LEU1_STRCO
ID LEU1_STRCO Reviewed; 573 AA.
AC O31046; Q9L2F5; Q9L2L9;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2002, sequence version 2.
DT 25-MAY-2022, entry version 133.
DE RecName: Full=2-isopropylmalate synthase {ECO:0000255|HAMAP-Rule:MF_00572};
DE EC=2.3.3.13 {ECO:0000255|HAMAP-Rule:MF_00572};
DE AltName: Full=Alpha-IPM synthase {ECO:0000255|HAMAP-Rule:MF_00572};
DE AltName: Full=Alpha-isopropylmalate synthase {ECO:0000255|HAMAP-Rule:MF_00572};
GN Name=leuA {ECO:0000255|HAMAP-Rule:MF_00572}; OrderedLocusNames=SCO2528;
GN ORFNames=SCC117.01c, SCC121.31c;
OS Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145).
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces; Streptomyces albidoflavus group.
OX NCBI_TaxID=100226;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=A3(2) / D132;
RX PubMed=10517590; DOI=10.1099/00221287-145-9-2375;
RA Craster H.L., Potter C.A., Baumberg S.;
RT "End-product control of expression of branched-chain amino acid
RT biosynthesis genes in Streptomyces coelicolor A3(2): paradoxical
RT relationships between DNA sequence and regulatory phenotype.";
RL Microbiology 145:2375-2384(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-471 / A3(2) / M145;
RX PubMed=12000953; DOI=10.1038/417141a;
RA Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L.,
RA Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D.,
RA Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A.,
RA Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S., Huang C.-H.,
RA Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S., Rabbinowitsch E.,
RA Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Saunders D.,
RA Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A.,
RA Woodward J.R., Barrell B.G., Parkhill J., Hopwood D.A.;
RT "Complete genome sequence of the model actinomycete Streptomyces coelicolor
RT A3(2).";
RL Nature 417:141-147(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:0000255|HAMAP-
CC Rule:MF_00572}.
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 Evidence={ECO:0000255|HAMAP-Rule:MF_00572};
CC -!- PATHWAY: Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine
CC from 3-methyl-2-oxobutanoate: step 1/4. {ECO:0000255|HAMAP-
CC Rule:MF_00572}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_00572}.
CC -!- SIMILARITY: Belongs to the alpha-IPM synthase/homocitrate synthase
CC family. LeuA type 2 subfamily. {ECO:0000255|HAMAP-Rule:MF_00572}.
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DR EMBL; AF026444; AAB82586.1; -; Genomic_DNA.
DR EMBL; AL939113; CAD55194.1; -; Genomic_DNA.
DR RefSeq; NP_733575.1; NC_003888.3.
DR RefSeq; WP_003976275.1; NZ_VNID01000001.1.
DR AlphaFoldDB; O31046; -.
DR SMR; O31046; -.
DR STRING; 100226.SCO2528; -.
DR GeneID; 1097962; -.
DR KEGG; sco:SCO2528; -.
DR PATRIC; fig|100226.15.peg.2573; -.
DR eggNOG; COG0119; Bacteria.
DR HOGENOM; CLU_004588_3_0_11; -.
DR InParanoid; O31046; -.
DR OMA; FGQGERT; -.
DR PhylomeDB; O31046; -.
DR UniPathway; UPA00048; UER00070.
DR Proteomes; UP000001973; Chromosome.
DR GO; GO:0003852; F:2-isopropylmalate synthase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0009098; P:leucine biosynthetic process; IEA:UniProtKB-UniRule.
DR CDD; cd07942; DRE_TIM_LeuA; 1.
DR Gene3D; 3.20.20.70; -; 1.
DR Gene3D; 3.30.160.270; -; 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; IPR036230; LeuA_allosteric_dom_sf.
DR InterPro; IPR039371; LeuA_N_DRE-TIM.
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; SSF110921; 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 Amino-acid biosynthesis; Branched-chain amino acid biosynthesis;
KW Leucine biosynthesis; Reference proteome; Transferase.
FT CHAIN 1..573
FT /note="2-isopropylmalate synthase"
FT /id="PRO_0000140444"
FT DOMAIN 37..314
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01151"
FT CONFLICT 74
FT /note="E -> V (in Ref. 1; AAB82586)"
FT /evidence="ECO:0000305"
FT CONFLICT 135
FT /note="Y -> F (in Ref. 1; AAB82586)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 573 AA; 63323 MW; 4CD2AE8646811F74 CRC64;
MANRQQPSPM PTAKYRGYDQ VDIADRTWPN QRITTAPRWL STDLRDGNQA LIDPMSPVRK
RAMFDLLVKM GYKEIEVGFP ASGQTDFDFV RSIIEEPGAI PDDVTISVLT QAREDLIERT
VESLKGARRA TVHLYNATAP VFRRVVFRGS RDDIKQIAVD GTRLVMEYAE KLLGPETEFG
YQYSPEIFTD TELDFALEVC EAVMDTYQPG PGREIILNLP ATVERSTPST HADRFEWMGR
NLSRREHVCL SVHPHNDRGT AVAAAELALM AGADRIEGCL FGQGERTGNV DLVTLGMNLF
SQGVDPQIDF SDIDEIRRTW EYCNQMEVHP RHPYVGDLVY TSFSGSHQDA IKKGFDAMEA
DAAARGVTVD DIEWAVPYLP IDPKDVGRSY EAVIRVNSQS GKGGIAYVLK NDHSLDLPRR
MQIEFSKLIQ AKTDAEGGEI TPTAIWDVFQ DEYLPNPDNP WGRIQVANGQ TTTDRDGVDT
LTVDATVDGA ETTLVGSGNG PISAFFHALQ GVGIDVRLLD YQEHTMSEGA SAQAASYIEC
AIGDKVLWGI GIDANTTRAS LKAVVSAVNR ATR
