ID A8LYI4_SALAI Unreviewed; 584 AA.
AC A8LYI4;
DT 04-DEC-2007, integrated into UniProtKB/TrEMBL.
DT 04-DEC-2007, sequence version 1.
DT 01-MAY-2013, entry version 39.
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=Sare_0263;
OS Salinispora arenicola (strain CNS-205).
OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC Micromonosporineae; Micromonosporaceae; Salinispora.
OX NCBI_TaxID=391037;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CNS-205;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T.,
RA Dalin E., Tice H., Pitluck S., Foster B., Schmutz J., Larimer F.,
RA Land M., Hauser L., Kyrpides N., Ivanova N., Jensen P.R., Moore B.S.,
RA Penn K., Jenkins C., Udwary D., Xiang L., Gontang E., Richardson P.;
RT "Complete sequence of Salinispora arenicola CNS-205.";
RL Submitted (OCT-2007) 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 2 subfamily.
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DR EMBL; CP000850; ABV96195.1; -; Genomic_DNA.
DR RefSeq; YP_001535186.1; NC_009953.1.
DR ProteinModelPortal; A8LYI4; -.
DR SMR; A8LYI4; 1-582.
DR STRING; 391037.Sare_0263; -.
DR EnsemblBacteria; ABV96195; ABV96195; Sare_0263.
DR GeneID; 5705278; -.
DR KEGG; saq:Sare_0263; -.
DR PATRIC; 23428959; VBISalAre38676_0269.
DR eggNOG; COG0119; -.
DR HOGENOM; HOG000110941; -.
DR KO; K01649; -.
DR OMA; QIDFSDI; -.
DR ProtClustDB; CLSK968554; -.
DR BioCyc; SARE391037:GH66-310-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_00572; LeuA_type2; 1; -.
DR InterPro; IPR013709; 2-isopropylmalate_synth_dimer.
DR InterPro; IPR002034; AIPM/Hcit_synth_CS.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR005668; IPM_Synthase.
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; TIGR00970; leuA_yeast; 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 Acyltransferase; Amino-acid biosynthesis;
KW Branched-chain amino acid biosynthesis; Complete proteome;
KW Leucine biosynthesis; Transferase.
SQ SEQUENCE 584 AA; 64882 MW; 49130E0D426E81E9 CRC64;
MAHPAVTPDA ETDPIARQQP SRMPYHRYQP YQQQFRTDLP DRSWPNRRVE TAPRWCAVDL
RDGNQALIDP MSPERKRRMF QLLVQLGYKE IEVGFPSASQ SDFDFVRQLI EQDLIPDDVT
IQVLTQCREH LIDRTFAALR GAKRAIVHFY NSTSTLQRRV VFGLDRDGIT DIATTGARLC
QKYAEIHTPD TDIHYEYSPE SYTGTELDYA LEVCAKVIEV VDPTPDHRLI VNLPATVEMA
MPNVYADSIE WMHRHLPRRD SLVLSLHPHN DRGTGVAAAE LGLLAGADRI EGCLFGNGER
TGNVDLVTLG LNLFSQGIDP MIDFSNIDEI KRTVEYCNQL PVHERHPYVG DLVYTAFSGS
HQDAIKKGFD ALSADAATAG VPVEKHSWAV PYLPIDPKDL GRTYEAVIRV NSQSGKGGVA
YVMQTEHQLD LPRRLQIEFS GVVQQVTDND GGEVDPQTMW EIFAGQYLLD HQTNPSVTLT
DYTLATVDGK VEFEAVVGYD GERHTVTAVG NGPVDAYVNA LQSLGVNVRV LDYHEHALSS
GGDAQAAAYV ECEVDGRTVW GAGVDANIVT ATIRAVTSAV NRTR
//
