LEU1_GLOVI
ID LEU1_GLOVI Reviewed; 538 AA.
AC Q7NI93;
DT 15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=2-isopropylmalate synthase {ECO:0000255|HAMAP-Rule:MF_01025};
DE EC=2.3.3.13 {ECO:0000255|HAMAP-Rule:MF_01025};
DE AltName: Full=Alpha-IPM synthase {ECO:0000255|HAMAP-Rule:MF_01025};
DE AltName: Full=Alpha-isopropylmalate synthase {ECO:0000255|HAMAP-Rule:MF_01025};
GN Name=leuA {ECO:0000255|HAMAP-Rule:MF_01025}; OrderedLocusNames=gll2290;
OS Gloeobacter violaceus (strain ATCC 29082 / PCC 7421).
OC Bacteria; Cyanobacteria; Gloeobacteria; Gloeobacterales; Gloeobacteraceae;
OC Gloeobacter.
OX NCBI_TaxID=251221;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29082 / PCC 7421;
RX PubMed=14621292; DOI=10.1093/dnares/10.4.137;
RA Nakamura Y., Kaneko T., Sato S., Mimuro M., Miyashita H., Tsuchiya T.,
RA Sasamoto S., Watanabe A., Kawashima K., Kishida Y., Kiyokawa C., Kohara M.,
RA Matsumoto M., Matsuno A., Nakazaki N., Shimpo S., Takeuchi C., Yamada M.,
RA Tabata S.;
RT "Complete genome structure of Gloeobacter violaceus PCC 7421, a
RT cyanobacterium that lacks thylakoids.";
RL DNA Res. 10:137-145(2003).
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_01025}.
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_01025};
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_01025}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_01025}.
CC -!- SIMILARITY: Belongs to the alpha-IPM synthase/homocitrate synthase
CC family. LeuA type 1 subfamily. {ECO:0000255|HAMAP-Rule:MF_01025}.
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DR EMBL; BA000045; BAC90231.1; -; Genomic_DNA.
DR RefSeq; NP_925236.1; NC_005125.1.
DR RefSeq; WP_011142287.1; NC_005125.1.
DR AlphaFoldDB; Q7NI93; -.
DR SMR; Q7NI93; -.
DR STRING; 251221.35212858; -.
DR PRIDE; Q7NI93; -.
DR EnsemblBacteria; BAC90231; BAC90231; BAC90231.
DR KEGG; gvi:gll2290; -.
DR PATRIC; fig|251221.4.peg.2326; -.
DR eggNOG; COG0119; Bacteria.
DR HOGENOM; CLU_022158_0_1_3; -.
DR InParanoid; Q7NI93; -.
DR OMA; NTMRMLV; -.
DR OrthoDB; 840579at2; -.
DR PhylomeDB; Q7NI93; -.
DR UniPathway; UPA00048; UER00070.
DR Proteomes; UP000000557; 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..538
FT /note="2-isopropylmalate synthase"
FT /id="PRO_0000140354"
FT DOMAIN 6..277
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01151"
SQ SEQUENCE 538 AA; 58035 MW; 9CF8C28EE4292178 CRC64;
MFQDRLIIFD TTLRDGEQSP GATLNADEKV EIARQLARLG VDVIEAGFAY ASPGDFEAVE
RVARTVGTED GPVICSLARA IRSDIQAAAE AIRPAARGRI HTFISTSDIH LEHQLRKSRA
EVLAIAAEMV AFAKGFVDDV EFSPMDAGRS APEYLYRVLE AAIAAGATTV NIPDTVGYLT
PAEFGGLIRG ITQNVRGIER AVISVHCHND LGLAVANSLA AIENGARQIE CTVNGIGERA
GNCSLEEIVM ALHVRRQFFN PIFGRPADST VPLSTIDTRQ IYKSSRLVSH LTGMLVQPNK
AIVGANAFAH ESGIHQDGVL KNRLTYEIMD AETVGVNENR IVLGKHSGRN AFRTRLVELG
YELGDADLNR AFLRFKELAD KKKTVSDWDI EAVISDEIRL IPEAYRLEQV QVSCGEPGLP
TATVRLTGPD GVERVDAAVG TGPVDAVYKA INRLIELPNE LIEFSVQSVT AGIDAMGEVT
IRVRQDGRTF SGHAANTDII VASARAYLNA LNKLHFALAH PTHSGGALAH PDAAAQKL
