ID   F7WAS9_SORMK            Unreviewed;       814 AA.
AC   F7WAS9;
DT   21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT   21-SEP-2011, sequence version 1.
DT   24-JAN-2024, entry version 40.
DE   SubName: Full=WGS project CABT00000000 data, contig 2.65 {ECO:0000313|EMBL:CCC14244.1};
GN   ORFNames=SMAC_08757 {ECO:0000313|EMBL:CCC14244.1};
OS   Sordaria macrospora (strain ATCC MYA-333 / DSM 997 / K(L3346) / K-hell).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Sordariaceae; Sordaria.
OX   NCBI_TaxID=771870 {ECO:0000313|EMBL:CCC14244.1, ECO:0000313|Proteomes:UP000001881};
RN   [1] {ECO:0000313|EMBL:CCC14244.1, ECO:0000313|Proteomes:UP000001881}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-333 / DSM 997 / K(L3346) / K-hell
RC   {ECO:0000313|Proteomes:UP000001881};
RC   TISSUE=Mycelium {ECO:0000313|EMBL:CCC14244.1};
RX   PubMed=20386741; DOI=10.1371/journal.pgen.1000891;
RA   Nowrousian M., Stajich J., Chu M., Engh I., Espagne E., Halliday K.,
RA   Kamerewerd J., Kempken F., Knab B., Kuo H.C., Osiewacz H.D., Poeggeler S.,
RA   Read N., Seiler S., Smith K., Zickler D., Kueck U., Freitag M.;
RT   "De novo assembly of a 40 Mb eukaryotic genome from short sequence reads:
RT   Sordaria macrospora, a model organism for fungal morphogenesis.";
RL   PLoS Genet. 6:E1000891-E1000891(2010).
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:CCC14244.1}.
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DR   EMBL; CABT02000065; CCC14244.1; -; Genomic_DNA.
DR   RefSeq; XP_003344312.1; XM_003344264.1.
DR   AlphaFoldDB; F7WAS9; -.
DR   STRING; 771870.F7WAS9; -.
DR   GeneID; 10801595; -.
DR   KEGG; smp:SMAC_08757; -.
DR   VEuPathDB; FungiDB:SMAC_08757; -.
DR   eggNOG; ENOG502QUUF; Eukaryota.
DR   HOGENOM; CLU_013954_2_0_1; -.
DR   InParanoid; F7WAS9; -.
DR   OMA; GCMDDRE; -.
DR   OrthoDB; 5485390at2759; -.
DR   Proteomes; UP000001881; 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   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:UP000001881};
KW   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT   DOMAIN          40..393
FT                   /note="Xylulose 5-phosphate/Fructose 6-phosphate
FT                   phosphoketolase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF09364"
FT   DOMAIN          600..811
FT                   /note="Xylulose 5-phosphate/Fructose 6-phosphate
FT                   phosphoketolase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF09363"
SQ   SEQUENCE   814 AA;  91074 MW;  D1F7130424E0B20D CRC64;
     MGGTQIPIPN PPPLPSHLPD NVLDLAVQVE RKKLPDDVRE SLRAFQRAGC YIAASMIFLR
     DNVLLKHDLQ VSHIKPRLLG HWGTCPGLIL VWSHLNVLIR NHNLDMIYVI GPGHGAPAAL
     ASLWLEGSLE RFYPGEYDRN ATGLRNLITR FSVPGGFPSH INAETPGSIH EGGELGYALA
     VSFGAVMDNP DLIVTCVVGD GEAETGPTAT AWHAIKYIDP KESGAVIPIL HVNGFKISER
     TIFGCMDDKE IACLFSGYGY QVRIVEDLEN IDDDLQSSLE WAVSEIKKIQ KAAREDNKPI
     VKPRWPMIVL RTPKGWTGPE EVEGQIIEGS FHSHQVPLPK ASSDEKQLQA LDGWLSSYKI
     NELLDDEGKP TEAITRVLPE AEKRLGQLKT TYDPHIPLKA IDWKQFGVEK GIDESCMKTA
     GKFLDKLFQE NPKTLRLFSP DELESNKLNA ILDHTQRDFQ WDEYSRANGG RVIEVLSEHN
     CQGFMQGYTL TGRTALFPSY ESFLGIVHTM MVQYSKFVKI AREVPWRGDL ASINYIETST
     WARQEHNGFS HQNPSFIGAV LNLKAETARV YLPPDANCFL STVHHVMKSK NKTNLIIGSK
     QPTAVYLSAD EAAEHCRQGA SIWHFASTPD PNFAGQSVQD PDVVLVGIGV EVTFEVIKAA
     ELLRSIAPAL KVRVINVTDL MILIEESKHP HSLSKPKFIE MFTTDRPVLF NYHGYPTELQ
     GLLFGREKAE RMDVEGYQEE GSTTTPFDMM LRNRVSRFDV AKWALKRGAE KNGEMKKDLE
     GLLGEVDKRV KGVREFIGNE GKDPDDIYHM PKFE
//