LEU1_THENN
ID LEU1_THENN Reviewed; 513 AA.
AC B9KB95;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAR-2009, sequence version 1.
DT 25-MAY-2022, entry version 70.
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=CTN_0115;
OS Thermotoga neapolitana (strain ATCC 49049 / DSM 4359 / NBRC 107923 / NS-E).
OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX NCBI_TaxID=309803;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49049 / DSM 4359 / NBRC 107923 / NS-E;
RA Lim S.K., Kim J.S., Cha S.H., Park B.C., Lee D.S., Tae H.S., Kim S.-J.,
RA Kim J.J., Park K.J., Lee S.Y.;
RT "The genome sequence of the hyperthermophilic bacterium Thermotoga
RT neapolitana.";
RL Submitted (NOV-2007) 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000916; ACM22291.1; -; Genomic_DNA.
DR RefSeq; WP_012645001.1; NC_011978.1.
DR AlphaFoldDB; B9KB95; -.
DR SMR; B9KB95; -.
DR STRING; 309803.CTN_0115; -.
DR PRIDE; B9KB95; -.
DR EnsemblBacteria; ACM22291; ACM22291; CTN_0115.
DR KEGG; tna:CTN_0115; -.
DR eggNOG; COG0119; Bacteria.
DR HOGENOM; CLU_022158_0_1_0; -.
DR OMA; NTMRMLV; -.
DR UniPathway; UPA00048; UER00070.
DR Proteomes; UP000000445; 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..513
FT /note="2-isopropylmalate synthase"
FT /id="PRO_1000149319"
FT DOMAIN 4..268
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01151"
SQ SEQUENCE 513 AA; 56878 MW; E5F41EC5EFA91EF8 CRC64;
MRRIKIFDTT LRDGEQSPGA SMSVEEKVEM ALMLEDLGVD LIEAGFPVSS PVQFEAVKRV
AEAVQRPIVV GLARCVEKDI DAAYEALKDR PKDKRMIHVF IATSPIHRKY KLRMEKEEIL
ERVRKYVTYA RQFFDLVEFS AEDASRTEVP FLIEVYRTAI ESGATTINVP DTVGYALPDE
FGELIRTLKE GVPGIENVDL SVHCHNDLGL AVANSIAAVQ NGATQVEVTL NGIGERAGNC
ALEEFVMALK VRKDRLPYET GIRTELIYPA SRLLTHITGL IPARNKPIVG ENVFLHESGI
HQDGVLKHRE TYEIMKPSDI GRSSETLVLG RHSGKHALRK KLESYGIKLD DETFQKVFEK
FTELADRKKE VYDDDLFSIV SEVLKEPLNG YRLVHFHVHT GNTLLPTAAV VLQVGNEKKE
AAETGNGPVD AIFKAIDKAL GLQPKLEEYI IQAVGTGKNA QGEVKLTLKI DGELYSGRGV
STDIVEASAI AYINAINKYL IAKGLLRKNG GVE