(data stored in ACNUC6288 zone)

SWISSPROT: TPIS_DEBHA

ID   TPIS_DEBHA              Reviewed;         248 AA.
AC   Q6BMB8;
DT   27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   08-MAY-2019, entry version 98.
DE   RecName: Full=Triosephosphate isomerase;
DE            Short=TIM;
DE            EC=5.3.1.1;
DE   AltName: Full=Triose-phosphate isomerase;
GN   Name=TPI1; OrderedLocusNames=DEHA2F06754g;
OS   Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / JCM 1990 / NBRC
OS   0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX   NCBI_TaxID=284592;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 36239 / CBS 767 / JCM 1990 / NBRC 0083 / IGC 2968;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S.,
RA   Lafontaine I., de Montigny J., Marck C., Neuveglise C., Talla E.,
RA   Goffard N., Frangeul L., Aigle M., Anthouard V., Babour A., Barbe V.,
RA   Barnay S., Blanchin S., Beckerich J.-M., Beyne E., Bleykasten C.,
RA   Boisrame A., Boyer J., Cattolico L., Confanioleri F., de Daruvar A.,
RA   Despons L., Fabre E., Fairhead C., Ferry-Dumazet H., Groppi A.,
RA   Hantraye F., Hennequin C., Jauniaux N., Joyet P., Kachouri R.,
RA   Kerrest A., Koszul R., Lemaire M., Lesur I., Ma L., Muller H.,
RA   Nicaud J.-M., Nikolski M., Oztas S., Ozier-Kalogeropoulos O.,
RA   Pellenz S., Potier S., Richard G.-F., Straub M.-L., Suleau A.,
RA   Swennen D., Tekaia F., Wesolowski-Louvel M., Westhof E., Wirth B.,
RA   Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M., Thierry A.,
RA   Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J.,
RA   Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-glyceraldehyde 3-phosphate = dihydroxyacetone
CC         phosphate; Xref=Rhea:RHEA:18585, ChEBI:CHEBI:57642,
CC         ChEBI:CHEBI:59776; 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}.
DR   EMBL; CR382138; CAG88985.1; -; Genomic_DNA.
DR   RefSeq; XP_460653.1; XM_460653.1.
DR   SMR; Q6BMB8; -.
DR   STRING; 4959.XP_460653.1; -.
DR   EnsemblFungi; CAG88985; CAG88985; DEHA2F06754g.
DR   GeneID; 2904121; -.
DR   KEGG; dha:DEHA2F06754g; -.
DR   HOGENOM; HOG000226413; -.
DR   InParanoid; Q6BMB8; -.
DR   KO; K01803; -.
DR   OMA; LCVGEGL; -.
DR   OrthoDB; 1272577at2759; -.
DR   UniPathway; UPA00109; UER00189.
DR   UniPathway; UPA00138; -.
DR   Proteomes; UP000000599; Chromosome F.
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;
DR   PRODOM; Q6BMB8.
DR   SWISS-2DPAGE; Q6BMB8.
KW   Complete proteome; Gluconeogenesis; Glycolysis; Isomerase;
KW   Reference proteome.
FT   CHAIN         1    248       Triosephosphate isomerase.
FT                                /FTId=PRO_0000090161.
FT   ACT_SITE     95     95       Electrophile. {ECO:0000250}.
FT   ACT_SITE    165    165       Proton acceptor. {ECO:0000250}.
FT   BINDING      10     10       Substrate. {ECO:0000250}.
FT   BINDING      12     12       Substrate. {ECO:0000250}.
SQ   SEQUENCE   248 AA;  26766 MW;  8BB219215B756304 CRC64;
     MARQFFVGGN FKMNGTRESV SKIVDGLNKA ELPSNVEVVI APPAPYIALA VNENKQKTIE
     VSAQNCFDKA SGAYTGEISP EQIKDLGATW TLTGHSERRT IIKESDDFIA SKTKFALDQG
     LSVILCIGET LEERKANVTL DVCARQLDAV ARVVSDWSKI VVAYEPVWAI GTGLAATPED
     AQETHKAIRE HLSKSIGADA AEKTRILYGG SVNGKNAPEF KDKADVDGFL VGGASLKPEF
     VDIIKSRL
//

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