TPIS_DROYA
ID TPIS_DROYA Reviewed; 247 AA.
AC O77458; Q6XIW2;
DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Triosephosphate isomerase;
DE Short=TIM;
DE EC=5.3.1.1;
DE AltName: Full=Triose-phosphate isomerase;
GN Name=Tpi;
OS Drosophila yakuba (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7245;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9615457; DOI=10.1093/oxfordjournals.molbev.a025979;
RA Hasson E., Wang I.-N., Zeng L.-W., Kreitman M., Eanes W.F.;
RT "Nucleotide variation in the triosephosphate isomerase (Tpi) locus of
RT Drosophila melanogaster and D. simulans.";
RL Mol. Biol. Evol. 15:756-769(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 78-247.
RX PubMed=14525923; DOI=10.1101/gr.1311003;
RA Domazet-Loso T., Tautz D.;
RT "An evolutionary analysis of orphan genes in Drosophila.";
RL Genome Res. 13:2213-2219(2003).
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.
CC -!- SIMILARITY: Belongs to the triosephosphate isomerase family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U60870; AAC39075.1; -; Genomic_DNA.
DR EMBL; AY231717; AAR09740.1; -; mRNA.
DR AlphaFoldDB; O77458; -.
DR SMR; O77458; -.
DR STRING; 7245.FBpp0268422; -.
DR eggNOG; KOG1643; Eukaryota.
DR UniPathway; UPA00109; UER00189.
DR UniPathway; UPA00138; -.
DR GO; GO:0004807; F:triose-phosphate isomerase activity; ISS:UniProtKB.
DR GO; GO:0006094; P:gluconeogenesis; IEA:UniProtKB-UniPathway.
DR GO; GO:0019682; P:glyceraldehyde-3-phosphate metabolic process; ISS:UniProtKB.
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 2: Evidence at transcript level;
KW Gluconeogenesis; Glycolysis; Isomerase.
FT CHAIN 1..247
FT /note="Triosephosphate isomerase"
FT /id="PRO_0000090132"
FT ACT_SITE 94
FT /note="Electrophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 164
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 100
FT /note="I -> V (in Ref. 2; AAR09740)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 247 AA; 26626 MW; 68D7C0269A80C3CB CRC64;
MSRKFCVGGN WKMNGDQKSI AEIAKTLSSA ALDPNTEVVI GCPAIYLMYA RNLLPCELGL
AGQNAYKVAK GAFTGEISPA MLKDIGADWV ILGHSERRAI FGESDALIAE KAEHALAEGL
KVIACIGETL EEREAGKTNE VVARQMCAYA QKIKDWKNVV VAYEPVWAIG TGKTATPDQA
QEVHAFLRQW LSDNISKEVS ASLRIQYGGS VTAANAKELA KKPDIDGFLV GGASLKPEFV
DIINARQ