LEU1_SCHPO
ID LEU1_SCHPO Reviewed; 584 AA.
AC O59736;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 2.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=2-isopropylmalate synthase;
DE EC=2.3.3.13;
DE AltName: Full=Alpha-IPM synthase;
DE AltName: Full=Alpha-isopropylmalate synthase;
GN Name=leu3; ORFNames=SPBC3E7.16c, SPBC4F6.03c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
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).
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 -!- PATHWAY: Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine
CC from 3-methyl-2-oxobutanoate: step 1/4.
CC -!- SIMILARITY: Belongs to the alpha-IPM synthase/homocitrate synthase
CC family. LeuA type 2 subfamily. {ECO:0000305}.
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DR EMBL; CU329671; CAA19019.1; -; Genomic_DNA.
DR PIR; T40500; T40500.
DR RefSeq; NP_596103.2; NM_001022019.3.
DR AlphaFoldDB; O59736; -.
DR SMR; O59736; -.
DR BioGRID; 277518; 8.
DR STRING; 4896.SPBC3E7.16c.1; -.
DR iPTMnet; O59736; -.
DR SwissPalm; O59736; -.
DR MaxQB; O59736; -.
DR PaxDb; O59736; -.
DR PRIDE; O59736; -.
DR EnsemblFungi; SPBC3E7.16c.1; SPBC3E7.16c.1:pep; SPBC3E7.16c.
DR GeneID; 2541003; -.
DR KEGG; spo:SPBC3E7.16c; -.
DR PomBase; SPBC3E7.16c; leu3.
DR VEuPathDB; FungiDB:SPBC3E7.16c; -.
DR eggNOG; KOG2367; Eukaryota.
DR HOGENOM; CLU_004588_3_0_1; -.
DR InParanoid; O59736; -.
DR OMA; WPDKVID; -.
DR PhylomeDB; O59736; -.
DR UniPathway; UPA00048; UER00070.
DR PRO; PR:O59736; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005739; C:mitochondrion; HDA:PomBase.
DR GO; GO:0003852; F:2-isopropylmalate synthase activity; ISS:PomBase.
DR GO; GO:0009098; P:leucine biosynthetic process; IMP:PomBase.
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..584
FT /note="2-isopropylmalate synthase"
FT /id="PRO_0000140445"
FT DOMAIN 45..323
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01151"
SQ SEQUENCE 584 AA; 64042 MW; 9371A03F82C032F6 CRC64;
MKSTFEAAGR VAKGMLKDPS KKYKPFKGIQ LPNRQWPNKV LTKAPRWLST DLRDGNQALP
DPMNGQEKLR YFKLLCSIGF KEIEVGFPSA SQTDFAFVRH LIETPGLIPD DVTISALTPS
REPLILRTIE ALRGAKNATV HLYNACSPLF REVVFRNSKQ ETLDLAIKGS KIVTAATKNA
LESKETNWGF EYSPETFSDT EPDFALEVCE AVKGMWKPSA AQPIIFNLPA TVEMSTPNTY
ADLIEYFSTN ISEREKVCVS LHPHNDRGTA VAAAELGQLA GGDRIEGCLF GNGERTGNVD
LVTLAFNLYT QGVSPNLDFS KLDEIIRITE DCNKINVHPR HPYAGNLVFT AFSGSHQDAI
SKGLKAYDER KAVDPVWKVP YLPLDPHDVN SEYAAIIRVN SQSGKGGVAY LLKTNCGLDL
PRALQVEFGS IVKDYSDTKG KELSIGEISD LFYTTYYLEF PGRFSVNDYT LSSNGPQSKC
IKCVVDIKGE KKDTPSRVVI EGVGNGPLSA LVDALRRQFN ISFDIGQYSE HAIGSGNGVK
AASYVEIIFN NTSFWGVGID ADVTSAGLKA VMSGVSRASR AFAK
