ID C3TQV7_ECOLX Unreviewed; 523 AA.
AC C3TQV7;
DT 16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT 16-JUN-2009, sequence version 1.
DT 27-MAR-2024, entry version 115.
DE RecName: Full=2-isopropylmalate synthase {ECO:0000256|ARBA:ARBA00018198, ECO:0000256|HAMAP-Rule:MF_01025};
DE EC=2.3.3.13 {ECO:0000256|ARBA:ARBA00012973, ECO:0000256|HAMAP-Rule:MF_01025};
DE AltName: Full=Alpha-IPM synthase {ECO:0000256|ARBA:ARBA00029993, ECO:0000256|HAMAP-Rule:MF_01025};
DE AltName: Full=Alpha-isopropylmalate synthase {ECO:0000256|HAMAP-Rule:MF_01025};
GN Name=leuA {ECO:0000256|HAMAP-Rule:MF_01025,
GN ECO:0000313|EMBL:EFE8674061.1};
GN ORFNames=BK383_14080 {ECO:0000313|EMBL:OJR54345.1}, C9E67_25720
GN {ECO:0000313|EMBL:QCL50243.1}, CY655_00400
GN {ECO:0000313|EMBL:AZZ24661.1}, DU321_03180
GN {ECO:0000313|EMBL:RRL50889.1}, ECs0078 {ECO:0000313|EMBL:ACI71659.1},
GN F7N46_13085 {ECO:0000313|EMBL:EFE8674061.1}, FKO60_12840
GN {ECO:0000313|EMBL:TZE48506.1}, HJQ60_000784
GN {ECO:0000313|EMBL:HAI5330860.1}, HL563_03205
GN {ECO:0000313|EMBL:HAJ0832757.1}, NCTC12950_04521
GN {ECO:0000313|EMBL:STP52960.1};
OS Escherichia coli.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=562 {ECO:0000313|EMBL:ACI71659.1};
RN [1] {ECO:0000313|EMBL:ACI71659.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=493/89 {ECO:0000313|EMBL:ACI71659.1}, 86-24
RC {ECO:0000313|EMBL:ACI71660.1}, 87-14 {ECO:0000313|EMBL:ACI71661.1},
RC TB182A {ECO:0000313|EMBL:ACI71662.1}, and TW14359
RC {ECO:0000313|EMBL:ACI71663.1};
RX PubMed=19439656; DOI=10.1073/pnas.0812949106;
RA Leopold S.R., Magrini V., Holt N.J., Shaikh N., Mardis E.R., Cagno J.,
RA Ogura Y., Iguchi A., Hayashi T., Mellmann A., Karch H., Besser T.E.,
RA Sawyer S.A., Whittam T.S., Tarr P.I.;
RT "A precise reconstruction of the emergence and constrained radiations of
RT Escherichia coli O157 portrayed by backbone concatenomic analysis.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:8713-8718(2009).
RN [2] {ECO:0000313|EMBL:OJR54345.1, ECO:0000313|Proteomes:UP000184277}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=570 {ECO:0000313|EMBL:OJR54345.1,
RC ECO:0000313|Proteomes:UP000184277};
RA Wang Y., Zhang R., Li J., Wu Z., Wenjuan Y., Schwarz S., Tyrrell J.,
RA Zheng Y., Wang S., Shen Z., Liu Z., Lei L., Li M., Zhang Q., Wu C.,
RA Zhang Q., Wu Y., Walsh T., Shen J.;
RT "Comprehensive resistome analysis reveals the prevalence of NDM and MCR-1
RT in Chinese poultry production.";
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:AZZ24661.1, ECO:0000313|Proteomes:UP000284592}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=E-1246 {ECO:0000313|EMBL:AZZ24661.1,
RC ECO:0000313|Proteomes:UP000284592};
RA Bikkarolla S.K., Nordberg V., Kabir M.H., Muller V., Fritzsche J.,
RA Ambjornsson T., Giske C.G., Naver L., Sandegren L., Westerlund F.;
RT "Combining optical DNA mapping and long-read sequencing for full genomic
RT characterization of plasmids in a nosocomial resistance outbreak.";
RL Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|EMBL:HAI5330860.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AMC_487 {ECO:0000313|EMBL:HAI5330860.1}, and EC00618
RC {ECO:0000313|EMBL:HAJ0832757.1};
RX PubMed=30286803;
RA Souvorov A., Agarwala R., Lipman D.J.;
RT "SKESA: strategic k-mer extension for scrupulous assemblies.";
RL Genome Biol. 19:153-153(2018).
