai S.M., White F.F.,
RA Setubal J.C., Kitajima J.P.;
RT "Comparison of the genomes of two Xanthomonas pathogens with differing
RT host specificities.";
RL Nature 417:459-463(2002).
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; AE008922; AAM42597.1; -; Genomic_DNA.
DR RefSeq; NP_638673.1; NC_003902.1.
DR ProteinModelPortal; P58901; -.
DR STRING; 190485.XCC3327; -.
DR EnsemblBacteria; AAM42597; AAM42597; XCC3327.
DR GeneID; 999518; -.
DR KEGG; xcc:XCC3327; -.
DR PATRIC; 24077743; VBIXanCam115730_3558.
DR eggNOG; COG0119; -.
DR HOGENOM; HOG000046859; -.
DR KO; K01649; -.
DR OMA; HKNAEEH; -.
DR ProtClustDB; PRK00915; -.
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; Reference proteome;
KW Transferase.
FT CHAIN 1 520 2-isopropylmalate synthase.
FT /FTId=PRO_0000140401.
SQ SEQUENCE 520 AA; 56222 MW; A8879B31E2E509D9 CRC64;
MNTTVSNQTP HIRIFDTTLR DGEQSPGCSM TPQQKLVMAR ALDALGVDII ETGFPASSYS
DREAVAMMGR ELRRPTLAVL SRCLQADIEI SARALEAAAN PRLHVFLSTS PLHREHKLRM
SREQVLESVH KHVTLARGYI DDIEFSAEDA TRTEEDFLAE VTRVAIAAGA TTINLPDTVG
FTTPEEIRGM FSRLIASVEG AEKVIFSTHC HNDLGLAAAN SLAAIEGGAR QVECTINGIG
ERAGNCALEE ITMALKVRGA FYNLDTAINT PRIVSTSQLL QRLVGMPVQR NKAVVGGNAF
AHESGIHQHG MLRHRGTYEI MRPEDVGWES SQMVLGRHSG RAAVEQRLRA LGYLLEEDEA
KLVFEQFKAL CEKQRVVTDA DLQALMQDAT VQEGYRLASM TISDVGSRAN ALVELSDPDG
NRVAETAQGN GPVDALFGAL ASATGVKLEL DSYQVHSVGI GADARGEASL SVRHDGVEYE
GTGTSKDIIE ASALAWLDVA NRLLRQRERG VVAGKTAAVA
//
