TPIS_SCHPO
ID TPIS_SCHPO Reviewed; 249 AA.
AC P07669; Q9P7I5;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Triosephosphate isomerase;
DE Short=TIM;
DE EC=5.3.1.1 {ECO:0000305|PubMed:3912263};
DE AltName: Full=Triose-phosphate isomerase;
GN Name=tpi1; Synonyms=tpi; ORFNames=SPCC24B10.21;
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 [GENOMIC DNA], CATALYTIC ACTIVITY, AND PATHWAY.
RX PubMed=3912263; DOI=10.1016/0378-1119(85)90031-9;
RA Russell P.R.;
RT "Transcription of the triose-phosphate-isomerase gene of
RT Schizosaccharomyces pombe initiates from a start point different from that
RT in Saccharomyces cerevisiae.";
RL Gene 40:125-130(1985).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 195-249.
RC STRAIN=SP808;
RX PubMed=7489897; DOI=10.1016/0378-1119(95)00412-y;
RA Ropp P.A., Copeland W.C.;
RT "Characterization of a new DNA polymerase from Schizosaccharomyces pombe: a
RT probable homologue of the Saccharomyces cerevisiae DNA polymerase gamma.";
RL Gene 165:103-107(1995).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-105 AND SER-199, 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 -!- CATALYTIC ACTIVITY:
CC Reaction=D-glyceraldehyde 3-phosphate = dihydroxyacetone phosphate;
CC Xref=Rhea:RHEA:18585, ChEBI:CHEBI:57642, ChEBI:CHEBI:59776;
CC EC=5.3.1.1; Evidence={ECO:0000305|PubMed:3912263};
CC -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.
CC {ECO:0000305|PubMed:3912263}.
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC phosphate from glycerone phosphate: step 1/1.
CC {ECO:0000305|PubMed:3912263}.
CC -!- SUBUNIT: Homodimer.
CC -!- SIMILARITY: Belongs to the triosephosphate isomerase family.
CC {ECO:0000305}.
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DR EMBL; M14432; AAA35348.1; -; Genomic_DNA.
DR EMBL; CU329672; CAB76230.1; -; Genomic_DNA.
DR EMBL; Z47976; CAA88011.1; -; Genomic_DNA.
DR PIR; A23987; ISZPT.
DR PIR; T50428; T50428.
DR RefSeq; NP_588024.1; NM_001023015.2.
DR AlphaFoldDB; P07669; -.
DR SMR; P07669; -.
DR BioGRID; 275313; 5.
DR STRING; 4896.SPCC24B10.21.1; -.
DR iPTMnet; P07669; -.
DR MaxQB; P07669; -.
DR PaxDb; P07669; -.
DR PRIDE; P07669; -.
DR EnsemblFungi; SPCC24B10.21.1; SPCC24B10.21.1:pep; SPCC24B10.21.
DR GeneID; 2538729; -.
DR KEGG; spo:SPCC24B10.21; -.
DR PomBase; SPCC24B10.21; tpi1.
DR VEuPathDB; FungiDB:SPCC24B10.21; -.
DR eggNOG; KOG1643; Eukaryota.
DR HOGENOM; CLU_024251_2_0_1; -.
DR InParanoid; P07669; -.
DR OMA; QEVCGAI; -.
DR PhylomeDB; P07669; -.
DR Reactome; R-SPO-70171; Glycolysis.
DR Reactome; R-SPO-70263; Gluconeogenesis.
DR UniPathway; UPA00109; UER00189.
DR UniPathway; UPA00138; -.
DR PRO; PR:P07669; -.
DR Proteomes; UP000002485; Chromosome III.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0004807; F:triose-phosphate isomerase activity; IGI:PomBase.
DR GO; GO:0061621; P:canonical glycolysis; IGI:PomBase.
DR GO; GO:0006094; P:gluconeogenesis; IBA:GO_Central.
DR GO; GO:0046166; P:glyceraldehyde-3-phosphate biosynthetic process; IBA:GO_Central.
DR GO; GO:0019563; P:glycerol catabolic process; IBA:GO_Central.
DR GO; GO:0006096; P:glycolytic process; IBA:GO_Central.
DR CDD; cd00311; TIM; 1.
DR Gene3D; 3.20.20.70; -; 1.
DR HAMAP; MF_00147_B; TIM_B; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR035990; TIM_sf.
DR InterPro; IPR022896; TrioseP_Isoase_bac/euk.
DR InterPro; IPR000652; Triosephosphate_isomerase.
DR InterPro; IPR020861; Triosephosphate_isomerase_AS.
DR PANTHER; PTHR21139; PTHR21139; 1.
DR Pfam; PF00121; TIM; 1.
DR SUPFAM; SSF51351; SSF51351; 1.
DR TIGRFAMs; TIGR00419; tim; 1.
DR PROSITE; PS00171; TIM_1; 1.
DR PROSITE; PS51440; TIM_2; 1.
PE 1: Evidence at protein level;
KW Gluconeogenesis; Glycolysis; Isomerase; Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT CHAIN 2..249
FT /note="Triosephosphate isomerase"
FT /id="PRO_0000090167"
FT ACT_SITE 95
FT /note="Electrophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 165
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 10
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 12
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MOD_RES 105
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 199
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT CONFLICT 87
FT /note="G -> A (in Ref. 1; AAA35348)"
FT /evidence="ECO:0000305"
FT CONFLICT 133
FT /note="E -> D (in Ref. 1; AAA35348)"
FT /evidence="ECO:0000305"
FT CONFLICT 141
FT /note="N -> T (in Ref. 1; AAA35348)"
FT /evidence="ECO:0000305"
FT CONFLICT 176
FT /note="A -> G (in Ref. 1; AAA35348)"
FT /evidence="ECO:0000305"
FT CONFLICT 180
FT /note="Q -> E (in Ref. 1; AAA35348)"
FT /evidence="ECO:0000305"
FT CONFLICT 213
FT /note="N -> T (in Ref. 1; AAA35348)"
FT /evidence="ECO:0000305"
FT CONFLICT 241
FT /note="H -> PT (in Ref. 1)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 249 AA; 27227 MW; 63A8724D7794CF32 CRC64;
MARKFFVGGN FKMNGSLESM KTIIEGLNTT KLNVGDVETV IFPQNMYLIT TRQQVKKDIG
VGAQNVFDKK NGAYTGENSA QSLIDAGITY TLTGHSERRT IFKESDEFVA DKTKFALEQG
LTVVACIGET LAEREANETI NVVVRQLNAI ADKVQNWSKI VIAYEPVWAI GTGKTATPEQ
AQEVHAEIRK WATNKLGASV AEGLRVIYGG SVNGGNCKEF LKFHDIDGFL VGGASLKPEF
HNIVNVHSL