RN [5] {ECO:0000313|EMBL:QCL50243.1, ECO:0000313|Proteomes:UP000298553}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=143 {ECO:0000313|EMBL:QCL50243.1,
RC ECO:0000313|Proteomes:UP000298553};
RA Bono J.L., Arthur T.M.;
RT "WGA of Escherichia coli O157:H7: comparison of multiple isolates.";
RL Submitted (APR-2018) to the EMBL/GenBank/DDBJ databases.
RN [6] {ECO:0000313|EMBL:STP52960.1, ECO:0000313|Proteomes:UP000255454}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC12950 {ECO:0000313|EMBL:STP52960.1,
RC ECO:0000313|Proteomes:UP000255454};
RG Pathogen Informatics;
RA Doyle S.;
RL Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
RN [7] {ECO:0000313|EMBL:RRL50889.1, ECO:0000313|Proteomes:UP000272662}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UMB1727 {ECO:0000313|EMBL:RRL50889.1,
RC ECO:0000313|Proteomes:UP000272662};
RA Garretto A., Miller-Ensminger T., Wolfe A.J., Putonti C.;
RT "E. coli isolates of the female bladder.";
RL Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
RN [8] {ECO:0000313|EMBL:TZE48506.1, ECO:0000313|Proteomes:UP000324120}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=347 {ECO:0000313|EMBL:TZE48506.1,
RC ECO:0000313|Proteomes:UP000324120};
RA Cormier A.C., Chalmer G., Cook S.R., Zaheer R., Hannon S.J., Booker C.W.,
RA Read R., Gow S.P., Mcallister T.A., Boerlin P.;
RT "The presence and diversity of blaCTX-M among Escherichia coli from urban
RT wastewater and feedlot cattle, in Alberta, Canada.";
RL Submitted (JUN-2019) to the EMBL/GenBank/DDBJ databases.
RN [9] {ECO:0000313|EMBL:EFE8674061.1, ECO:0000313|Proteomes:UP000533482}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FSIS11923834 {ECO:0000313|EMBL:EFE8674061.1,
RC ECO:0000313|Proteomes:UP000533482};
RG NARMS: The National Antimicrobial Resistance Monitoring System;
RL Submitted (SEP-2019) to the EMBL/GenBank/DDBJ databases.
RN [10] {ECO:0000313|EMBL:HAI5330860.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=AMC_487 {ECO:0000313|EMBL:HAI5330860.1}, and EC00618
RC {ECO:0000313|EMBL:HAJ0832757.1};
RG NCBI Pathogen Detection Project;
RL Submitted (MAR-2020) 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-ketoisovalerate) to form 3-carboxy-3-
CC hydroxy-4-methylpentanoate (2-isopropylmalate).
CC {ECO:0000256|ARBA:ARBA00037629, ECO:0000256|HAMAP-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:0000256|HAMAP-Rule:MF_01025};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01025};
CC -!- PATHWAY: Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine
CC from 3-methyl-2-oxobutanoate: step 1/4. {ECO:0000256|ARBA:ARBA00004689,
CC ECO:0000256|HAMAP-Rule:MF_01025}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01025}.
CC -!- SIMILARITY: Belongs to the alpha-IPM synthase/homocitrate synthase
CC family. LeuA type 1 subfamily. {ECO:0000256|ARBA:ARBA00009396,
CC ECO:0000256|HAMAP-Rule:MF_01025}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; EU906545; ACI71659.1; -; Genomic_DNA.
DR EMBL; EU906546; ACI71660.1; -; Genomic_DNA.
DR EMBL; EU906547; ACI71661.1; -; Genomic_DNA.
DR EMBL; EU906548; ACI71662.1; -; Genomic_DNA.
DR EMBL; EU906549; ACI71663.1; -; Genomic_DNA.
DR EMBL; CP025573; AZZ24661.1; -; Genomic_DNA.
DR EMBL; AASOHJ010000014; EFE8674061.1; -; Genomic_DNA.
DR EMBL; DABERK010000003; HAI5330860.1; -; Genomic_DNA.
DR EMBL; DABGYN010000002; HAJ0832757.1; -; Genomic_DNA.
DR EMBL; MOKI01000027; OJR54345.1; -; Genomic_DNA.
