LEUC_SCHPO
ID LEUC_SCHPO Reviewed; 758 AA.
AC O14289;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=3-isopropylmalate dehydratase;
DE EC=4.2.1.33;
DE AltName: Full=Alpha-IPM isomerase;
DE Short=IPMI;
DE AltName: Full=Isopropylmalate isomerase;
GN Name=leu2; ORFNames=SPAC9E9.03;
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).
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-486 AND SER-488, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=18257517; DOI=10.1021/pr7006335;
RA Wilson-Grady J.T., Villen J., Gygi S.P.;
RT "Phosphoproteome analysis of fission yeast.";
RL J. Proteome Res. 7:1088-1097(2008).
CC -!- FUNCTION: Catalyzes the isomerization between 2-isopropylmalate and 3-
CC isopropylmalate, via the formation of 2-isopropylmaleate.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2R,3S)-3-isopropylmalate = (2S)-2-isopropylmalate;
CC Xref=Rhea:RHEA:32287, ChEBI:CHEBI:1178, ChEBI:CHEBI:35121;
CC EC=4.2.1.33;
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000250};
CC Note=Binds 1 [4Fe-4S] cluster per subunit. {ECO:0000250};
CC -!- PATHWAY: Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine
CC from 3-methyl-2-oxobutanoate: step 2/4.
CC -!- SIMILARITY: Belongs to the aconitase/IPM isomerase family.
CC {ECO:0000305}.
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DR EMBL; CU329670; CAB16402.1; -; Genomic_DNA.
DR PIR; T39210; T39210.
DR RefSeq; NP_594576.1; NM_001020005.2.
DR AlphaFoldDB; O14289; -.
DR SMR; O14289; -.
DR BioGRID; 279721; 22.
DR STRING; 4896.SPAC9E9.03.1; -.
DR iPTMnet; O14289; -.
DR MaxQB; O14289; -.
DR PaxDb; O14289; -.
DR PRIDE; O14289; -.
DR EnsemblFungi; SPAC9E9.03.1; SPAC9E9.03.1:pep; SPAC9E9.03.
DR GeneID; 2543296; -.
DR KEGG; spo:SPAC9E9.03; -.
DR PomBase; SPAC9E9.03; leu2.
DR VEuPathDB; FungiDB:SPAC9E9.03; -.
DR eggNOG; KOG0454; Eukaryota.
DR HOGENOM; CLU_006714_1_2_1; -.
DR InParanoid; O14289; -.
DR OMA; DHIVNEQ; -.
DR PhylomeDB; O14289; -.
DR UniPathway; UPA00048; UER00071.
DR PRO; PR:O14289; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0009316; C:3-isopropylmalate dehydratase complex; IEA:InterPro.
DR GO; GO:0003861; F:3-isopropylmalate dehydratase activity; ISO:PomBase.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0009098; P:leucine biosynthetic process; EXP:PomBase.
DR CDD; cd01583; IPMI; 1.
DR CDD; cd01577; IPMI_Swivel; 1.
DR Gene3D; 3.20.19.10; -; 1.
DR Gene3D; 3.30.499.10; -; 2.
DR HAMAP; MF_01026; LeuC_type1; 1.
DR HAMAP; MF_01031; LeuD_type1; 1.
DR InterPro; IPR004430; 3-IsopropMal_deHydase_lsu.
DR InterPro; IPR004431; 3-IsopropMal_deHydase_ssu.
DR InterPro; IPR012235; 3-IsopropMal_deHydtase_ssu/lsu.
DR InterPro; IPR015931; Acnase/IPM_dHydase_lsu_aba_1/3.
DR InterPro; IPR001030; Acoase/IPM_deHydtase_lsu_aba.
DR InterPro; IPR015928; Aconitase/3IPM_dehydase_swvl.
DR InterPro; IPR018136; Aconitase_4Fe-4S_BS.
DR InterPro; IPR036008; Aconitase_4Fe-4S_dom.
DR InterPro; IPR000573; AconitaseA/IPMdHydase_ssu_swvl.
DR InterPro; IPR033941; IPMI_cat.
DR InterPro; IPR033940; IPMI_Swivel.
DR Pfam; PF00330; Aconitase; 1.
DR Pfam; PF00694; Aconitase_C; 1.
DR PIRSF; PIRSF001418; ACN; 1.
DR PRINTS; PR00415; ACONITASE.
DR SUPFAM; SSF53732; SSF53732; 1.
DR TIGRFAMs; TIGR00170; leuC; 1.
DR TIGRFAMs; TIGR00171; leuD; 1.
DR PROSITE; PS00450; ACONITASE_1; 1.
DR PROSITE; PS01244; ACONITASE_2; 1.
PE 1: Evidence at protein level;
KW 4Fe-4S; Amino-acid biosynthesis; Branched-chain amino acid biosynthesis;
KW Iron; Iron-sulfur; Leucine biosynthesis; Lyase; Metal-binding;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..758
FT /note="3-isopropylmalate dehydratase"
FT /id="PRO_0000076892"
FT BINDING 359
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 420
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 423
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT MOD_RES 486
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 488
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 758 AA; 82783 MW; CE78C36828380E47 CRC64;
MSPSVASPKT LYDKVWDSHV VDLQEDGTCL LYIDRHLIHE VTSPQAFEGL RTAGRKVRHP
ELALATVDHN IPTDPRKDMK DIASFIHQPD SRTQVLALEN NIKEFGLTYY GMNDRRQGIV
HVIGPEQGFT LPGTTLVCGD SHTSTHGAFG ALAFGIGTSE VEHVLATQTI LQRKSKNMRI
RVNGKLPEGI ASKDLILHII GVIGTAGGTG SVIEFCGEAI EGLSMEARMS MCNMSIEAGA
RAGMIAPDAT TFEYVKNRPL APKGDDWEQA VAYWKTLRSD ENAKYDIEVE INAADVLPTV
TWGTSPQDVI PINGNIPDPA HVKDNVRAAS IQRSLEYMGL KPNTSIVSYP IDKVFIGSCT
NSRIEDLRLA AAVVKGRKVA ANVKDAMIVP GSGLVKKMAE AEGLDQIFIE AGFDWREAGC
SMCLGMNPDQ LKPYERCAST SNRNFEGRQG AKGRTHLVSP AMAAAAAIKG HLCNVREFFG
DVSNGSPSII TNKNYDPSHD VEGDIGLSVD DATDAVTDAD GIATNVAGSV SSGSAGIPKF
TVVEGIAAPL PMANVDTDKI IPKQFLKTIK RTGLGQFAFY EIRYDADGKE IPDFVLNREP
YRHATVLVAH DNFGCGSSRE HAPWALNDFG IRVIIAPSFA DIFFNNCFKN GMLPIPTPIE
QVNDMMKAAE NQVKFSVDLV NQTITYGDKQ VKFDVEPFRK HCLVNGLDDI GLTLQKETMI
DAFEAAREEN FPWMNIKRSR ARLSPVKSNK QSSSRNDW
