ID   G0S2H5_CHATD            Unreviewed;       829 AA.
AC   G0S2H5;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   03-MAY-2023, entry version 39.
DE   SubName: Full=Phosphoketolase-like protein {ECO:0000313|EMBL:EGS22208.1};
GN   ORFNames=CTHT_0017250 {ECO:0000313|EMBL:EGS22208.1};
OS   Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719)
OS   (Thermochaetoides thermophila).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Chaetomiaceae; Thermochaetoides.
OX   NCBI_TaxID=759272 {ECO:0000313|Proteomes:UP000008066};
RN   [1] {ECO:0000313|EMBL:EGS22208.1, ECO:0000313|Proteomes:UP000008066}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 1495 / CBS 144.50 / IMI 039719
RC   {ECO:0000313|Proteomes:UP000008066};
RX   PubMed=21784248; DOI=10.1016/j.cell.2011.06.039;
RA   Amlacher S., Sarges P., Flemming D., van Noort V., Kunze R., Devos D.P.,
RA   Arumugam M., Bork P., Hurt E.;
RT   "Insight into structure and assembly of the nuclear pore complex by
RT   utilizing the genome of a eukaryotic thermophile.";
RL   Cell 146:277-289(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; GL988040; EGS22208.1; -; Genomic_DNA.
DR   RefSeq; XP_006692227.1; XM_006692164.1.
DR   AlphaFoldDB; G0S2H5; -.
DR   STRING; 759272.G0S2H5; -.
DR   GeneID; 18255763; -.
DR   KEGG; cthr:CTHT_0017250; -.
DR   eggNOG; ENOG502QUUF; Eukaryota.
DR   HOGENOM; CLU_013954_2_0_1; -.
DR   OMA; TMDHCLR; -.
DR   OrthoDB; 5485390at2759; -.
DR   Proteomes; UP000008066; 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:UP000008066};
KW   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT   DOMAIN          28..388
FT                   /note="Xylulose 5-phosphate/Fructose 6-phosphate
FT                   phosphoketolase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF09364"
FT   DOMAIN          606..808
FT                   /note="Xylulose 5-phosphate/Fructose 6-phosphate
FT                   phosphoketolase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF09363"
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..19
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   829 AA;  93529 MW;  8E8FCF8B9D7379E3 CRC64;
     MGDSIESSQV ESISPYGPAR STIQGEPLTD EELKKYNDWF KASLYLSLGM IYLRQNPLLK
     EPLSKEHLKA RLLGHFGSCP GQIFTYMHFN RLIKKYDLDA IFISGPGHGA PAVLSQAYLE
     GTYSEVYPEC SEDEEGLQKF FKQFSFPGGI GSHATPETPG SIHEGGELGY SLSHAFGAVF
     DNPNLIALTM VGDGEAETGP LATSWHSTKF LNPITDGAVL PVLHLNGYKI NNPTILARIS
     HKELESLFIG YGYQPYFVEG DDIETMHQAM AATLEHAVLE IRRFQQQARE SGKAFRPRWP
     VIILRTPKGW TGPRKVDDKY LEGYWRSHQV PITDVHENEE HLQLLEQWMR SYEPDRLFPD
     GKLLPELRDL APTGVRRMSA NPVANGGLLR KPLKMPDFRK YALKVDRPAG TNGFSMANMA
     RFLRDIMTMN QDNFRLFGPD ETESNKLASV YEAGKKVWLG EYFEEDENGG NLATEGRVME
     MLSEHTCEGW LEGYLLTGRH GLLNSYEPFI HVIDSMVNQH CKWLEKSLEV PWRAKISSLN
     ILLTAVVWRQ DHNGFTHQDP GFLDVVANKS PEVVRIYLPP DGNCLLSCMD HCLRSSNYVN
     VIVADKQEHL QFLSMDDAIV HCTKGIGIWP QFSTDQGGEP DVVMASCGDI STQESLAAVD
     LLLSHFPDLK IRFINVVDLF KLIPYTDHPH GLTDEEWVSL FTADKPIIFN FHSYPWLVYR
     LASKRPGANQ NLHVRGYREK GNIDTPLELA IRNGTDRFSL AIEAIDHVPR LKNRGAAARD
     ALKSAQIKAR NEAFENGVDP PLLKNWVWPH TGLWKRRSES PVEMTDVIG
//