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Database: UniProt
Entry: J9VR37_CRYNH
LinkDB: J9VR37_CRYNH
Original site: J9VR37_CRYNH 
ID   J9VR37_CRYNH            Unreviewed;       834 AA.
AC   J9VR37;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   24-JAN-2024, entry version 39.
DE   SubName: Full=Phosphoketolase {ECO:0000313|EMBL:AFR94180.1};
GN   ORFNames=CNAG_06923 {ECO:0000313|EMBL:AFR94180.1};
OS   Cryptococcus neoformans var. grubii serotype A (strain H99 / ATCC 208821 /
OS   CBS 10515 / FGSC 9487) (Filobasidiella neoformans var. grubii).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC   Tremellales; Cryptococcaceae; Cryptococcus;
OC   Cryptococcus neoformans species complex.
OX   NCBI_TaxID=235443 {ECO:0000313|EMBL:AFR94180.1, ECO:0000313|Proteomes:UP000010091};
RN   [1] {ECO:0000313|EMBL:AFR94180.1, ECO:0000313|Proteomes:UP000010091}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=H99 / ATCC 208821 / CBS 10515 / FGSC 9487
RC   {ECO:0000313|Proteomes:UP000010091};
RX   PubMed=24743168; DOI=10.1371/journal.pgen.1004261;
RA   Janbon G., Ormerod K.L., Paulet D., Byrnes E.J.III., Yadav V.,
RA   Chatterjee G., Mullapudi N., Hon C.C., Billmyre R.B., Brunel F., Bahn Y.S.,
RA   Chen W., Chen Y., Chow E.W., Coppee J.Y., Floyd-Averette A., Gaillardin C.,
RA   Gerik K.J., Goldberg J., Gonzalez-Hilarion S., Gujja S., Hamlin J.L.,
RA   Hsueh Y.P., Ianiri G., Jones S., Kodira C.D., Kozubowski L., Lam W.,
RA   Marra M., Mesner L.D., Mieczkowski P.A., Moyrand F., Nielsen K., Proux C.,
RA   Rossignol T., Schein J.E., Sun S., Wollschlaeger C., Wood I.A., Zeng Q.,
RA   Neuveglise C., Newlon C.S., Perfect J.R., Lodge J.K., Idnurm A.,
RA   Stajich J.E., Kronstad J.W., Sanyal K., Heitman J., Fraser J.A.,
RA   Cuomo C.A., Dietrich F.S.;
RT   "Analysis of the genome and transcriptome of Cryptococcus neoformans var.
RT   grubii reveals complex RNA expression and microevolution leading to
RT   virulence attenuation.";
RL   PLoS Genet. 10:E1004261-E1004261(2014).
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; CP003822; AFR94180.1; -; Genomic_DNA.
DR   RefSeq; XP_012048352.1; XM_012192962.1.
DR   AlphaFoldDB; J9VR37; -.
DR   SwissPalm; J9VR37; -.
DR   GeneID; 23890077; -.
DR   KEGG; cng:CNAG_06923; -.
DR   VEuPathDB; FungiDB:CNAG_06923; -.
DR   HOGENOM; CLU_013954_2_0_1; -.
DR   OrthoDB; 5485390at2759; -.
DR   Proteomes; UP000010091; Chromosome 3.
DR   GO; GO:0016832; F:aldehyde-lyase activity; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   CDD; cd02011; TPP_PK; 1.
DR   Gene3D; 3.40.50.920; -; 1.
DR   Gene3D; 3.40.50.970; -; 2.
DR   HAMAP; MF_01403; Phosphoketolase; 1.
DR   InterPro; IPR023962; Phosphoketolase.
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:SF0; 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   PROSITE; PS60002; PHOSPHOKETOLASE_1; 1.
DR   PROSITE; PS60003; PHOSPHOKETOLASE_2; 1.
PE   3: Inferred from homology;
KW   Lyase {ECO:0000256|ARBA:ARBA00023239};
KW   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT   DOMAIN          23..384
FT                   /note="Xylulose 5-phosphate/Fructose 6-phosphate
FT                   phosphoketolase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF09364"
FT   DOMAIN          602..804
FT                   /note="Xylulose 5-phosphate/Fructose 6-phosphate
FT                   phosphoketolase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF09363"
FT   REGION          815..834
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   834 AA;  93669 MW;  FA0B5E1A2E4933E4 CRC64;
     MADETSSLTS FGQARSTVKD QPLTTEELKQ MDAYMRASLY LCLGMLYLRH NPLLREPLKK
     EHLKARLLGH WGSDSGQIFT YIHMNRLIKK YDLDALFVSG PGHGAPAVLS QSYLEGVYTE
     VYPNITEDVE GMRRFFKQFS FPGGIGSHAT PETPGSLHEG GELGYSISHA FGTVFDNPNL
     ITLTMVGDGE SETGPLATSW HSTKFLNPIT DGAVLPVLHL NGYKINNPTV LARISHEEIE
     ALFVGYGWKP YFVEGSDLTS MHQAMAATLE KAVLEIKAYQ KQARDSGKAF RPRWPMVILR
     SPKGWTAPRD VSGHHLEGYW RAHQIPLADV ASNSEHLQLL ENWMRSYKPE ELFTEDGKLI
     PELKALPPTG QARMSANPVS NGGLVRKTLN LPDFKDYAIK DIAPGVTLAP SMSNMALFVR
     DVIKKNQTNF RLFGPDETES NKLAAVYEAG KKVWMGEYLP EDTDGGNLAQ AGRVMEILSE
     HTVEGWLEGY VLSGRHGLLN SYEPFIHIID SMVNQHCKWI EKCLEVEWRA KVSSLNILLT
     ATVWRQDHNG FTHQDPGFLD VVANKSPEVV RIYLPPDGNC LLSVMNHCFD SKNYVNVIVA
     DKQDHLQYLD MEAAVAHCTK GLGIWEWACV GDPNDNPDLI MACCGDVPTM ESLAATALLK
     EYLPELKIRF VNVVDLFKLI SHVDHPHGLT DRQWVSYFTG DTPIIFNFHS YPWLIHRLTY
     KRPGSHNIHV RGYKEKGNID TPLELAIRNE TDRYSLAMDA IDRLPHLQNK GSMAREKLYD
     AQIKARDWAF EHGIDPEDVR KWKWPYGPKT EGIASKLGFG GENKQQVASV GTSE
//
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