TPIS_CANAL
ID TPIS_CANAL Reviewed; 248 AA.
AC Q9P940; A0A1D8PKS9; P82613; Q5ADU6; Q9P848;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Triosephosphate isomerase;
DE Short=TIM;
DE EC=5.3.1.1;
DE AltName: Full=Triose-phosphate isomerase;
GN Name=TPI1; OrderedLocusNames=CAALFM_C307440WA;
GN ORFNames=CaO19.14037, CaO19.6745;
OS Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=237561;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=11231556; DOI=10.1038/85677;
RA De Backer M.D., Nelissen B., Logghe M., Viaene J., Loonen I.,
RA Vandoninck S., de Hoogt R., Dewaele S., Simons F.A., Verhasselt P.,
RA Vanhoof G., Contreras R., Luyten W.H.M.L.;
RT "An antisense-based functional genomics approach for identification of
RT genes critical for growth of Candida albicans.";
RL Nat. Biotechnol. 19:235-241(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=1161;
RX PubMed=11124701;
RX DOI=10.1002/1097-0061(200101)18:1<49::aid-yea646>3.0.co;2-m;
RA Hoyer L.L., Hecht J.E.;
RT "The ALS5 gene of Candida albicans and analysis of the Als5p N-terminal
RT domain.";
RL Yeast 18:49-60(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA Scherer S.;
RT "The diploid genome sequence of Candida albicans.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA Chibana H., Nantel A., Magee P.T.;
RT "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT on the eight chromosomes.";
RL Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT specific measurements and provides a simple model for repeat and indel
RT structure.";
RL Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
RN [6]
RP PROTEIN SEQUENCE OF 2-11.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX DOI=10.1002/1615-9861(200104)1:4<550::AID-PROT550>3.0.CO;2-W;
RA Pitarch A., Diez-Orejas R., Molero G., Pardo M., Sanchez M., Gil C.,
RA Nombela C.;
RT "Analysis of the serologic response to systemic Candida albicans infection
RT in a murine model.";
RL Proteomics 1:550-559(2001).
RN [7]
RP PROTEIN SEQUENCE OF 123-134 AND 139-145, SUBCELLULAR LOCATION, AND
RP ANTIGENICITY.
RC STRAIN=SC5314 / ATCC MYA-2876; TISSUE=Protoplast;
RX PubMed=15378761; DOI=10.1002/pmic.200400903;
RA Pitarch A., Abian J., Carrascal M., Sanchez M., Nombela C., Gil C.;
RT "Proteomics-based identification of novel Candida albicans antigens for
RT diagnosis of systemic candidiasis in patients with underlying hematological
RT malignancies.";
RL Proteomics 4:3084-3106(2004).
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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15378761}.
CC -!- MISCELLANEOUS: Has antigenic properties.
CC -!- MISCELLANEOUS: Critical for growth.
CC -!- SIMILARITY: Belongs to the triosephosphate isomerase family.
CC {ECO:0000305}.
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DR EMBL; AJ390491; CAB77631.1; -; mRNA.
DR EMBL; AF124845; AAF28895.1; -; Genomic_DNA.
DR EMBL; CP017625; AOW28746.1; -; Genomic_DNA.
DR RefSeq; XP_719842.1; XM_714749.1.
DR AlphaFoldDB; Q9P940; -.
DR SMR; Q9P940; -.
DR BioGRID; 1221576; 1.
DR STRING; 237561.Q9P940; -.
DR COMPLUYEAST-2DPAGE; Q9P940; -.
DR PRIDE; Q9P940; -.
DR GeneID; 3638482; -.
DR KEGG; cal:CAALFM_C307440WA; -.
DR CGD; CAL0000173961; TPI1.
DR VEuPathDB; FungiDB:C3_07440W_A; -.
DR eggNOG; KOG1643; Eukaryota.
DR HOGENOM; CLU_024251_2_1_1; -.
DR InParanoid; Q9P940; -.
DR OMA; QEVCGAI; -.
DR OrthoDB; 1272577at2759; -.
DR UniPathway; UPA00109; UER00189.
DR UniPathway; UPA00138; -.
DR PRO; PR:Q9P940; -.
DR Proteomes; UP000000559; Chromosome 3.
DR GO; GO:0009986; C:cell surface; IDA:CGD.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0062040; C:fungal biofilm matrix; IDA:CGD.
DR GO; GO:0009277; C:fungal-type cell wall; IDA:CGD.
DR GO; GO:0030446; C:hyphal cell wall; IDA:CGD.
DR GO; GO:0004807; F:triose-phosphate isomerase activity; IBA:GO_Central.
DR GO; GO:0061621; P:canonical glycolysis; IEA:EnsemblFungi.
DR GO; GO:0009267; P:cellular response to starvation; IMP:CGD.
DR GO; GO:0030447; P:filamentous growth; IMP:CGD.
DR GO; GO:0036180; P:filamentous growth of a population of unicellular organisms in response to biotic stimulus; IMP:CGD.
DR GO; GO:0036170; P:filamentous growth of a population of unicellular organisms in response to starvation; IMP:CGD.
DR GO; GO:0006094; P:gluconeogenesis; IBA:GO_Central.
DR GO; GO:0046166; P:glyceraldehyde-3-phosphate biosynthetic process; IBA:GO_Central.
DR GO; GO:0019563; P:glycerol catabolic process; IBA:GO_Central.
DR GO; GO:0006096; P:glycolytic process; IBA:GO_Central.
DR GO; GO:0044416; P:induction by symbiont of host defense response; IDA:CGD.
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 Cytoplasm; Direct protein sequencing; Gluconeogenesis; Glycolysis;
KW Isomerase; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.6"
FT CHAIN 2..248
FT /note="Triosephosphate isomerase"
FT /id="PRO_0000090158"
FT ACT_SITE 95
FT /note="Electrophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 165
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 195
FT /note="S -> T (in Ref. 1; CAB77631)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 248 AA; 26611 MW; 732EBBFE55BB7A10 CRC64;
MARQFFVGGN FKANGTKQQI TSIIDNLNKA DLPKDVEVVI CPPALYLGLA VEQNKQPTVA
IGAQNVFDKS CGAFTGETCA SQILDVGASW TLTGHSERRT IIKESDEFIA EKTKFALDTG
VKVILCIGET LEERKGGVTL DVCARQLDAV SKIVSDWSNI VVAYEPVWAI GTGLAATPED
AEETHKGIRA HLAKSIGAEQ AEKTRILYGG SVNGKNAKDF KDKANVDGFL VGGASLKPEF
VDIIKSRL
