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Database: UniProt
Entry: A0A066XJ70_COLSU
LinkDB: A0A066XJ70_COLSU
Original site: A0A066XJ70_COLSU 
ID   A0A066XJ70_COLSU        Unreviewed;       818 AA.
AC   A0A066XJ70;
DT   03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT   03-SEP-2014, sequence version 1.
DT   24-JAN-2024, entry version 29.
DE   SubName: Full=Putative XFP domain-containing protein {ECO:0000313|EMBL:KDN65796.1};
GN   ORFNames=CSUB01_10326 {ECO:0000313|EMBL:KDN65796.1};
OS   Colletotrichum sublineola (Sorghum anthracnose fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC   Colletotrichum graminicola species complex.
OX   NCBI_TaxID=1173701 {ECO:0000313|EMBL:KDN65796.1, ECO:0000313|Proteomes:UP000027238};
RN   [1] {ECO:0000313|Proteomes:UP000027238}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TX430BB {ECO:0000313|Proteomes:UP000027238};
RX   PubMed=24926053; DOI=10.1128/genomeA.00540-14;
RA   Baroncelli R., Sanz-Martin J.M., Rech G.E., Sukno S.A., Thon M.R.;
RT   "Draft genome sequence of Colletotrichum sublineola, a destructive pathogen
RT   of cultivated sorghum.";
RL   Genome Announc. 2:E0054014-E0054014(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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KDN65796.1}.
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DR   EMBL; JMSE01000985; KDN65796.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A066XJ70; -.
DR   STRING; 1173701.A0A066XJ70; -.
DR   eggNOG; ENOG502QUUF; Eukaryota.
DR   HOGENOM; CLU_013954_2_0_1; -.
DR   OMA; TMDHCLR; -.
DR   OrthoDB; 5485390at2759; -.
DR   Proteomes; UP000027238; Unassembled WGS sequence.
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   Reference proteome {ECO:0000313|Proteomes:UP000027238};
KW   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT   DOMAIN          24..384
FT                   /note="Xylulose 5-phosphate/Fructose 6-phosphate
FT                   phosphoketolase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF09364"
FT   DOMAIN          602..803
FT                   /note="Xylulose 5-phosphate/Fructose 6-phosphate
FT                   phosphoketolase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF09363"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   818 AA;  92284 MW;  3C588BBD1E2CCC90 CRC64;
     MTDKEVESIS PYGPARSTVK GEPLSKEDIE KYNDFFKASL YLALGMIFLK ENPLLREPLK
     KEHMKLRLLG HFGSAPGQIF TWMHFNRLIK KYDLDSIFIS GPGHGAPAVL SQSYLEGVYS
     EVYPEKSEDI EGLQKFFKSF SFPGGIGSHA TPETPGSIHE GGELGYSVSH AFGAVYDHPD
     LIALTVVGDG EAETGPLATA WHSTKFLNPI IDGAVLPVLH LNGYKINNPT ILARISHKEL
     ENLFLGYGWQ PYFVEGDDVD TMHQAMAATL EHCVLEIRKF QKQARDSGKA FRPIWPMIVL
     RSPKGWTGPR KIDNNYMEGY WRAHQVPIPS ATTNPEHLKI LEEWMRSYEP ERLFKDGRIS
     DELKALCPIG NRRMSANPVA NGGVLRKPLK LPDFRNYAIK VDKSGGTNAA SMNNMATYLR
     DVIALNQNSF RLFGPDETES NKLGAVYEAG KKVWMGEYFE EDANGGNLAP EGRVMEMLSE
     HTCEGWLEGY ILTGRHGLLN SYEPFIHVID SMVNQHCKWI EKALEVEWRN KIASLNILLT
     AVVWRQDHNG FTHQDPGFLD VVANKSPEVV RIYLPPDGNC LLSTMNHCLA SSNYVNVIVA
     DKQDHLQYLT MDKAIEHCTK GIGIWPQFST DQGEEPDLVM ASCGDISTQE SLAAIDLLLQ
     HFPDLKIRCV NCVDLFKLIS HEDHSHGLTD AEWVALFTDD KPIIFNFHSY PWLVHRLAYK
     RPGNMNLHVR GYKEKGNIDT PLELAIRNQT DRFSLAMDAI DRMPQLHNRG AAARETLRNQ
     QIAARIEAFE TGMDPPFLKN WSWSHNGLWK QTVSKITN
//
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