LEU1_SYNS3
ID LEU1_SYNS3 Reviewed; 540 AA.
AC Q0IBI3;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2006, sequence version 1.
DT 25-MAY-2022, entry version 97.
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=sync_0976;
OS Synechococcus sp. (strain CC9311).
OC Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus;
OC unclassified Synechococcus.
OX NCBI_TaxID=64471;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CC9311;
RX PubMed=16938853; DOI=10.1073/pnas.0602963103;
RA Palenik B., Ren Q., Dupont C.L., Myers G.S., Heidelberg J.F., Badger J.H.,
RA Madupu R., Nelson W.C., Brinkac L.M., Dodson R.J., Durkin A.S.,
RA Daugherty S.C., Sullivan S.A., Khouri H., Mohamoud Y., Halpin R.,
RA Paulsen I.T.;
RT "Genome sequence of Synechococcus CC9311: insights into adaptation to a
RT coastal environment.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:13555-13559(2006).
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; CP000435; ABI46602.1; -; Genomic_DNA.
DR RefSeq; WP_011618911.1; NC_008319.1.
DR AlphaFoldDB; Q0IBI3; -.
DR SMR; Q0IBI3; -.
DR STRING; 64471.sync_0976; -.
DR EnsemblBacteria; ABI46602; ABI46602; sync_0976.
DR KEGG; syg:sync_0976; -.
DR eggNOG; COG0119; Bacteria.
DR HOGENOM; CLU_022158_0_1_3; -.
DR OMA; NTMRMLV; -.
DR OrthoDB; 840579at2; -.
DR UniPathway; UPA00048; UER00070.
DR Proteomes; UP000001961; 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..540
FT /note="2-isopropylmalate synthase"
FT /id="PRO_1000149316"
FT DOMAIN 8..273
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01151"
SQ SEQUENCE 540 AA; 58010 MW; 89F700377AE0A81F CRC64;
MAKDPGRVLI FDTTLRDGEQ SPGASLNLEE KLAIAQQLAR LGVDVIEAGF PFASPGDFAA
VQRIAQQVGG ENGPIICGLA RASRGDIKAC ADAVAPAPKQ RIHTFIATSD IHLEHKLRKS
RKDVLGIVPE MVAYARSFVD DVEFSCEDAG RSDPEFLYEV IEAAISAGAS TVNIPDTVGY
TTPTEFGRLI EGINRNVPNI DEAVISVHGH NDLGLAVANF LEAVKSGARQ LECTVNGIGE
RAGNAALEEL VMAMHVRRRY FNPFFGRDED SPTPLTAVRT EEITKTSRLV SNLTGMVVQP
NKAIVGANAF AHESGIHQDG VLKNRLTYEI VDARTVGLTD NRISLGKLSG RSAVRARLEE
LGYDLSREDL DDAFARFKDL ADRKREITDR DLESIVSVQV QQPDAKYQLK LVQVSCGSSL
QPTATVTLAD ENGQEQTAAS VGTGPVDAVC RSLNQLAGEP NELVEFSVKS VTEGIDAMGD
VTIRLRRDGQ LYSGHSAHTD VVVAAAEAFV NALNRLVAGT AGPTIHPQLD MAQLDSSPVH