LEU1_SYNP2
ID LEU1_SYNP2 Reviewed; 533 AA.
AC B1XLQ9;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-2008, sequence version 1.
DT 25-MAY-2022, entry version 92.
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};
GN OrderedLocusNames=SYNPCC7002_A1356;
OS Synechococcus sp. (strain ATCC 27264 / PCC 7002 / PR-6) (Agmenellum
OS quadruplicatum).
OC Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus;
OC unclassified Synechococcus.
OX NCBI_TaxID=32049;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27264 / PCC 7002 / PR-6;
RA Li T., Zhao J., Zhao C., Liu Z., Zhao F., Marquardt J., Nomura C.T.,
RA Persson S., Detter J.C., Richardson P.M., Lanz C., Schuster S.C., Wang J.,
RA Li S., Huang X., Cai T., Yu Z., Luo J., Zhao J., Bryant D.A.;
RT "Complete sequence of Synechococcus sp. PCC 7002.";
RL Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
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; CP000951; ACA99352.1; -; Genomic_DNA.
DR RefSeq; WP_012306975.1; NC_010475.1.
DR AlphaFoldDB; B1XLQ9; -.
DR SMR; B1XLQ9; -.
DR STRING; 32049.SYNPCC7002_A1356; -.
DR PRIDE; B1XLQ9; -.
DR EnsemblBacteria; ACA99352; ACA99352; SYNPCC7002_A1356.
DR KEGG; syp:SYNPCC7002_A1356; -.
DR eggNOG; COG0119; Bacteria.
DR HOGENOM; CLU_022158_0_1_3; -.
DR OMA; NTMRMLV; -.
DR UniPathway; UPA00048; UER00070.
DR Proteomes; UP000001688; 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..533
FT /note="2-isopropylmalate synthase"
FT /id="PRO_1000149313"
FT DOMAIN 8..269
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01151"
SQ SEQUENCE 533 AA; 57650 MW; 54309D752D66DC5E CRC64;
MNNQDDRIII FDTTLRDGEQ SPGATLNGDE KLAIARALAR LGVDVIEAGF PRASRGDFDA
VQRIAAEVGT ENGPTICGLA RATKGDIEAA GNALKPAFSN RIHTFIATSD IHLEYKLRKS
RKDVLAIAPE MVAYAKTFTN DVEFSPEDAG RSDPEFLYQI LEAVIDAGAT TVNIPDTVGY
TTPAEFGALI KGIKENVPNI DRAIISVHGH NDLGLAVANF LEAVKNGARQ LECTINGIGE
RAGNAALEEL VMALHVRRQY YNPFLGRPAD SEAPLTSINT KEIYKTSRLV SNLTGLSVQA
NKAIVGLNAF AHESGIHQDG VLKNKLTYEI MDAQSIGLTD NQIILGKHSG RNAFRTRLAE
LGFDLSDNDL NKAFLRFKDL ADKKKEITDW DLEAIVKDET QQPPELFRLE LVQVSCGDHA
QPTATITIRT PGGKELTDAA IGTGPVDAIY KAINRVVQVP NELIEYSVQS VTAGIDAIGE
VTIRLRHEGR IYSGHAANTD IVVASARAYI SALNRLYAAL QEDVSANPAK ASL