LEU1_BIFLS
ID LEU1_BIFLS Reviewed; 638 AA.
AC B7GT76; E8MNG1;
DT 05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 1.
DT 03-AUG-2022, entry version 77.
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=Blon_0170, BLIJ_0173;
OS Bifidobacterium longum subsp. infantis (strain ATCC 15697 / DSM 20088 / JCM
OS 1222 / NCTC 11817 / S12).
OC Bacteria; Actinobacteria; Bifidobacteriales; Bifidobacteriaceae;
OC Bifidobacterium.
OX NCBI_TaxID=391904;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15697 / DSM 20088 / JCM 1222 / NCTC 11817 / S12;
RX PubMed=19033196; DOI=10.1073/pnas.0809584105;
RA Sela D.A., Chapman J., Adeuya A., Kim J.H., Chen F., Whitehead T.R.,
RA Lapidus A., Rokhsar D.S., Lebrilla C.B., German J.B., Price N.P.,
RA Richardson P.M., Mills D.A.;
RT "The genome sequence of Bifidobacterium longum subsp. infantis reveals
RT adaptations for milk utilization within the infant microbiome.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:18964-18969(2008).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15697 / DSM 20088 / JCM 1222 / NCTC 11817 / S12;
RX PubMed=21270894; DOI=10.1038/nature09646;
RA Fukuda S., Toh H., Hase K., Oshima K., Nakanishi Y., Yoshimura K., Tobe T.,
RA Clarke J.M., Topping D.L., Suzuki T., Taylor T.D., Itoh K., Kikuchi J.,
RA Morita H., Hattori M., Ohno H.;
RT "Bifidobacteria can protect from enteropathogenic infection through
RT production of acetate.";
RL Nature 469:543-547(2011).
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; CP001095; ACJ51299.1; -; Genomic_DNA.
DR EMBL; AP010889; BAJ67767.1; -; Genomic_DNA.
DR RefSeq; WP_012576620.1; NZ_JDTT01000001.1.
DR AlphaFoldDB; B7GT76; -.
DR SMR; B7GT76; -.
DR PRIDE; B7GT76; -.
DR EnsemblBacteria; ACJ51299; ACJ51299; Blon_0170.
DR KEGG; bln:Blon_0170; -.
DR KEGG; blon:BLIJ_0173; -.
DR PATRIC; fig|391904.8.peg.174; -.
DR HOGENOM; CLU_004588_3_2_11; -.
DR OMA; WPDKVID; -.
DR UniPathway; UPA00048; UER00070.
DR Proteomes; UP000001360; 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; Transferase.
FT CHAIN 1..638
FT /note="2-isopropylmalate synthase"
FT /id="PRO_0000406871"
FT DOMAIN 72..346
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01151"
SQ SEQUENCE 638 AA; 70506 MW; F1D196772C0A2974 CRC64;
MGQDQSSVFD LAAVAAASNG GNNDPLLPPA RFIGDPQKPS RMPYNKYASY SEQIPFDYPE
RTWPGKRLQR APRWCSVDLR DGNQALVNPM DSERKLRFWN LLVSMGFKEI EVGFPSASET
DFDFIRMLIE RELIPDDVTI VVLTQCREHL IRRTYEALKG AKRAIVHFYN SVSVLQREVV
FRKNKEEIKK LATDAAELCK DLENEAKGID LYYEYSPESF TGTEPEYAVE VCNAVIGVIK
PTPEHPMIIN LPATVEMTTP NVFADEVEYV STHLDDRDSV VLSLHPHNDE GMGVAATELA
VLAGADRVEG CLLGNGERTG NVDLVTLGLN WLTQGIDPQL DLSNVPEIRK TVEYCNQIKI
SERHPYAGNF VFTAFSGSHQ DAIKKGLEAR QVAAERAGAD LDSFVWLVPY LPIDPKDIGR
TYEAIIRVNS QSGKGGMAYL LKTNHNLDLP KRLQIEFDKI VQNYADTTKK EVKDGDIWRL
FKDEYLPVEQ SGMTAAGVVV GDTHDASLEP WGRLKLLKVA VSSGEDGSDT VLKARLLDRG
VNVGDDEPVE REASGIGNGP IAAFLNAISN FGVEASIMDY VEHTMSVGTD AMAASYVECQ
IGEADDAQIV WGVGIDSSIT TSALKAIISA INRSQRQR
