LEU1_GEOSE
ID LEU1_GEOSE Reviewed; 515 AA.
AC Q8RL85;
DT 26-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 25-MAY-2022, entry version 70.
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};
OS Geobacillus stearothermophilus (Bacillus stearothermophilus).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus.
OX NCBI_TaxID=1422;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 29609 / DSM 2027 / NCA 1503 / NCIMB 8924;
RX PubMed=14702326; DOI=10.1128/jb.186.2.570-574.2004;
RA Porat I., Vinogradov M., Vyazmensky M., Lu C.-D., Chipman D.M.,
RA Abdelal A.T., Barak Z.;
RT "Cloning and characterization of acetohydroxyacid synthase from Bacillus
RT stearothermophilus.";
RL J. Bacteriol. 186:570-574(2004).
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 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; AY083837; AAL99359.1; -; Genomic_DNA.
DR AlphaFoldDB; Q8RL85; -.
DR SMR; Q8RL85; -.
DR UniPathway; UPA00048; UER00070.
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; PS50991; PYR_CT; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis; Branched-chain amino acid biosynthesis;
KW Leucine biosynthesis; Transferase.
FT CHAIN 1..515
FT /note="2-isopropylmalate synthase"
FT /id="PRO_0000140331"
FT DOMAIN 4..266
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01151"
SQ SEQUENCE 515 AA; 57033 MW; C765B253EF4F42FD CRC64;
MRNIKFFDTT LRDGEQSAGV NLNLQEKLEI ARQLERLRVD IIEAGFPASS KGDFEAVKQI
AETVRTCSVT GLSRSVRSDI DAAWEALKGG AEPRLHLFIA TSPIHMVHKL RMTPEQVIEA
AVEAVKYAKR FFPIVQWSAE DACRSELPFL AKIVAEVIKA GASVINIPDT VGYITPKEYG
EIFLYLQNNV QNIENVSLSA HCHDDLGMAV VNSLSAIEHG ATQVECTING IGERAGNAAL
EEIAVALHIR KDYYQVETRL NLQEIKRTSN LVSKLTGVVV PPNKAVVGKN AFAHESGIHQ
DGVLKEKTTY EIISPELVGV PSNSMVLGKN SGRHALRYRV EELGYTLSDE EINQLFVRFK
ELADKKKDIT DDDLIALIFE EKFDHFKDFY QLSSIQVQYG TNQIPTAVVV LKYGKGNEIQ
EAATGSGSVY ALYNTLERCF QTEVTLLDYR IESVGGGRDA LAQVFVKVRV RDVETSGRGT
AQDVLEASAK AYINAMNRVF MIEAMRAENE KVATS