DR EMBL; CP028607; QCL50243.1; -; Genomic_DNA.
DR EMBL; RRVG01000002; RRL50889.1; -; Genomic_DNA.
DR EMBL; UGFM01000001; STP52960.1; -; Genomic_DNA.
DR EMBL; VHKY01000007; TZE48506.1; -; Genomic_DNA.
DR RefSeq; WP_000082847.1; NZ_WXYZ01000001.1.
DR GeneID; 75169974; -.
DR PATRIC; fig|562.6969.peg.4153; -.
DR OMA; NTMRMLV; -.
DR UniPathway; UPA00048; UER00070.
DR Proteomes; UP000184277; Unassembled WGS sequence.
DR Proteomes; UP000255454; Unassembled WGS sequence.
DR Proteomes; UP000272662; Unassembled WGS sequence.
DR Proteomes; UP000284592; Chromosome.
DR Proteomes; UP000298553; Chromosome.
DR Proteomes; UP000324120; Unassembled WGS sequence.
DR Proteomes; UP000533482; Unassembled WGS sequence.
DR Proteomes; UP000845800; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-UniRule.
DR GO; GO:0003852; F:2-isopropylmalate synthase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0003985; F:acetyl-CoA C-acetyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0009098; P:leucine biosynthetic process; IEA:UniProtKB-UniRule.
DR CDD; cd07940; DRE_TIM_IPMS; 1.
DR Gene3D; 1.10.238.260; -; 1.
DR Gene3D; 3.30.160.270; -; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 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 NCBIfam; TIGR00973; leuA_bact; 1.
DR PANTHER; PTHR10277:SF9; 2-ISOPROPYLMALATE SYNTHASE 1, CHLOROPLASTIC-RELATED; 1.
DR PANTHER; PTHR10277; HOMOCITRATE SYNTHASE-RELATED; 1.
DR Pfam; PF00682; HMGL-like; 1.
DR Pfam; PF08502; LeuA_dimer; 1.
DR SMART; SM00917; LeuA_dimer; 1.
DR SUPFAM; SSF110921; 2-isopropylmalate synthase LeuA, allosteric (dimerisation) domain; 1.
DR SUPFAM; SSF51569; Aldolase; 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 Acyltransferase {ECO:0000313|EMBL:EFE8674061.1};
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605, ECO:0000256|HAMAP-
KW Rule:MF_01025};
KW Branched-chain amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023304,
KW ECO:0000256|HAMAP-Rule:MF_01025};
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01025};
KW Leucine biosynthesis {ECO:0000256|ARBA:ARBA00022430, ECO:0000256|HAMAP-
KW Rule:MF_01025};
KW Manganese {ECO:0000256|ARBA:ARBA00023211, ECO:0000256|HAMAP-Rule:MF_01025};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_01025};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_01025}.
FT DOMAIN 5..267
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50991"
FT REGION 392..523
FT /note="Regulatory domain"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01025"
FT BINDING 14
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01025"
FT BINDING 202
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01025"
FT BINDING 204
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01025"
FT BINDING 238
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01025"
SQ SEQUENCE 523 AA; 57314 MW; DE6DE91AB788351A CRC64;
MSQQVIIFDT TLRDGEQALQ ASLSVKEKLQ IALALERMGV DVMEVGFPVS SPGDFESVQT
IARQVKNSRV CALARCVEKD IDVAAESLKV AEAFRIHTFI ATSPMHIATK LRSTLDEVIE
RAIYMVKRAR NYTDDVEFSC EDAGRTPIAD LARVVEAAIN AGATTINIPD TVGYTMPFEF
AGIISGLYER VPNIDKAIIS VHTHDDLGLA VGNSLAAVHA GARQVEGAMN GIGERAGNCS
LEEVIMAIKV RKDILNVHTA INHQEIWRTS QLVSQICNMP IPANKAIVGS GAFAHSSGIH
QDGVLKNREN YEIMTPESIG LNQIQLNLTS RSGRAAVKHR MDEMGYKESE YNLDNLYDAF
LKLADKKGQV FDYDLEALAF IGKQQEEPEH FRLDYFSVQS GSNDIATAAV KLACGEEVKA
EAANGNGPVD AVYQAINRIT DYNVELVKYS LTAKGHGKDA LGQVDIVANY NGRRFHGVGL
ATDIVESSAK AMVHVLNNIW RATEVEKELQ RKAQHNENNK ETV
//
