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Database: UniProt
Entry: E5WJ67_9BACI
LinkDB: E5WJ67_9BACI
Original site: E5WJ67_9BACI 
ID   E5WJ67_9BACI            Unreviewed;       514 AA.
AC   E5WJ67;
DT   08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT   08-MAR-2011, sequence version 1.
DT   24-JAN-2024, entry version 63.
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=HMPREF1013_02491 {ECO:0000313|EMBL:EFV77284.1};
OS   Bacillus sp. 2_A_57_CT2.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=665959 {ECO:0000313|EMBL:EFV77284.1, ECO:0000313|Proteomes:UP000003283};
RN   [1] {ECO:0000313|EMBL:EFV77284.1, ECO:0000313|Proteomes:UP000003283}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2_A_57_CT2 {ECO:0000313|EMBL:EFV77284.1,
RC   ECO:0000313|Proteomes:UP000003283};
RG   The Broad Institute Genome Sequencing Platform;
RA   Earl A., Ward D., Feldgarden M., Gevers D., Daigneault M., Strauss J.,
RA   Allen-Vercoe E., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA   Abouelleil A., Alvarado L., Arachchi H.M., Berlin A., Brown A.,
RA   Chapman S.B., Chen Z., Dunbar C., Freedman E., Gearin G., Gellesch M.,
RA   Goldberg J., Griggs A., Gujja S., Heilman E., Heiman D., Howarth C.,
RA   Larson L., Lui A., MacDonald P.J.P., Mehta T., Montmayeur A., Murphy C.,
RA   Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T., Shenoy N.,
RA   Sisk P., Stolte C., Sykes S., White J., Yandava C., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Bacillus sp. strain 2_A_57_CT2.";
RL   Submitted (DEC-2010) 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:EFV77284.1}.
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DR   EMBL; ACWD01000034; EFV77284.1; -; Genomic_DNA.
DR   RefSeq; WP_009333173.1; NZ_GL635752.1.
DR   AlphaFoldDB; E5WJ67; -.
DR   eggNOG; COG0119; Bacteria.
DR   HOGENOM; CLU_022158_0_1_9; -.
DR   UniPathway; UPA00048; UER00070.
DR   Proteomes; UP000003283; 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   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:UP000003283};
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          391..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;  55981 MW;  3F680AD974351F0C CRC64;
     MRTIKIFDTT LRDGEQSAGV NLNFSEKLEI ARQLERLNVD IIEAGFPAAS KGDFASVQKI
     AQTINNCSVT GLARAVISDI DAAWGALKDG AEPRIHTFLA TSPIHRQYKL KKTKEEVVET
     AVETVKYAAS KFPIVQWSAE DATRTELPFL AEIIEKVIQA GATIINIPDT VGYTTPQEYG
     EIFQYLRNHV PSIDKVSLSA HCHDDLGMAI ANSLSAIENG ATQIEGTING IGERAGNAAL
     EELAVALYIR NNHYQASTRL NLQEISRTSS LISKLTGMVV PANKAIVGRN AFAHESGIHQ
     DGVLKEKTTY EIISPDLVGF QSNSMVLGKH SGRHAFKNRL SELGLEVADE EANRLFTVFK
     DLADRKKEMT DDDLAAIVLE EKLSKEQRFY DLIGIQIQYG TNSVPTATVT LSGSNNEVIQ
     EAGTGAGSIE ALYNTLEKCL NGTANLLDYR IQSVGAGRDA LAQVYVKLNY EGVETSGRGL
     AQDVLEASSK AYLNAVNRVI YMKEKAQAQA VEAN
//
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