TPP_ENCCU
ID TPP_ENCCU Reviewed; 718 AA.
AC Q8SSL0; O96721;
DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 25-MAY-2022, entry version 96.
DE RecName: Full=Probable trehalose-phosphatase;
DE EC=3.1.3.12;
DE AltName: Full=Trehalose-6-phosphate phosphatase;
DE Short=TPP;
GN OrderedLocusNames=ECU01_0870;
OS Encephalitozoon cuniculi (strain GB-M1) (Microsporidian parasite).
OC Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Unikaryonidae;
OC Encephalitozoon.
OX NCBI_TaxID=284813;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Duffieux F., Peyret P., Roe B.A., Vivares C.P.;
RT "Putative trehalose 6-phosphate phosphatase from the chromosome I of
RT Encephalitozoon cuniculi (Microspora).";
RL Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GB-M1;
RX PubMed=11157783; DOI=10.1101/gr.164301;
RA Peyret P., Katinka M.D., Duprat S., Duffieux F., Barbe V., Barbazanges M.,
RA Weissenbach J., Saurin W., Vivares C.P.;
RT "Sequence and analysis of chromosome I of the amitochondriate intracellular
RT parasite Encephalitozoon cuniculi (Microspora).";
RL Genome Res. 11:198-207(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GB-M1;
RX PubMed=11719806; DOI=10.1038/35106579;
RA Katinka M.D., Duprat S., Cornillot E., Metenier G., Thomarat F.,
RA Prensier G., Barbe V., Peyretaillade E., Brottier P., Wincker P.,
RA Delbac F., El Alaoui H., Peyret P., Saurin W., Gouy M., Weissenbach J.,
RA Vivares C.P.;
RT "Genome sequence and gene compaction of the eukaryote parasite
RT Encephalitozoon cuniculi.";
RL Nature 414:450-453(2001).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], AND
RP DEVELOPMENTAL STAGE.
RX PubMed=16691553; DOI=10.1002/pmic.200500796;
RA Brosson D., Kuhn L., Delbac F., Garin J., Vivares C.P., Texier C.;
RT "Proteomic analysis of the eukaryotic parasite Encephalitozoon cuniculi
RT (microsporidia): a reference map for proteins expressed in late sporogonial
RT stages.";
RL Proteomics 6:3625-3635(2006).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=alpha,alpha-trehalose 6-phosphate + H2O = alpha,alpha-
CC trehalose + phosphate; Xref=Rhea:RHEA:23420, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:16551, ChEBI:CHEBI:43474, ChEBI:CHEBI:58429; EC=3.1.3.12;
CC -!- DEVELOPMENTAL STAGE: Expressed in late sporogonial stages.
CC {ECO:0000269|PubMed:16691553}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the
CC glycosyltransferase 20 family. {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the trehalose
CC phosphatase family. {ECO:0000305}.
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DR EMBL; AJ006825; CAA07262.1; -; Genomic_DNA.
DR EMBL; AL391737; CAD24957.1; -; Genomic_DNA.
DR RefSeq; XP_965922.1; XM_960829.1.
DR AlphaFoldDB; Q8SSL0; -.
DR SMR; Q8SSL0; -.
DR STRING; 284813.Q8SSL0; -.
DR CAZy; GT20; Glycosyltransferase Family 20.
DR GeneID; 860263; -.
DR KEGG; ecu:ECU01_0870; -.
DR VEuPathDB; MicrosporidiaDB:ECU01_0870; -.
DR HOGENOM; CLU_002351_3_3_1; -.
DR InParanoid; Q8SSL0; -.
DR OMA; RMAYYSI; -.
DR OrthoDB; 772297at2759; -.
DR Proteomes; UP000000819; Chromosome I.
DR GO; GO:0004805; F:trehalose-phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0005992; P:trehalose biosynthetic process; IEA:InterPro.
DR Gene3D; 3.40.50.1000; -; 1.
DR InterPro; IPR001830; Glyco_trans_20.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR003337; Trehalose_PPase.
DR PANTHER; PTHR10788; PTHR10788; 2.
DR Pfam; PF00982; Glyco_transf_20; 1.
DR Pfam; PF02358; Trehalose_PPase; 1.
DR SUPFAM; SSF56784; SSF56784; 1.
DR TIGRFAMs; TIGR00685; T6PP; 1.
PE 1: Evidence at protein level;
KW Hydrolase; Reference proteome.
FT CHAIN 1..718
FT /note="Probable trehalose-phosphatase"
FT /id="PRO_0000122507"
FT REGION 449..470
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 421
FT /note="R -> K (in Ref. 1; CAA07262)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 718 AA; 82064 MW; B82FC7D318854CD5 CRC64;
MKIIVAAEEL PICASRMEPS EAIKNWISTP LKKIPHPDKA SKIQIEFGDR SKESLHLFAK
PHFMVPDMLD DDEMFFVGAP GFYSPEEFSD EDCRRIEESM KAYRCYPIFQ KRVKYSKMIE
EILGKNTYEF VQSNFDHANM FARYKEYNTR WHEKIMEIYE EGDVVWVMDH SLFLLPGMLG
NSIPVGMSAS VPFSSLLKCI PFWEQIFSSI LCCRYIEFNE SSSKESFDLL VSQKTGFCMG
DPGYKDIREP LTCVGKKGID KDVLLKMSSE VHEFEGLGKG KVILLPSDSQ THLLGVEAYL
SRYGKEITVL FLRTRVLNGD SDKQAEVMRL REYLEINYKV LSREFTPASD PEFISMLKRC
DLCHCPEVAD VCSLFGIPVV RNNPYDFFDI ADEINENLMQ RGEGSKEGSS EVIGKMEWKK
RFMTSLLSIS GMEYDVDLEP KEPRIRSSLS MDQTGHKKVD AKKKPGIRKK NREKEEAVEI
ILNNKEDANA ARIVNDFKKS KARTLVMDYD GTLTNIVARP PMAAPTQEIK DLLIRLGKIC
RVVISTGRSV EDCDKFFPKE IEVFAEHGAC HRIDGKWKEG GTFPQKDLAW RIGQFFLART
PGSELERKKT GYAFHFRNVS PLIGVKQARA LFELLMRVCK DYVKKGNHVI EVRSSKKSCA
MEKIEEGFVL CAGDDVADED MFDVCKGYTI KVGDQSTSAA YRVKDPENFR MLLGRLLE