LEU1_NOSS1
ID LEU1_NOSS1 Reviewed; 531 AA.
AC P48575;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2002, sequence version 2.
DT 25-MAY-2022, entry version 123.
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=alr4840;
OS Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576).
OC Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Nostoc.
OX NCBI_TaxID=103690;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9139910; DOI=10.1128/jb.179.9.2930-2937.1997;
RA Stricker O., Masepohl B., Klipp W., Boehme H.;
RT "Identification and characterization of the nifV-nifZ-nifT gene region from
RT the filamentous cyanobacterium Anabaena sp. strain PCC 7120.";
RL J. Bacteriol. 179:2930-2937(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7120 / SAG 25.82 / UTEX 2576;
RX PubMed=11759840; DOI=10.1093/dnares/8.5.205;
RA Kaneko T., Nakamura Y., Wolk C.P., Kuritz T., Sasamoto S., Watanabe A.,
RA Iriguchi M., Ishikawa A., Kawashima K., Kimura T., Kishida Y., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakazaki N., Shimpo S., Sugimoto M.,
RA Takazawa M., Yamada M., Yasuda M., Tabata S.;
RT "Complete genomic sequence of the filamentous nitrogen-fixing
RT cyanobacterium Anabaena sp. strain PCC 7120.";
RL DNA Res. 8:205-213(2001).
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).
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 -!- PATHWAY: Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine
CC from 3-methyl-2-oxobutanoate: step 1/4.
CC -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the alpha-IPM synthase/homocitrate synthase
CC family. LeuA type 1 subfamily. {ECO:0000305}.
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DR EMBL; Z46907; CAA87005.1; -; Genomic_DNA.
DR EMBL; BA000019; BAB76539.1; -; Genomic_DNA.
DR PIR; AH2410; AH2410.
DR PIR; S52294; S52294.
DR RefSeq; WP_010998968.1; NZ_RSCN01000037.1.
DR AlphaFoldDB; P48575; -.
DR SMR; P48575; -.
DR STRING; 103690.17133977; -.
DR EnsemblBacteria; BAB76539; BAB76539; BAB76539.
DR KEGG; ana:alr4840; -.
DR eggNOG; COG0119; Bacteria.
DR OMA; NTMRMLV; -.
DR OrthoDB; 840579at2; -.
DR UniPathway; UPA00048; UER00070.
DR Proteomes; UP000002483; 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 Gene3D; 3.20.20.70; -; 1.
DR Gene3D; 3.30.160.270; -; 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; IPR036230; LeuA_allosteric_dom_sf.
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; SSF110921; 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 Leucine biosynthesis; Reference proteome; Transferase.
FT CHAIN 1..531
FT /note="2-isopropylmalate synthase"
FT /id="PRO_0000140327"
FT DOMAIN 8..284
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01151"
FT CONFLICT 416..423
FT /note="CGSNARPT -> AVAMHVQP (in Ref. 1; CAA87005)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 531 AA; 57762 MW; D45ED65407D0967C CRC64;
MTTKPEKIII FDTTLRDGEQ CPGATLNIDE KLAIAKQLAR LGVDIIEAGF AFASPGDFEA
VHKIAQTVGT QSGPVICSLA RARHDDIKAA AEAIKPAAKG RIHTFIATSD IHLQYKLKKT
RPEVIAIAEE MVAYAKSFTD DVEFSPEDAG RSDPEFLYQV LERAIAAGAT TINIPDTVGY
TTPSEFGAII KGIKENVPNI DQAIISVHGH NDLGLAVANF LEAVKNGARQ LECTINGIGE
RAGNAALEEL VMAMHVRRQY FNPFLGRHPD SEEALTNIDT KQIYKTSRLV SNLTGMLVQP
NKAIVGANAF AHESGIHQDG VLKNKLTYEI MDAQLIGLTD NQIVLGKHSG RNAFRTRLKE
LGFELSETEL NKAFVKFKEV ADKKKEISDW DLEAIVNDEI QQAPDLFRVE LVQVSCGSNA
RPTATVTLRT PDGEELTDAA IGTGPVDAVY KAINRVVNVP NQLIEFSVQS VTAGIDAIGE
VTIRLRYESR VFSGHAANTD IIVASAQAYV NALNRLYASL QTQDKQTEVT A