ID A9BME7_DELAS Unreviewed; 563 AA.
AC A9BME7;
DT 15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT 15-JAN-2008, sequence version 1.
DT 24-JAN-2024, entry version 98.
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 OrderedLocusNames=Daci_4863 {ECO:0000313|EMBL:ABX37492.1};
OS Delftia acidovorans (strain DSM 14801 / SPH-1).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Delftia.
OX NCBI_TaxID=398578 {ECO:0000313|EMBL:ABX37492.1, ECO:0000313|Proteomes:UP000000784};
RN [1] {ECO:0000313|EMBL:ABX37492.1, ECO:0000313|Proteomes:UP000000784}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14801 / SPH-1 {ECO:0000313|Proteomes:UP000000784};
RX PubMed=15240283; DOI=10.1128/AEM.70.7.4053-4063.2004;
RA Schleheck D., Knepper T.P., Fischer K., Cook A.M.;
RT "Mineralization of individual congeners of linear alkylbenzenesulfonate by
RT defined pairs of heterotrophic bacteria.";
RL Appl. Environ. Microbiol. 70:4053-4063(2004).
RN [2] {ECO:0000313|Proteomes:UP000000784}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14801 / SPH-1 {ECO:0000313|Proteomes:UP000000784};
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Lowry S., Clum A., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Kim E., Schleheck D., Richardson P.;
RT "Complete sequence of Delftia acidovorans DSM 14801 / SPH-1.";
RL Submitted (NOV-2007) 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; CP000884; ABX37492.1; -; Genomic_DNA.
DR RefSeq; WP_012206662.1; NC_010002.1.
DR AlphaFoldDB; A9BME7; -.
DR STRING; 398578.Daci_4863; -.
DR GeneID; 24116297; -.
DR KEGG; dac:Daci_4863; -.
DR eggNOG; COG0119; Bacteria.
DR HOGENOM; CLU_004588_3_0_4; -.
DR OMA; WPDKVID; -.
DR UniPathway; UPA00048; UER00070.
DR Proteomes; UP000000784; Chromosome.
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; PS00816; AIPM_HOMOCIT_SYNTH_2; 1.
DR PROSITE; PS50991; PYR_CT; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000313|EMBL:ABX37492.1};
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605, ECO:0000256|HAMAP-
KW 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|ARBA:ARBA00022430, ECO:0000256|HAMAP-
KW Rule:MF_00572}; 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:UP000000784};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00572}.
FT DOMAIN 33..307
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50991"
FT REGION 439..563
FT /note="Regulatory domain"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00572"
FT BINDING 42
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00572"
FT BINDING 246
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00572"
FT BINDING 248
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00572"
FT BINDING 282
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00572"
SQ SEQUENCE 563 AA; 62766 MW; 17746B26B4B6CF79 CRC64;
MLQNPSTKYR PFAFAPVRLQ NRSWPDATIT KAPIWCSVDL RDGNQALIEP MDIDRKMRMF
EQLVKIGFKE IEVGFPSASQ VEFDFMRKLI EENRIPDDVT IQVLTQAREH LIRRTFEALE
GVPRAIVHLY NATAPVMRRV VLNMSEDEIV ELATTNARMF NEIAAGYPQT QWTFQYSPEM
YSDTELEFSK RVIDAVTDVW QPTTERKCII NLPTTVEHST PNLFADMVEW THRHIQRRDS
IVLSVHPHND RGTGTATAEL ALMAGADRLE GCLFGNGERT GNLDVVNVAL NMYIQGVSPG
LDFSDIDGIR STVEHCNQLP VHPRHPYVGD LVYTSFSGSH QDAIKKAFAD RKEGDVWDMP
YLPIDPKDLG RSYEAVIRVN SQSGKGGIAY LLESEYGLQL PRRLQIEFSQ VVQREMDASG
KELAAADLWN LFQREYGLQS VQAPHYRLSE NDGVVSLSAD LAVEGGKRTV EAEGTGPIDA
FVQALSEHSG RAVRVLDYAE HAIGEGANAK AIAYVELRVD ESHVCYGVGV DANIVSASFR
AIMSGLQRVP SAENAVAQEA VAA
//