ID A0A0C2VL66_9BACL Unreviewed; 514 AA.
AC A0A0C2VL66;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 39.
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|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 ORFNames=KP78_22870 {ECO:0000313|EMBL:KIL44743.1};
OS Jeotgalibacillus soli.
OC Bacteria; Bacillota; Bacilli; Bacillales; Planococcaceae; Jeotgalibacillus.
OX NCBI_TaxID=889306 {ECO:0000313|EMBL:KIL44743.1, ECO:0000313|Proteomes:UP000031938};
RN [1] {ECO:0000313|EMBL:KIL44743.1, ECO:0000313|Proteomes:UP000031938}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=P9 {ECO:0000313|EMBL:KIL44743.1,
RC ECO:0000313|Proteomes:UP000031938};
RA Goh K.M., Chan K.-G., Yaakop A.S., Ee R., Gan H.M., Chan C.S.;
RT "Genome sequencing of Jeotgalibacillus soli.";
RL Submitted (JAN-2015) 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). {ECO:0000256|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: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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KIL44743.1}.
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DR EMBL; JXRP01000018; KIL44743.1; -; Genomic_DNA.
DR RefSeq; WP_041088805.1; NZ_JXRP01000018.1.
DR AlphaFoldDB; A0A0C2VL66; -.
DR STRING; 889306.KP78_22870; -.
DR PATRIC; fig|889306.3.peg.2300; -.
DR OrthoDB; 9804858at2; -.
DR UniPathway; UPA00048; UER00070.
DR Proteomes; UP000031938; 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:KIL44743.1};
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}; Reference proteome {ECO:0000313|Proteomes:UP000031938};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_01025}.
FT DOMAIN 4..266
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50991"
FT REGION 392..514
FT /note="Regulatory domain"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01025"
FT BINDING 13
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01025"
FT BINDING 201
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01025"
FT BINDING 203
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01025"
FT BINDING 237
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01025"
SQ SEQUENCE 514 AA; 56048 MW; 3816420BC35FB778 CRC64;
MRKIDIFDTT LRDGEQSAGI NLNTAEKLEI AKQLERFGAN VIEAGFPASS PGDFEAVQKI
ANTVQNSIVT GLARAVKTDI ETSWEALKGG AEPHLHIFLA TSPIHMTYKL KKTPDQVVDI
AVESVKYAKK FFPLVQWSAE DAFRSDFDFL VRIVEQVIKA GATTINLPDT VGYATPAEYG
AMFKYLKENA KGIEKVKLSA HCHDDLGMAV ANTLAAIENG ADQVEGTING IGERAGNAGL
EEVAVALHIR KDFYNIETDV KLDEIKRISQ LVSQLTGMVV PANKAVVGKN AFAHESGIHQ
DGVLKERSTY EIITPELIGE TSNRMVLGKH SGRHAFKDRA VSMGFHLSEE KINDAFQAFK
RLADKKKEIS EEDLFVILTD QQIQDNETPT YELKSVQVQY GSDSIPTATV SVTSPDGELL
QEASTGAGSV EAIYNTLERL VKGKVHLLDF RVTSIGKGRD ALGEAVVNLT YNGNSSSGRD
VAQDVLEASA KAYLNAINRQ LVNERQRTPA KTVG
//
