TPIS_CULTA
ID TPIS_CULTA Reviewed; 247 AA.
AC P30741;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Triosephosphate isomerase;
DE Short=TIM;
DE EC=5.3.1.1;
DE AltName: Full=Triose-phosphate isomerase;
GN Name=Tpi;
OS Culex tarsalis (Encephalitis mosquito).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Culicinae; Culicini; Culex; Culex.
OX NCBI_TaxID=7177;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-27.
RX PubMed=8429888; DOI=10.1038/361470a0;
RA Tittiger C., Whyard S., Walker V.K.;
RT "A novel intron site in the triosephosphate isomerase gene from the
RT mosquito Culex tarsalis.";
RL Nature 361:470-472(1993).
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}.
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DR EMBL; L07390; AAA73976.1; -; Genomic_DNA.
DR PIR; S29716; S29716.
DR AlphaFoldDB; P30741; -.
DR SMR; P30741; -.
DR PRIDE; P30741; -.
DR UniPathway; UPA00109; UER00189.
DR UniPathway; UPA00138; -.
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.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:8429888"
FT CHAIN 2..247
FT /note="Triosephosphate isomerase"
FT /id="PRO_0000090129"
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"
SQ SEQUENCE 247 AA; 26389 MW; F5B84AB1765D9022 CRC64;
MGRKFCVGGN WKMNGDKASI ADLCKVLTTG PLNADTEVVV GCPAPYLTLA RSQLPDSVCV
AAQNCYKVPK GAFTGEISPA MLKDLNIGWV ILGHSERRAI FGESDELIAD KVAHALAEGL
KVIACIGETL QEREAGQTEA VCFRQTKAIA DKVKDWSNVV IAYEPVWAIG TGKTASPEQA
QEVHAALRKW FTENVSADVS AAIRIQYGGS VTAANCRELA AKPDIDGFLV GGASLKPEFI
QIVNARQ