ID   TPIS_BOMMO              Reviewed;         248 AA.
AC   P82204; P82220; Q643R1;
DT   09-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 2.
DT   03-AUG-2022, entry version 85.
DE   RecName: Full=Triosephosphate isomerase;
DE            Short=TIM;
DE            EC=5.3.1.1;
DE   AltName: Full=Triose-phosphate isomerase;
GN   Name=Tpi;
OS   Bombyx mori (Silk moth).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Bombycoidea;
OC   Bombycidae; Bombycinae; Bombyx.
OX   NCBI_TaxID=7091;
RN   [1] {ECO:0000312|EMBL:AAU34185.1}
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Niu B.L., Meng Z.Q., Lu S.L.;
RT   "Triosephosphate isomerase (Tpi) gene from Bombyx mori.";
RL   Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000305}
RP   PROTEIN SEQUENCE OF 2-25.
RC   STRAIN=Xinhang X Keming {ECO:0000269|PubMed:11280994};
RC   TISSUE=Body wall {ECO:0000269|PubMed:11280994}, and
RC   Fat body {ECO:0000269|PubMed:11280994};
RX   PubMed=11280994;
RA   Zhong B.-X.;
RT   "Protein database for several tissues derived from five instar of
RT   silkworm.";
RL   Yi Chuan Xue Bao 28:217-224(2001).
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};
CC   -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis. {ECO:0000305}.
CC   -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC       phosphate from glycerone phosphate: step 1/1.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P60174}.
CC   -!- SIMILARITY: Belongs to the triosephosphate isomerase family.
CC       {ECO:0000255}.
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DR   EMBL; AY734490; AAU34185.1; -; Genomic_DNA.
DR   RefSeq; NP_001119730.1; NM_001126258.1.
DR   AlphaFoldDB; P82204; -.
DR   SMR; P82204; -.
DR   GeneID; 100146104; -.
DR   KEGG; bmor:100146104; -.
DR   CTD; 43582; -.
DR   eggNOG; KOG1643; Eukaryota.
DR   InParanoid; P82204; -.
DR   OrthoDB; 1272577at2759; -.
DR   UniPathway; UPA00109; UER00189.
DR   UniPathway; UPA00138; -.
DR   Proteomes; UP000005204; 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   1: Evidence at protein level;
KW   Direct protein sequencing; Gluconeogenesis; Glycolysis; Isomerase;
KW   Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:11280994"
FT   CHAIN           2..248
FT                   /note="Triosephosphate isomerase"
FT                   /evidence="ECO:0000269|PubMed:11280994"
FT                   /id="PRO_0000090126"
FT   ACT_SITE        94
FT                   /note="Electrophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        165
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         12
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        21
FT                   /note="N -> I (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        25
FT                   /note="N -> V (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   248 AA;  26779 MW;  A5047E83A7111D53 CRC64;
     MGRKFVVGGN WKMNGDKNQI NEIVNNLKKG PLDPNVEVIV GVPAIYLSYV KTIIPDNVEV
     AAQNCWKSPK GAFTGEISPA MIKDVGVNWV ILGHSERRTI FGEKDELVAE KVAHALESGL
     KVIACIGETL EERESGKTEE VVFRQLKALV SAIGDKWENI VLAYEPVWAI GTGKTATPQQ
     AQDVHHALRN WLSANVSGSV SDAVRIQYGG SVTAANAKEL ASCKDIDGFL VGGASLKPEF
     VEIVNANQ