LEU1_STACT
ID LEU1_STACT Reviewed; 510 AA.
AC B9DMJ6;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAR-2009, sequence version 1.
DT 25-MAY-2022, entry version 80.
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=Sca_1563;
OS Staphylococcus carnosus (strain TM300).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=396513;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TM300;
RX PubMed=19060169; DOI=10.1128/aem.01982-08;
RA Rosenstein R., Nerz C., Biswas L., Resch A., Raddatz G., Schuster S.C.,
RA Goetz F.;
RT "Genome analysis of the meat starter culture bacterium Staphylococcus
RT carnosus TM300.";
RL Appl. Environ. Microbiol. 75:811-822(2009).
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; AM295250; CAL28468.1; -; Genomic_DNA.
DR AlphaFoldDB; B9DMJ6; -.
DR SMR; B9DMJ6; -.
DR STRING; 396513.SCA_1563; -.
DR KEGG; sca:SCA_1563; -.
DR eggNOG; COG0119; Bacteria.
DR HOGENOM; CLU_022158_0_1_9; -.
DR OMA; NTMRMLV; -.
DR UniPathway; UPA00048; UER00070.
DR Proteomes; UP000000444; 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; 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; 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..510
FT /note="2-isopropylmalate synthase"
FT /id="PRO_1000149309"
FT DOMAIN 4..266
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01151"
SQ SEQUENCE 510 AA; 55476 MW; F6CE3E2623EC450C CRC64;
MSHIQVFDTT LRDGEQTPGV SFSFDERLTI AKQLEKWGVD VIEAGFPASS QGSFDSVKAI
SETLTKTAVV GLARCKKSDI DAVYEATKDA KYPQLHVFIA SSPIHLEHKL KMTQEELLEN
ITENVSYGKS LFDVVQFSPE DATRTDLDFL VKCVQTAVDA GASIINIPDT VGFSYPSEFG
NIFKVLIENV KSDHEVTYSA HCHDDLGLAV ANSMAAIENG ATRIEGAVNG IGERAGNTAL
EEVALGLYVR RDHYGIETNL KLDETKATSD LVASFAGIRV PRNKAIVGQN AFSHESGIHQ
DGFLKHPETY EIMTPQLVGI KSSELPLGKL SGKHAFAEKL KQLGYDITAE KQVELFKQFK
SIADKKKNVS DHDVHALVQG HSHETNAAYQ VETLQLQFVS EGVQSAVVVL KDHEGKEYPS
AAIGTGSIVA VYNAVDQIFK APSELLNYQI TSVTEGSDAQ AQVNVEIRID GKTYYGIGVD
HDVLLASCKA YVEANSNHLA DTARKDGVVS