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Database: UniProt
Entry: S9W2V5_SCHCR
LinkDB: S9W2V5_SCHCR
Original site: S9W2V5_SCHCR 
ID   S9W2V5_SCHCR            Unreviewed;       823 AA.
AC   S9W2V5;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   24-JAN-2024, entry version 31.
DE   SubName: Full=Phosphoketolase {ECO:0000313|EMBL:EPY52884.1};
GN   ORFNames=SPOG_02203 {ECO:0000313|EMBL:EPY52884.1};
OS   Schizosaccharomyces cryophilus (strain OY26 / ATCC MYA-4695 / CBS 11777 /
OS   NBRC 106824 / NRRL Y48691) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC   Schizosaccharomyces.
OX   NCBI_TaxID=653667 {ECO:0000313|EMBL:EPY52884.1, ECO:0000313|Proteomes:UP000015464};
RN   [1] {ECO:0000313|EMBL:EPY52884.1, ECO:0000313|Proteomes:UP000015464}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OY26 / ATCC MYA-4695 / CBS 11777 / NBRC 106824 / NRRL Y48691
RC   {ECO:0000313|Proteomes:UP000015464};
RX   PubMed=21511999; DOI=10.1126/science.1203357;
RA   Rhind N., Chen Z., Yassour M., Thompson D.A., Haas B.J., Habib N.,
RA   Wapinski I., Roy S., Lin M.F., Heiman D.I., Young S.K., Furuya K., Guo Y.,
RA   Pidoux A., Chen H.M., Robbertse B., Goldberg J.M., Aoki K., Bayne E.H.,
RA   Berlin A.M., Desjardins C.A., Dobbs E., Dukaj L., Fan L., FitzGerald M.G.,
RA   French C., Gujja S., Hansen K., Keifenheim D., Levin J.Z., Mosher R.A.,
RA   Mueller C.A., Pfiffner J., Priest M., Russ C., Smialowska A., Swoboda P.,
RA   Sykes S.M., Vaughn M., Vengrova S., Yoder R., Zeng Q., Allshire R.,
RA   Baulcombe D., Birren B.W., Brown W., Ekwall K., Kellis M., Leatherwood J.,
RA   Levin H., Margalit H., Martienssen R., Nieduszynski C.A., Spatafora J.W.,
RA   Friedman N., Dalgaard J.Z., Baumann P., Niki H., Regev A., Nusbaum C.;
RT   "Comparative functional genomics of the fission yeasts.";
RL   Science 332:930-936(2011).
CC   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC         Evidence={ECO:0000256|ARBA:ARBA00001964};
CC   -!- SIMILARITY: Belongs to the XFP family. {ECO:0000256|ARBA:ARBA00005623}.
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DR   EMBL; KE546989; EPY52884.1; -; Genomic_DNA.
DR   RefSeq; XP_013022762.1; XM_013167308.1.
DR   AlphaFoldDB; S9W2V5; -.
DR   STRING; 653667.S9W2V5; -.
DR   EnsemblFungi; EPY52884; EPY52884; SPOG_02203.
DR   GeneID; 25036527; -.
DR   eggNOG; ENOG502QUUF; Eukaryota.
DR   HOGENOM; CLU_013954_2_0_1; -.
DR   OMA; GCMDDRE; -.
DR   OrthoDB; 5485390at2759; -.
DR   Proteomes; UP000015464; Unassembled WGS sequence.
DR   GO; GO:0016832; F:aldehyde-lyase activity; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   Gene3D; 3.40.50.920; -; 1.
DR   Gene3D; 3.40.50.970; -; 2.
DR   InterPro; IPR029061; THDP-binding.
DR   InterPro; IPR009014; Transketo_C/PFOR_II.
DR   InterPro; IPR005593; Xul5P/Fru6P_PKetolase.
DR   InterPro; IPR018969; Xul5P/Fru6P_PKetolase_C.
DR   InterPro; IPR019790; Xul5P/Fru6P_PKetolase_CS.
DR   InterPro; IPR018970; Xul5P/Fru6P_PKetolase_N.
DR   InterPro; IPR019789; Xul5P/Fru6P_PKetolase_ThDP_BS.
DR   PANTHER; PTHR31273; PHOSPHOKETOLASE-RELATED; 1.
DR   PANTHER; PTHR31273:SF1; PHOSPHOKETOLASE-RELATED; 1.
DR   Pfam; PF03894; XFP; 1.
DR   Pfam; PF09363; XFP_C; 1.
DR   Pfam; PF09364; XFP_N; 1.
DR   PIRSF; PIRSF017245; Phosphoketolase; 1.
DR   SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 2.
DR   SUPFAM; SSF52922; TK C-terminal domain-like; 1.
DR   PROSITE; PS60002; PHOSPHOKETOLASE_1; 1.
DR   PROSITE; PS60003; PHOSPHOKETOLASE_2; 1.
PE   3: Inferred from homology;
KW   Lyase {ECO:0000256|ARBA:ARBA00023239};
KW   Reference proteome {ECO:0000313|Proteomes:UP000015464};
KW   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT   DOMAIN          50..409
FT                   /note="Xylulose 5-phosphate/Fructose 6-phosphate
FT                   phosphoketolase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF09364"
FT   DOMAIN          614..814
FT                   /note="Xylulose 5-phosphate/Fructose 6-phosphate
FT                   phosphoketolase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF09363"
SQ   SEQUENCE   823 AA;  92370 MW;  73966C127C321067 CRC64;
     MSADDIPNAS PEALSKQVEI AEKQPFPPSM PSRLPHELSC LYVPLDTSNI SDDEVAAVDR
     YQRACDYLAC SLIFLSKDIY TGGDLTEDDV KTRLLGHWGT CPGLSIAYSH CNRVINKYDL
     DMIFVVGPGH GAPAILAALF LEDSLGPFYP QYQFNREGLK NLISTFSLPG GFPSHVNAEC
     PGSIHEGGEL GYALSVSYGA VQDHPDLIVT CVIGDGEAES GPMAGSWQTH KFLDPAESGA
     VIPILSLNGY KISERTIYGC MDDFELLALF SGFGYQVAIV NYTDQFNREM AAAMDWAVET
     IRDIQHHARV KRELIKPRWP MIILRSPKGK GCPKTLKGTF LEGTYHAHQV PLKAARTDPT
     QRKMLKDWLS SYRFDEFLDE EGLPTRGIRE YIPRVNKRMG QRHETYNAYT PLNVTDWKKF
     GVPKGEKTSA TQVVGRYMGE LVRANNTTLR IFSPDELESN KLDGVLQYTD RTMQTDPTLM
     TKGGRVTEVL SEHICQGLMQ GYTLTGRTAI FPSYEAFMTI VVSMLIQYSK FIKMGLELPW
     HGKFGSLNYV TSSTWARQEH NGYSHQSPRF ITTMLSFKPG ISRVYFPADA NCFLATMARC
     MRSENTINLM VSSKNPQPSY LSIEEAEAHC TAGASVWKFC STDNGVSPDV VLVGIGNEIM
     FEVVKAAEML TNDIPSLRVR VVNVTDLMVL SSLHPHGMTQ LEFDALFTKN CHVHFNYHGY
     VMDLKSLLFD RIEPSRVTMN GYQEEGTTTT PFTMMMVNNT SRYDVARQAL QHSLHNPVVA
     VNCHNLSSNY SHKMDEIKDY IFKYKDDPPE TYDVPDFKDK RTI
//
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