LEU1_PYRAB
ID LEU1_PYRAB Reviewed; 486 AA.
AC Q9UZ08; G8ZHF5;
DT 26-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 112.
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=PYRAB13490; ORFNames=PAB0890;
OS Pyrococcus abyssi (strain GE5 / Orsay).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=272844;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GE5 / Orsay;
RX PubMed=12622808; DOI=10.1046/j.1365-2958.2003.03381.x;
RA Cohen G.N., Barbe V., Flament D., Galperin M., Heilig R., Lecompte O.,
RA Poch O., Prieur D., Querellou J., Ripp R., Thierry J.-C., Van der Oost J.,
RA Weissenbach J., Zivanovic Y., Forterre P.;
RT "An integrated analysis of the genome of the hyperthermophilic archaeon
RT Pyrococcus abyssi.";
RL Mol. Microbiol. 47:1495-1512(2003).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=GE5 / Orsay;
RX PubMed=22057919; DOI=10.1007/s00284-011-0035-x;
RA Gao J., Wang J.;
RT "Re-annotation of two hyperthermophilic archaea Pyrococcus abyssi GE5 and
RT Pyrococcus furiosus DSM 3638.";
RL Curr. Microbiol. 64:118-129(2012).
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:0000250}.
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 -!- SIMILARITY: Belongs to the alpha-IPM synthase/homocitrate synthase
CC family. LeuA type 1 subfamily. {ECO:0000305}.
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DR EMBL; AJ248287; CAB50254.1; -; Genomic_DNA.
DR EMBL; HE613800; CCE70792.1; -; Genomic_DNA.
DR PIR; A75045; A75045.
DR RefSeq; WP_010868464.1; NC_000868.1.
DR AlphaFoldDB; Q9UZ08; -.
DR SMR; Q9UZ08; -.
DR STRING; 272844.PAB0890; -.
DR EnsemblBacteria; CAB50254; CAB50254; PAB0890.
DR GeneID; 1496738; -.
DR KEGG; pab:PAB0890; -.
DR PATRIC; fig|272844.11.peg.1435; -.
DR eggNOG; arCOG02092; Archaea.
DR HOGENOM; CLU_022158_0_1_2; -.
DR OMA; NTMRMLV; -.
DR OrthoDB; 10632at2157; -.
DR PhylomeDB; Q9UZ08; -.
DR UniPathway; UPA00048; UER00070.
DR Proteomes; UP000000810; Chromosome.
DR Proteomes; UP000009139; 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; Transferase.
FT CHAIN 1..486
FT /note="2-isopropylmalate synthase"
FT /id="PRO_0000140418"
FT DOMAIN 4..266
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01151"
SQ SEQUENCE 486 AA; 53768 MW; 721D5B4724CC49B2 CRC64;
MRKVYIFDTT LRDGEQTPGV SLTVEEKVEI AKQLAKLNVD VIEAGFPIAS EGEFKAVKKI
ATEVEDPTIA ALARAVEKDI DRAGEALRNA EKNRIHTFIA TSPIHMKYKL RKEPEEVKKL
AVKAVEHATK YTEDVEFSAE DATRSDWDFL VEVYEAVIDA GATVINVPDT VGYATPEEFY
ELVRYLRRNI SNIKGVQISV HCHDDLGLAV ANSLSAIRAG ADQVEVTVNG IGERAGNAAL
EEVIVALDVR RDFYKVKTDV NLKEIARTSK LVSHLTGIEV PPNKAIVGGN AFAHESGIHQ
DGVLKERTTY EIIDPKKLGF SGSKIVLGKH SGRHAFRKKL EELGYSLTEE HLERAFKKFK
DIADRKRWIT DTDIEAIIQE ELTKSNGKLK VEIIHVTSGK VSTATVRISM NGEERIEVAW
FKNGPIDALF SAINKALGEE FKLREYRVSS VTSGKDSLGE VLVRVEVNGE IFVGRGLSTD
IIEASA
