ID   TPIS_COPC7              Reviewed;         251 AA.
AC   Q12574; A8NNK1;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 2.
DT   03-AUG-2022, entry version 109.
DE   RecName: Full=Triosephosphate isomerase;
DE            Short=TIM;
DE            EC=5.3.1.1;
DE   AltName: Full=Triose-phosphate isomerase;
GN   Name=TPI; ORFNames=CC1G_07287;
OS   Coprinopsis cinerea (strain Okayama-7 / 130 / ATCC MYA-4618 / FGSC 9003)
OS   (Inky cap fungus) (Hormographiella aspergillata).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Psathyrellaceae; Coprinopsis.
OX   NCBI_TaxID=240176;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=7667320; DOI=10.1073/pnas.92.18.8507;
RA   Logsdon J.M. Jr., Tyshenko M.G., Dixon C., D-Jafari J., Walker V.K.,
RA   Palmer J.D.;
RT   "Seven newly discovered intron positions in the triose-phosphate isomerase
RT   gene: evidence for the introns-late theory.";
RL   Proc. Natl. Acad. Sci. U.S.A. 92:8507-8511(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Okayama-7 / 130 / ATCC MYA-4618 / FGSC 9003;
RX   PubMed=20547848; DOI=10.1073/pnas.1003391107;
RA   Stajich J.E., Wilke S.K., Ahren D., Au C.H., Birren B.W., Borodovsky M.,
RA   Burns C., Canbaeck B., Casselton L.A., Cheng C.K., Deng J., Dietrich F.S.,
RA   Fargo D.C., Farman M.L., Gathman A.C., Goldberg J., Guigo R., Hoegger P.J.,
RA   Hooker J.B., Huggins A., James T.Y., Kamada T., Kilaru S., Kodira C.,
RA   Kuees U., Kupfer D., Kwan H.S., Lomsadze A., Li W., Lilly W.W., Ma L.-J.,
RA   Mackey A.J., Manning G., Martin F., Muraguchi H., Natvig D.O.,
RA   Palmerini H., Ramesh M.A., Rehmeyer C.J., Roe B.A., Shenoy N., Stanke M.,
RA   Ter-Hovhannisyan V., Tunlid A., Velagapudi R., Vision T.J., Zeng Q.,
RA   Zolan M.E., Pukkila P.J.;
RT   "Insights into evolution of multicellular fungi from the assembled
RT   chromosomes of the mushroom Coprinopsis cinerea (Coprinus cinereus).";
RL   Proc. Natl. Acad. Sci. U.S.A. 107:11889-11894(2010).
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;
CC   -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.
CC   -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC       phosphate from glycerone phosphate: step 1/1.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the triosephosphate isomerase family.
CC       {ECO:0000305}.
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DR   EMBL; U23079; AAA79845.1; -; Genomic_DNA.
DR   EMBL; AACS02000012; EAU86629.1; -; Genomic_DNA.
DR   RefSeq; XP_001835145.1; XM_001835093.2.
DR   AlphaFoldDB; Q12574; -.
DR   SMR; Q12574; -.
DR   STRING; 5346.XP_001835145.1; -.
DR   PRIDE; Q12574; -.
DR   EnsemblFungi; EAU86629; EAU86629; CC1G_07287.
DR   GeneID; 6011672; -.
DR   KEGG; cci:CC1G_07287; -.
DR   VEuPathDB; FungiDB:CC1G_07287; -.
DR   eggNOG; KOG1643; Eukaryota.
DR   HOGENOM; CLU_024251_2_3_1; -.
DR   InParanoid; Q12574; -.
DR   OMA; QEVCGAI; -.
DR   OrthoDB; 1272577at2759; -.
DR   UniPathway; UPA00109; UER00189.
DR   UniPathway; UPA00138; -.
DR   Proteomes; UP000001861; Unassembled WGS sequence.
DR   GO; GO:0004807; F:triose-phosphate isomerase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006094; P:gluconeogenesis; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniPathway.
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   3: Inferred from homology;
KW   Gluconeogenesis; Glycolysis; Isomerase; Reference proteome.
FT   CHAIN           1..251
FT                   /note="Triosephosphate isomerase"
FT                   /id="PRO_0000090160"
FT   ACT_SITE        95
FT                   /note="Electrophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        167
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   CONFLICT        24
FT                   /note="L -> P (in Ref. 1; AAA79845)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   251 AA;  26884 MW;  AD94227FA6CD2133 CRC64;
     MTRSFFVGGN WKLNPTSLSA AKALVEALNK ADLDPSTEVV VAPPALYLLP IQEIAGKAVK
     VAAQNAYFKE SGAFTGEISP KQISDAGIPY VILGHSERRT LFHETSEVVA LKTRAALDNG
     LKVILCIGET LKEREEGRTA AVCEEQLSAV VKQLKEEDWS NIVIAYEPVW AIGTGKVATT
     SQAQETHVDV RKYLATAVSP KVASETRVIY GGSVNAANSK DLASQQDIDG FLVGGASLKP
     EFVDIINARK A