LEU1_RENSM
ID LEU1_RENSM Reviewed; 582 AA.
AC A9WML8;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 1.
DT 25-MAY-2022, entry version 84.
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};
GN OrderedLocusNames=RSal33209_1593;
OS Renibacterium salmoninarum (strain ATCC 33209 / DSM 20767 / JCM 11484 /
OS NBRC 15589 / NCIMB 2235).
OC Bacteria; Actinobacteria; Micrococcales; Micrococcaceae; Renibacterium.
OX NCBI_TaxID=288705;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33209 / DSM 20767 / JCM 11484 / NBRC 15589 / NCIMB 2235;
RX PubMed=18723615; DOI=10.1128/jb.00721-08;
RA Wiens G.D., Rockey D.D., Wu Z., Chang J., Levy R., Crane S., Chen D.S.,
RA Capri G.R., Burnett J.R., Sudheesh P.S., Schipma M.J., Burd H.,
RA Bhattacharyya A., Rhodes L.D., Kaul R., Strom M.S.;
RT "Genome sequence of the fish pathogen Renibacterium salmoninarum suggests
RT reductive evolution away from an environmental Arthrobacter ancestor.";
RL J. Bacteriol. 190:6970-6982(2008).
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; CP000910; ABY23329.1; -; Genomic_DNA.
DR RefSeq; WP_012245006.1; NC_010168.1.
DR AlphaFoldDB; A9WML8; -.
DR SMR; A9WML8; -.
DR STRING; 288705.RSal33209_1593; -.
DR EnsemblBacteria; ABY23329; ABY23329; RSal33209_1593.
DR KEGG; rsa:RSal33209_1593; -.
DR eggNOG; COG0119; Bacteria.
DR HOGENOM; CLU_004588_3_0_11; -.
DR OMA; WPDKVID; -.
DR OrthoDB; 840579at2; -.
DR UniPathway; UPA00048; UER00070.
DR Proteomes; UP000002007; 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..582
FT /note="2-isopropylmalate synthase"
FT /id="PRO_1000129511"
FT DOMAIN 40..314
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01151"
SQ SEQUENCE 582 AA; 63841 MW; E161B3DB6C1647C7 CRC64;
MRNAQKPSGM PVHRYLPFHE QIEVELPDRT WPTKRITTAP RWCAVDLRDG NQALIDPMSP
ARKLKMFELL VKMGYKEIEV GFPSASQTDF DFVRQLIQGG HIPEDVTIQV LTQAREHLIE
RTYESLVGAK QAIVHLYNST SVLQRRVVFN EDQDGIMALA TQGALLCKKY QETLTDTKIT
YEYSPESFTG TELDYAVRVC NAVADIFEAS ADNQVIVNLP ATVEMITPNV YADSIEWMSH
NLHPREGIIL SLHPHNDRGT GVAAAELGYL AGADRIEGCL FGNGERAGNV DLVTLGLNMF
SQGVDPMIDF SDIDEIRRTV EYCNQLPAPE RMPYGGDLVF TAFSGSHQDA IKKGFEALER
DADAAGIAVA DTVWAVPYLP VDPKDLGRSY EAVIRVNSQS GKGGVAYLLK SEHSLDLPRR
AQIEFSGVIQ RRTDSVGGEV SADQRWEAFT DEYLPSPAGH PGGQWGRYAL GSMNADTEED
GTTKLNTAMR IDGVEQRRSG SGNGPIAALL NILHDDGVDV RVLDYSEHAL SEGGNASAAS
YVECAVGDRV LWGLGIDPNT TVSSLKAVIS AVNRAIRDNQ VD