TPIS_PARBA
ID TPIS_PARBA Reviewed; 249 AA.
AC Q96VN5; C1GVB2; Q870F0;
DT 27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-SEP-2009, sequence version 3.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Triosephosphate isomerase;
DE Short=TIM;
DE EC=5.3.1.1;
DE AltName: Full=Triose-phosphate isomerase;
GN Name=TPI1; Synonyms=TPI; ORFNames=PAAG_02585;
OS Paracoccidioides lutzii (strain ATCC MYA-826 / Pb01) (Paracoccidioides
OS brasiliensis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Onygenales incertae sedis; Paracoccidioides.
OX NCBI_TaxID=502779;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND PROTEIN SEQUENCE OF 87-97;
RP 144-158 AND 161-175.
RX PubMed=15310465; DOI=10.1016/j.micinf.2004.05.001;
RA Pereira L.A., Pereira M., Felipe M.S.S., Zancope-Oliveira R.M.,
RA de Almeida Soares C.M.;
RT "Proteomic identification, nucleotide sequence, heterologous expression and
RT immunological reactivity of the triosephosphate isomerase of
RT Paracoccidioides brasiliensis.";
RL Microbes Infect. 6:892-900(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-826 / Pb01;
RX PubMed=22046142; DOI=10.1371/journal.pgen.1002345;
RA Desjardins C.A., Champion M.D., Holder J.W., Muszewska A., Goldberg J.,
RA Bailao A.M., Brigido M.M., Ferreira M.E., Garcia A.M., Grynberg M.,
RA Gujja S., Heiman D.I., Henn M.R., Kodira C.D., Leon-Narvaez H.,
RA Longo L.V.G., Ma L.-J., Malavazi I., Matsuo A.L., Morais F.V., Pereira M.,
RA Rodriguez-Brito S., Sakthikumar S., Salem-Izacc S.M., Sykes S.M.,
RA Teixeira M.M., Vallejo M.C., Walter M.E., Yandava C., Young S., Zeng Q.,
RA Zucker J., Felipe M.S., Goldman G.H., Haas B.J., McEwen J.G., Nino-Vega G.,
RA Puccia R., San-Blas G., Soares C.M., Birren B.W., Cuomo C.A.;
RT "Comparative genomic analysis of human fungal pathogens causing
RT paracoccidioidomycosis.";
RL PLoS Genet. 7:E1002345-E1002345(2011).
RN [3]
RP PROTEIN SEQUENCE OF 161-175, AND INDUCTION.
RX PubMed=11418327; DOI=10.1016/s1286-4579(01)01409-5;
RA da Fonseca C.A., Jesuino R.S.A., Felipe M.S.S., Cunha D.A., Brito W.A.,
RA de Almeida Soares C.M.;
RT "Two-dimensional electrophoresis and characterization of antigens from
RT Paracoccidioides brasiliensis.";
RL Microbes Infect. 3:535-542(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;
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 -!- INDUCTION: Preferentially expressed in yeast cells, the host parasitic
CC phase. {ECO:0000269|PubMed:11418327}.
CC -!- PTM: The N-terminus is blocked.
CC -!- SIMILARITY: Belongs to the triosephosphate isomerase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EEH40530.2; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AY037936; AAK71466.2; -; Genomic_DNA.
DR EMBL; AY250089; AAP02959.2; -; mRNA.
DR EMBL; KN293996; EEH40530.2; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_002795879.2; XM_002795833.2.
DR AlphaFoldDB; Q96VN5; -.
DR SMR; Q96VN5; -.
DR STRING; 502779.Q96VN5; -.
DR MoonProt; Q96VN5; -.
DR PRIDE; Q96VN5; -.
DR EnsemblFungi; EEH40530; EEH40530; PAAG_02585.
DR GeneID; 9098797; -.
DR KEGG; pbl:PAAG_02585; -.
DR eggNOG; KOG1643; Eukaryota.
DR HOGENOM; CLU_024251_2_0_1; -.
DR OrthoDB; 1272577at2759; -.
DR UniPathway; UPA00109; UER00189.
DR UniPathway; UPA00138; -.
DR Proteomes; UP000002059; Partially assembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IDA:CAFA.
DR GO; GO:0009277; C:fungal-type cell wall; IDA:CAFA.
DR GO; GO:1990430; F:extracellular matrix protein binding; IDA:CAFA.
DR GO; GO:0004807; F:triose-phosphate isomerase activity; IDA:UniProtKB.
DR GO; GO:0044650; P:adhesion of symbiont to host cell; IDA:CAFA.
DR GO; GO:0061621; P:canonical glycolysis; IEA:EnsemblFungi.
DR GO; GO:0006094; P:gluconeogenesis; IEA:UniProtKB-UniPathway.
DR GO; GO:0006096; P:glycolytic process; IDA:UniProtKB.
DR GO; GO:2000535; P:regulation of entry of bacterium into host cell; IDA:CAFA.
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 CHAIN 1..249
FT /note="Triosephosphate isomerase"
FT /id="PRO_0000090166"
FT ACT_SITE 94
FT /note="Electrophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 166
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 205
FT /note="I -> T (in Ref. 1; AAK71466/AAP02959)"
FT /evidence="ECO:0000305"
FT CONFLICT 216
FT /note="N -> S (in Ref. 1; AAK71466/AAP02959)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 249 AA; 27062 MW; 64A1ECDE8C5058EC CRC64;
MPRKFFVGGN FKMNGTAKSI THIITNLNSA KLDPSTEIVI APPAIYLVLA RQLANGQVAV
SAQNVFDKPN GAFTGELSVE QLRDEKITWT LAGHSERRVL LREDDEFVAR KTKAAINGGL
NVILCIGESL EEREAGKTID VVTRQLDAVA EEVSPAEWNK VVIAYEPIWA IGTGKVATTE
QAQEVHASIR KWLNEKISPE AAENIRVIYG GSVTENNCRD LAAQPDVDGF LVGGASLKPA
FVDIINARL
