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
//