LEU1_ACIET
ID LEU1_ACIET Reviewed; 512 AA.
AC B9MA32;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 74.
DE RecName: Full=2-isopropylmalate synthase {ECO:0000255|HAMAP-Rule:MF_01025};
DE EC=2.3.3.13 {ECO:0000255|HAMAP-Rule:MF_01025};
DE AltName: Full=Alpha-IPM synthase {ECO:0000255|HAMAP-Rule:MF_01025};
DE AltName: Full=Alpha-isopropylmalate synthase {ECO:0000255|HAMAP-Rule:MF_01025};
GN Name=leuA {ECO:0000255|HAMAP-Rule:MF_01025}; OrderedLocusNames=Dtpsy_1948;
OS Acidovorax ebreus (strain TPSY) (Diaphorobacter sp. (strain TPSY)).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Diaphorobacter.
OX NCBI_TaxID=535289;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TPSY;
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C., Han C.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Coates J.D.;
RT "Complete sequence of Diaphorobacter sp. TPSY.";
RL Submitted (JAN-2009) 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-oxoisovalerate) to form 3-carboxy-3-
CC hydroxy-4-methylpentanoate (2-isopropylmalate). {ECO:0000255|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:0000255|HAMAP-Rule:MF_01025};
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_01025}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_01025}.
CC -!- SIMILARITY: Belongs to the alpha-IPM synthase/homocitrate synthase
CC family. LeuA type 1 subfamily. {ECO:0000255|HAMAP-Rule:MF_01025}.
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DR EMBL; CP001392; ACM33404.1; -; Genomic_DNA.
DR RefSeq; WP_015913456.1; NC_011992.1.
DR AlphaFoldDB; B9MA32; -.
DR SMR; B9MA32; -.
DR STRING; 535289.Dtpsy_1948; -.
DR EnsemblBacteria; ACM33404; ACM33404; Dtpsy_1948.
DR KEGG; dia:Dtpsy_1948; -.
DR eggNOG; COG0119; Bacteria.
DR HOGENOM; CLU_022158_0_1_4; -.
DR OMA; NTMRMLV; -.
DR OrthoDB; 840579at2; -.
DR UniPathway; UPA00048; UER00070.
DR Proteomes; UP000000450; 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 Gene3D; 3.20.20.70; -; 1.
DR Gene3D; 3.30.160.270; -; 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 Pfam; PF00682; HMGL-like; 1.
DR Pfam; PF08502; LeuA_dimer; 1.
DR SMART; SM00917; LeuA_dimer; 1.
DR SUPFAM; SSF110921; SSF110921; 1.
DR TIGRFAMs; TIGR00973; leuA_bact; 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; Transferase.
FT CHAIN 1..512
FT /note="2-isopropylmalate synthase"
FT /id="PRO_1000149179"
FT DOMAIN 5..268
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01151"
SQ SEQUENCE 512 AA; 55456 MW; 63656656ED1122D9 CRC64;
MTDKLIIFDT TLRDGEQSPG ASMTRDEKLR IARQLERLRV DVIEAGFAAS SNGDFESVQA
IARAVKDSTV CSLARANDRD IARAAEALKE ANRARIHTFI ATSALHMEKK LRMTPEQVLE
QARQAVRFAR NLVEDIEFSP EDGYRSDPDF LCRVIETVIA EGATTINVPD TVGYAIPELY
GNFIKNLRER IPNSDKAIWS VHCHNDLGMA VANSLAGVKI GGARQVECTI NGLGERAGNC
SLEEVVMAVK TRRDYFGLDV GIDTQHIVAA SRMVSQTTGF VVQPNKAVVG ANAFAHASGI
HQDGVLKARD TYEIMRAEDV GWSANKIVLG KLSGRNAFKQ RLQELGVQLE SEGEINVAFA
KFKELADRKS EIFDEDILAL VSDESVTSEK EQFGFVSLAQ HSETGERPEA TIVFTVDGKE
VRSSAEGNGP VDASMKAIEA HVRSGAEMVL YSVNAISGST ESQGEVTVRL QSAGRVVNGV
GADPDIVVAS AKAYLSALNK LQSKAERVAA QG