ID W6RXV3_9CLOT Unreviewed; 560 AA.
AC W6RXV3;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE RecName: Full=2-isopropylmalate synthase {ECO:0000256|ARBA:ARBA00012973, ECO:0000256|HAMAP-Rule:MF_00572};
DE EC=2.3.3.13 {ECO:0000256|ARBA:ARBA00012973, ECO:0000256|HAMAP-Rule:MF_00572};
DE AltName: Full=Alpha-IPM synthase {ECO:0000256|HAMAP-Rule:MF_00572};
DE AltName: Full=Alpha-isopropylmalate synthase {ECO:0000256|HAMAP-Rule:MF_00572};
GN Name=leuA {ECO:0000256|HAMAP-Rule:MF_00572,
GN ECO:0000313|EMBL:CDM69486.1};
GN ORFNames=CM240_2349 {ECO:0000313|EMBL:CDM69486.1};
OS Clostridium bornimense.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1216932 {ECO:0000313|EMBL:CDM69486.1, ECO:0000313|Proteomes:UP000019426};
RN [1] {ECO:0000313|EMBL:CDM69486.1, ECO:0000313|Proteomes:UP000019426}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M2/40 {ECO:0000313|Proteomes:UP000019426};
RA Wibberg D., Puehler A., Schlueter A.;
RT "Complete genome sequence of Clostridum sp. M2/40.";
RL Submitted (NOV-2013) 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_00572}.
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|ARBA:ARBA00000064, ECO:0000256|HAMAP-
CC Rule:MF_00572};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00572};
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_00572}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00572}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00572}.
CC -!- SIMILARITY: Belongs to the alpha-IPM synthase/homocitrate synthase
CC family. LeuA type 2 subfamily. {ECO:0000256|ARBA:ARBA00009767,
CC ECO:0000256|HAMAP-Rule:MF_00572}.
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; HG917868; CDM69486.1; -; Genomic_DNA.
DR RefSeq; WP_044039295.1; NZ_HG917868.1.
DR AlphaFoldDB; W6RXV3; -.
DR STRING; 1216932.CM240_2349; -.
DR KEGG; clt:CM240_2349; -.
DR PATRIC; fig|1216932.3.peg.2327; -.
DR eggNOG; COG0119; Bacteria.
DR HOGENOM; CLU_004588_3_0_9; -.
DR OrthoDB; 9804858at2; -.
DR UniPathway; UPA00048; UER00070.
DR Proteomes; UP000019426; Chromosome 1.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0009098; P:leucine biosynthetic process; IEA:UniProtKB-UniRule.
DR CDD; cd07942; DRE_TIM_LeuA; 1.
DR Gene3D; 3.30.160.270; -; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR HAMAP; MF_00572; LeuA_type2; 1.
DR InterPro; IPR013709; 2-isopropylmalate_synth_dimer.
DR InterPro; IPR002034; AIPM/Hcit_synth_CS.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR005668; IPM_Synthase.
DR InterPro; IPR036230; LeuA_allosteric_dom_sf.
DR InterPro; IPR039371; LeuA_N_DRE-TIM.
DR InterPro; IPR000891; PYR_CT.
DR NCBIfam; TIGR00970; leuA_yeast; 1.
DR PANTHER; PTHR46911; -; 1.
DR PANTHER; PTHR46911:SF1; 2-ISOPROPYLMALATE SYNTHASE; 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 SUPFAM; SSF89000; post-HMGL domain-like; 1.
DR PROSITE; PS00815; AIPM_HOMOCIT_SYNTH_1; 1.
DR PROSITE; PS50991; PYR_CT; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000313|EMBL:CDM69486.1};
KW Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00572};
KW Branched-chain amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023304,
KW ECO:0000256|HAMAP-Rule:MF_00572};
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00572};
KW Leucine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00572};
KW Magnesium {ECO:0000256|HAMAP-Rule:MF_00572};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_00572}; Reference proteome {ECO:0000313|Proteomes:UP000019426};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00572}.
FT DOMAIN 30..304
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50991"
FT REGION 438..560
FT /note="Regulatory domain"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00572"
FT BINDING 39
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00572"
FT BINDING 243
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00572"
FT BINDING 245
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00572"
FT BINDING 279
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00572"
SQ SEQUENCE 560 AA; 63154 MW; 0CACCBBB0900A95C CRC64;
MSYDFKKYRK YPVVNLPNRK WPNNVIEKAP IWCSVDLRDG NQSLPSPMNV EEKKEMFKLL
VDMGFKEIEI GFPSASETEY KFLRALVEDN LIPDDVTIQV LTQAREHLIK KTFESLVGVK
KAIVHLYNST STLQREVVFK KSKEEIIDIA VSGAKLLNEY KNKYPETDFT FEYSPESFTG
TELDYALEIC EAVIDVWKPT KDKKVIINLP STVEMATPNV YADQIEWFST HVSNRENIIL
SLHTHNDRGT CTASSELGLL AGADRLEGTL FGNGERTGNL DIVTTAMNLY SQGIEPKLDF
HDINKLIEVY ERCTKLTVHD RHPYAGKLVY AAFSGSHQDA IRKGFIAMKE KNSSIWEVPY
LPIDPHDLGR EYEEIIRINS QSGKGGAAYI MENDFGFMLP KAMHPEFGAF VQEKSDELGV
ELTANEIFDI FKEHYLDINK PYTLKGYEIQ STDDVEGGKN IVSIKAKVAV NGEEKEIIGK
GNGPLNAFYN GLISDEDVDC KFKNYFEHAL EGGSCSRAVC YIQIESKGKE WFGVGISENI
ATASLNALVS AMNRCGNIRK
//
