ID A0A2S9A5A5_9MICO Unreviewed; 583 AA.
AC A0A2S9A5A5;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
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 ORFNames=CQ047_12315 {ECO:0000313|EMBL:PRB08654.1};
OS Microbacterium sp. MYb72.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Microbacterium.
OX NCBI_TaxID=1848693 {ECO:0000313|EMBL:PRB08654.1, ECO:0000313|Proteomes:UP000238041};
RN [1] {ECO:0000313|EMBL:PRB08654.1, ECO:0000313|Proteomes:UP000238041}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MYb72 {ECO:0000313|EMBL:PRB08654.1,
RC ECO:0000313|Proteomes:UP000238041};
RA Zimmermann J., Obeng N., Yang W., Obeng O., Kissoyan K., Pees B.,
RA Dirksen P., Hoppner M., Franke A., Rosenstiel P., Leippe M., Dierking K.,
RA Kaleta C., Schulenburg H.;
RT "Genomic, metabolic, and phenotypic characteristics of bacterial isolates
RT from the natural microbiome of the model nematode Caenorhabditis elegans.";
RL Submitted (SEP-2017) 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 -!- 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:PRB08654.1}.
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DR EMBL; PCOT01000020; PRB08654.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2S9A5A5; -.
DR OrthoDB; 9803573at2; -.
DR UniPathway; UPA00048; UER00070.
DR Proteomes; UP000238041; Unassembled WGS sequence.
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 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 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};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00572}.
FT DOMAIN 61..334
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50991"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 476..583
FT /note="Regulatory domain"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00572"
FT BINDING 70
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00572"
FT BINDING 273
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00572"
FT BINDING 275
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00572"
FT BINDING 309
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00572"
SQ SEQUENCE 583 AA; 63869 MW; 458FF81B16C45DA1 CRC64;
MTSRTFPTLS TPSGPVPADA PHWNRQRGSQ MPSHRYLSVH DRVPLPLAER NWPMRRLTAA
PLWVPVDLRD GNQALAEPMD PARKRRFFEL MVAMGYKEIE VGYPSASQTD FDFVRLLAET
DLAPEDVTIV VFTAARTDLI ERTVASVDGI RNPVVIHVYT ATAPIWRDVV LGRSRAELKE
LILDAGRDVL SLAGDHSNVR FEFSPEVFNL TEPDYVLDVC DAMTTLWDAT PERPVILNLP
ATVEIASPNV YADQIEYMHR NLARRDGVIL SVHPHNDRGT GIACAELAVL AGAQRVEGCI
FGNGERTGNV DIATLALNLH AQGVDPMIDF SDIDEIRRTV EHSNGIEVHA RHPYVGDLVH
TAFSGTHQDA IRKGLAEHRA RAAHEGVAEK DLAWRVPYLP IDPADLGRGY DAVIRVNSQS
GKGGIAYLLE TGYGVELPRR LQIDFARRVQ AQADAAGAEF SPEELWALFT ESYVDRGAAE
TPELVHYRVD DGQTEIALRI DGVDIAHRTD RVGPVESLVA ALASGGIQVD VLSLHQTSIG
HGTDSDALTL IEYRIGTESG WAAGRARSVL DATFAAVLRA AVG
//
