LEU1_RIPO1
ID LEU1_RIPO1 Reviewed; 536 AA.
AC B7JYP4;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 1.
DT 25-MAY-2022, entry version 69.
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=PCC8801_0832;
OS Rippkaea orientalis (strain PCC 8801) (Cyanothece sp. (strain PCC 8801)).
OC Bacteria; Cyanobacteria; Oscillatoriophycideae; Chroococcales;
OC Aphanothecaceae; Rippkaea; Rippkaea orientalis.
OX NCBI_TaxID=41431;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 8801;
RX PubMed=21972240; DOI=10.1128/mbio.00214-11;
RA Bandyopadhyay A., Elvitigala T., Welsh E., Stockel J., Liberton M., Min H.,
RA Sherman L.A., Pakrasi H.B.;
RT "Novel metabolic attributes of the genus Cyanothece, comprising a group of
RT unicellular nitrogen-fixing Cyanobacteria.";
RL MBio 2:E214-E214(2011).
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; CP001287; ACK64914.1; -; Genomic_DNA.
DR RefSeq; WP_012594190.1; NC_011726.1.
DR AlphaFoldDB; B7JYP4; -.
DR SMR; B7JYP4; -.
DR STRING; 41431.PCC8801_0832; -.
DR EnsemblBacteria; ACK64914; ACK64914; PCC8801_0832.
DR KEGG; cyp:PCC8801_0832; -.
DR eggNOG; COG0119; Bacteria.
DR HOGENOM; CLU_022158_0_1_3; -.
DR OMA; NTMRMLV; -.
DR OrthoDB; 840579at2; -.
DR UniPathway; UPA00048; UER00070.
DR Proteomes; UP000008204; 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..536
FT /note="2-isopropylmalate synthase"
FT /id="PRO_1000149174"
FT DOMAIN 8..269
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01151"
SQ SEQUENCE 536 AA; 58285 MW; 43198448585700A2 CRC64;
MSNQPDRIII FDTTLRDGEQ SPGASLTVEE KLTIARSLAR LGVDIIEAGF PYASPGDFEA
VQKIAQTVGT EDGPRICGLA RATQKDIQTA AEAVKPAAKG RIHTFLATSD IHLQYKLKKT
RQEVLAIVPD MVAYAKSLVD DVEFSPEDAG RSDPEFLYQV LERAIAAGAT TINIPDTVGY
TTPSEFGALI GGIKQNVPNI DQAIISVHGH NDLGLAVANF LEAVKNGARQ LECTINGIGE
RAGNAALEEL VMALHVRRQY FNPFLGRPPE STEPLTNINT KEIYRTSRLV SQLTGMMVQP
NKAIVGKNAF AHESGIHQDG VLKNKLTYEI MDAESIGLTH NQIVLGKLSG RNAFRTRLKE
LGFELSDTEI NNAFLRFKEV ADKKKEITDW DLAAIVNDEM QQAPELFRLE LVQVSCGDHA
CPTATVTLRT PDGQELTDAA IGTGPVDAVY KAINRVVQVP NELIEFSVKS VTAGIDAMGE
VTIRLRYEDK IYSGYAANTD IITASARAYI SALNRLYGSI QDQSATEVTK SEVAAI