LEU1_ARTS2
ID LEU1_ARTS2 Reviewed; 579 AA.
AC A0JX36;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 12-DEC-2006, sequence version 1.
DT 25-MAY-2022, entry version 89.
DE RecName: Full=2-isopropylmalate synthase {ECO:0000255|HAMAP-Rule:MF_00572};
DE EC=2.3.3.13 {ECO:0000255|HAMAP-Rule:MF_00572};
DE AltName: Full=Alpha-IPM synthase {ECO:0000255|HAMAP-Rule:MF_00572};
DE AltName: Full=Alpha-isopropylmalate synthase {ECO:0000255|HAMAP-Rule:MF_00572};
GN Name=leuA {ECO:0000255|HAMAP-Rule:MF_00572}; OrderedLocusNames=Arth_2226;
OS Arthrobacter sp. (strain FB24).
OC Bacteria; Actinobacteria; Micrococcales; Micrococcaceae; Arthrobacter.
OX NCBI_TaxID=290399;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FB24;
RX PubMed=24501649; DOI=10.4056/sigs.4438185;
RA Nakatsu C.H., Barabote R., Thompson S., Bruce D., Detter C., Brettin T.,
RA Han C., Beasley F., Chen W., Konopka A., Xie G.;
RT "Complete genome sequence of Arthrobacter sp. strain FB24.";
RL Stand. Genomic Sci. 9:106-116(2013).
CC -!- FUNCTION: Catalyzes the condensation of the acetyl group of acetyl-CoA
CC with 3-methyl-2-oxobutanoate (2-oxoisovalerate) to form 3-carboxy-3-
CC hydroxy-4-methylpentanoate (2-isopropylmalate). {ECO:0000255|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:0000255|HAMAP-Rule:MF_00572};
CC -!- PATHWAY: Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine
CC from 3-methyl-2-oxobutanoate: step 1/4. {ECO:0000255|HAMAP-
CC Rule:MF_00572}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_00572}.
CC -!- SIMILARITY: Belongs to the alpha-IPM synthase/homocitrate synthase
CC family. LeuA type 2 subfamily. {ECO:0000255|HAMAP-Rule:MF_00572}.
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DR EMBL; CP000454; ABK03606.1; -; Genomic_DNA.
DR RefSeq; WP_011692070.1; NC_008541.1.
DR AlphaFoldDB; A0JX36; -.
DR SMR; A0JX36; -.
DR STRING; 290399.Arth_2226; -.
DR PRIDE; A0JX36; -.
DR EnsemblBacteria; ABK03606; ABK03606; Arth_2226.
DR KEGG; art:Arth_2226; -.
DR eggNOG; COG0119; Bacteria.
DR HOGENOM; CLU_004588_3_0_11; -.
DR OMA; WPDKVID; -.
DR OrthoDB; 840579at2; -.
DR UniPathway; UPA00048; UER00070.
DR Proteomes; UP000000754; Chromosome.
DR GO; GO:0003852; F:2-isopropylmalate synthase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0009098; P:leucine biosynthetic process; IEA:UniProtKB-UniRule.
DR CDD; cd07942; DRE_TIM_LeuA; 1.
DR Gene3D; 3.20.20.70; -; 1.
DR Gene3D; 3.30.160.270; -; 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 Pfam; PF00682; HMGL-like; 1.
DR Pfam; PF08502; LeuA_dimer; 1.
DR SMART; SM00917; LeuA_dimer; 1.
DR SUPFAM; SSF110921; SSF110921; 1.
DR TIGRFAMs; TIGR00970; leuA_yeast; 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; Branched-chain amino acid biosynthesis;
KW Leucine biosynthesis; Reference proteome; Transferase.
FT CHAIN 1..579
FT /note="2-isopropylmalate synthase"
FT /id="PRO_1000025028"
FT DOMAIN 40..314
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01151"
SQ SEQUENCE 579 AA; 63597 MW; CF3C48DF82F898AD CRC64;
MRNAQKPSGM PVHRYMPFQD QITVELPDRT WPDKVITKAP RWCAVDLRDG NQALIDPMSP
ARKMKMFDLL VRMGYKEIEV GFPSASQTDF DFVRQLIEGN HIPDDVTIQV LTQAREHLIE
RTYESLVGAK QAIVHLYNST SVLQRRVVFN QDEDGILDIA LQGARLCKKY EETLADTHIT
YEYSPESFTG TELEYAVRVC NAVADVFEAS ADSQVIINLP ATVEMATPNV YADSIEWMSR
HLHPREGIIL SLHPHNDRGT GVAAAELGYL AGADRIEGCL FGNGERTGNV DLVTLGLNMF
VQGIDPMIDF SDIDDVRRTV EYCNQLPVAE RSPYGGDLVF TAFSGSHQDA IKKGFEALEK
DAAAAGKDVA DYTWQVPYLP VDPKDLGRSY EAVIRVNSQS GKGGVAYLLK NEHSLDLPRR
AQIEFSGVIQ KRTDTVGGEV SGAQLWQIFQ DEYLPSSKED GQWGRYSLGS FSTETDDDGA
MTLHATVTVD GVQVRRTGSG NGPIAALLSI LGQDGVDVRV LDYSEHALSE GGNARAAAYV
ECAVGERVLW GVGIDSNTTT SSLKAVISAV NRAIRDAQA