ID A0A0U0WQ49_SALET Unreviewed; 523 AA.
AC A0A0U0WQ49;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 24-JAN-2024, entry version 46.
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:SUE48814.1};
GN ORFNames=B7N00_13025 {ECO:0000313|EMBL:EDG5017872.1}, B7N01_12280
GN {ECO:0000313|EMBL:EDG4995205.1}, B7N35_10895
GN {ECO:0000313|EMBL:EDG5126531.1}, B7N72_12375
GN {ECO:0000313|EMBL:EDG5370903.1}, B7N78_13265
GN {ECO:0000313|EMBL:EDG5280734.1}, B7N80_08195
GN {ECO:0000313|EMBL:EDG5288357.1}, B7N84_14335
GN {ECO:0000313|EMBL:EDG5267513.1}, DRU31_11365
GN {ECO:0000313|EMBL:EBS2452909.1}, E0916_13440
GN {ECO:0000313|EMBL:ECF1446957.1}, EJV93_16105
GN {ECO:0000313|EMBL:ECA2722715.1}, ERS008202_01859
GN {ECO:0000313|EMBL:CNU09365.1}, ERS008207_01280
GN {ECO:0000313|EMBL:CNT89427.1}, EWC73_11320
GN {ECO:0000313|EMBL:ECE8536786.1}, G0B02_13555
GN {ECO:0000313|EMBL:HAC6380127.1}, G0D18_11640
GN {ECO:0000313|EMBL:HAC6681300.1}, G2206_11140
GN {ECO:0000313|EMBL:HAE0435313.1}, NCTC5754_03786
GN {ECO:0000313|EMBL:SUE48814.1};
OS Salmonella enterica subsp. enterica serovar Bovismorbificans.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=58097 {ECO:0000313|EMBL:SUE48814.1, ECO:0000313|Proteomes:UP000254190};
RN [1] {ECO:0000313|Proteomes:UP000039541, ECO:0000313|Proteomes:UP000042394}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3476 {ECO:0000313|EMBL:CNU09365.1,
RC ECO:0000313|Proteomes:UP000039541}, and D4891
RC {ECO:0000313|EMBL:CNT89427.1, ECO:0000313|Proteomes:UP000042394};
RG Pathogen Informatics;
RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:HAC6380127.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=BCW_3301 {ECO:0000313|EMBL:HAC6380127.1}, M123
RC {ECO:0000313|EMBL:HAC6681300.1}, and MS140073
RC {ECO:0000313|EMBL:HAE0435313.1};
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 [3] {ECO:0000313|EMBL:SUE48814.1, ECO:0000313|Proteomes:UP000254190}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC5754 {ECO:0000313|EMBL:SUE48814.1,
RC ECO:0000313|Proteomes:UP000254190};
RG Pathogen Informatics;
RA Doyle S.;
RL Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|EMBL:EBS2452909.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=136768 {ECO:0000313|EMBL:EDG4995205.1}, 138330
RC {ECO:0000313|EMBL:EDG5288357.1}, 143652
RC {ECO:0000313|EMBL:EDG5370903.1}, 273631
RC {ECO:0000313|EMBL:EDG5017872.1}, 330535
RC {ECO:0000313|EMBL:EDG5267513.1}, 333944
RC {ECO:0000313|EMBL:EDG5280734.1}, 337042
RC {ECO:0000313|EMBL:EDG5126531.1}, 387147
RC {ECO:0000313|EMBL:EBS2452909.1}, 470200
RC {ECO:0000313|EMBL:ECE8536786.1}, 598023
RC {ECO:0000313|EMBL:ECA2722715.1}, and 692616
RC {ECO:0000313|EMBL:ECF1446957.1};
RA Ashton P.M., Dallman T., Nair S., De Pinna E., Peters T., Grant K.;
RL Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases.
RN [5] {ECO:0000313|EMBL:HAC6681300.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=BCW_3301 {ECO:0000313|EMBL:HAC6380127.1}, M123
RC {ECO:0000313|EMBL:HAC6681300.1}, and MS140073
RC {ECO:0000313|EMBL:HAE0435313.1};
RG NCBI Pathogen Detection Project;
RL Submitted (JUL-2018) 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}.
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DR EMBL; CQPD01000010; CNT89427.1; -; Genomic_DNA.
DR EMBL; CQPC01000020; CNU09365.1; -; Genomic_DNA.
DR EMBL; AAGUWJ010000007; EBS2452909.1; -; Genomic_DNA.
DR EMBL; AAHTVM010000008; ECA2722715.1; -; Genomic_DNA.
DR EMBL; AAIJHK010000008; ECE8536786.1; -; Genomic_DNA.
DR EMBL; AAIKGE010000007; ECF1446957.1; -; Genomic_DNA.
DR EMBL; AAMEJW010000011; EDG4995205.1; -; Genomic_DNA.
DR EMBL; AAMEJY010000007; EDG5017872.1; -; Genomic_DNA.
DR EMBL; AAMEKY010000007; EDG5126531.1; -; Genomic_DNA.
DR EMBL; AAMEMC010000007; EDG5267513.1; -; Genomic_DNA.
DR EMBL; AAMEMH010000008; EDG5280734.1; -; Genomic_DNA.
DR EMBL; AAMEML010000006; EDG5288357.1; -; Genomic_DNA.
DR EMBL; AAMEMP010000011; EDG5370903.1; -; Genomic_DNA.
DR EMBL; DAAMEZ010000008; HAC6380127.1; -; Genomic_DNA.
DR EMBL; DAAMHM010000007; HAC6681300.1; -; Genomic_DNA.
DR EMBL; DAAQQK010000010; HAE0435313.1; -; Genomic_DNA.
DR EMBL; UGVQ01000002; SUE48814.1; -; Genomic_DNA.
DR RefSeq; WP_020999933.1; NZ_WFIN01000008.1.
DR AlphaFoldDB; A0A0U0WQ49; -.
DR UniPathway; UPA00048; UER00070.
DR Proteomes; UP000039541; Unassembled WGS sequence.
DR Proteomes; UP000042394; Unassembled WGS sequence.
DR Proteomes; UP000254190; Unassembled WGS sequence.
DR Proteomes; UP000839929; 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:SUE48814.1};
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; 57483 MW; 47F7F90D9829B610 CRC64;
MSQQVIIFDT TLRDGEQALQ ASLSAKEKLQ IALALERMGV DVMEVGFPVS SPGDFESVQT
IARTIKNSRV CALARCVEKD IDVAAQALKV ADAFRIHTFI ATSPMHIATK LRSTLDEVIE
RAVYMVKRAR NYTDDVEFSC EDAGRTPVDD LARVVEAAIN AGARTINIPD TVGYTMPFEF
AGIISGLYER VPNIDKAIIS VHTHDDLGIA VGNSLAAVYA GARQVEGAMN GIGERAGNCA
LEEVIMAIKV RKDIMNVHTN INHHEIWRTS QTVSQICNMP IPANKAIVGS GAFAHSSGIH
QDGVLKNREN YEIMTPESIG LNQIQLNLTS RSGRAAVKHR MEEMGYKDTD YNMDHLYDAF
LKLADKKGQV FDYDLEALAF INKQQEEPEH FRLDYFSVQS GSSDIATASV KLACGEEIKA
EAANGNGPVD AIYQAINRLT GYDVELVKYD LNAKGQGKDA LGQVDIVVNY HGRRFHGVGL
ATDIVESSAK AMVHVLNNIW RAAEVEKELQ RKAQNKENNK ETV
//
