LEU11_LEPIN
ID LEU11_LEPIN Reviewed; 501 AA.
AC Q8F445;
DT 15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 2.
DT 25-MAY-2022, entry version 100.
DE RecName: Full=2-isopropylmalate synthase 1 {ECO:0000255|HAMAP-Rule:MF_01025};
DE EC=2.3.3.13 {ECO:0000255|HAMAP-Rule:MF_01025, ECO:0000269|PubMed:15292141};
DE AltName: Full=Alpha-IPM synthase 1 {ECO:0000255|HAMAP-Rule:MF_01025};
DE AltName: Full=Alpha-isopropylmalate synthase 1 {ECO:0000255|HAMAP-Rule:MF_01025, ECO:0000303|PubMed:15292141};
GN Name=leuA1 {ECO:0000303|PubMed:15292141}; OrderedLocusNames=LA_2202;
OS Leptospira interrogans serogroup Icterohaemorrhagiae serovar Lai (strain
OS 56601).
OC Bacteria; Spirochaetes; Leptospirales; Leptospiraceae; Leptospira.
OX NCBI_TaxID=189518;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=56601;
RX PubMed=12712204; DOI=10.1038/nature01597;
RA Ren S.-X., Fu G., Jiang X.-G., Zeng R., Miao Y.-G., Xu H., Zhang Y.-X.,
RA Xiong H., Lu G., Lu L.-F., Jiang H.-Q., Jia J., Tu Y.-F., Jiang J.-X.,
RA Gu W.-Y., Zhang Y.-Q., Cai Z., Sheng H.-H., Yin H.-F., Zhang Y., Zhu G.-F.,
RA Wan M., Huang H.-L., Qian Z., Wang S.-Y., Ma W., Yao Z.-J., Shen Y.,
RA Qiang B.-Q., Xia Q.-C., Guo X.-K., Danchin A., Saint Girons I.,
RA Somerville R.L., Wen Y.-M., Shi M.-H., Chen Z., Xu J.-G., Zhao G.-P.;
RT "Unique physiological and pathogenic features of Leptospira interrogans
RT revealed by whole-genome sequencing.";
RL Nature 422:888-893(2003).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, AND INDUCTION.
RC STRAIN=56601;
RX PubMed=15292141; DOI=10.1128/jb.186.16.5400-5409.2004;
RA Xu H., Zhang Y., Guo X., Ren S., Staempfli A.A., Chiao J., Jiang W.,
RA Zhao G.;
RT "Isoleucine biosynthesis in Leptospira interrogans serotype lai strain
RT 56601 proceeds via a threonine-independent pathway.";
RL J. Bacteriol. 186:5400-5409(2004).
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) (PubMed:15292141). Does
CC not have citramalate synthase activity (PubMed:15292141).
CC {ECO:0000269|PubMed:15292141}.
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 ECO:0000269|PubMed:15292141};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21525;
CC Evidence={ECO:0000269|PubMed:15292141};
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, ECO:0000269|PubMed:15292141}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_01025}.
CC -!- INDUCTION: Expression is significantly repressed by leucine and
CC moderately repressed by isoleucine. {ECO:0000269|PubMed:15292141}.
CC -!- SIMILARITY: Belongs to the alpha-IPM synthase/homocitrate synthase
CC family. LeuA type 1 subfamily. {ECO:0000255|HAMAP-Rule:MF_01025}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAN49401.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE010300; AAN49401.1; ALT_INIT; Genomic_DNA.
DR RefSeq; NP_712383.1; NC_004342.2.
DR AlphaFoldDB; Q8F445; -.
DR SMR; Q8F445; -.
DR STRING; 189518.LA_2202; -.
DR EnsemblBacteria; AAN49401; AAN49401; LA_2202.
DR KEGG; lil:LA_2202; -.
DR PATRIC; fig|189518.3.peg.2193; -.
DR HOGENOM; CLU_022158_0_1_12; -.
DR InParanoid; Q8F445; -.
DR OMA; NTMRMLV; -.
DR UniPathway; UPA00048; UER00070.
DR Proteomes; UP000001408; Chromosome I.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0003852; F:2-isopropylmalate synthase activity; IBA:GO_Central.
DR GO; GO:0009098; P:leucine biosynthetic process; IBA:GO_Central.
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 1: Evidence at protein level;
KW Amino-acid biosynthesis; Branched-chain amino acid biosynthesis;
KW Leucine biosynthesis; Reference proteome; Transferase.
FT CHAIN 1..501
FT /note="2-isopropylmalate synthase 1"
FT /id="PRO_0000140358"
FT DOMAIN 7..269
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01151"
SQ SEQUENCE 501 AA; 54744 MW; 42367A0105493548 CRC64;
MDLKDYVRIF DTTLRDGEQC PGAAMTENEK LEIASQLATM KVDIIEAGFP VSSPVQFQAV
ERIARETEGP MIAALARAMK ADIEAASKAL QPAKKRRIHT FIASSPIHMK YKLGKEPKEV
LKMAVEAVTL CRQFVDDVEF SPEDATRSEP EFLRELCEAV IAAGATTINI PDTVGYTTPA
EYGGLFKFLL SNVRGAEKII FSAHCHNDLG LATANSLAAV QNGARQIECT INGIGERAGN
TAMEEVVMAM RTRKDTFGIQ TQIKTEEIAR ASYLVKTITG MLVQPNKAIV GANAFAHESG
IHQDGVIKHR ETYEIMKPET VGLSSNRMVL GRHSGRAGFK DRIVKLGFSP QVEELEAAYQ
RFLEIADRKK EIYDEDIRAL FSEEARKSTG DRFQLEGFTV STGTKSTPTA GVRILIDGHV
REESATGDGP VDAIYKAIQK TTGMDPEVSR LVISPVTEGQ DAMAEASVTL EYKGDRVVGK
GSSTDIIEAC SRAYISALNR L
