ID S7PZK2_GLOTA Unreviewed; 807 AA.
AC S7PZK2;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 03-MAY-2023, entry version 32.
DE SubName: Full=D-xylulose 5-phosphate/D-fructose 6-phosphate phosphoketolase {ECO:0000313|EMBL:EPQ52727.1};
GN ORFNames=GLOTRDRAFT_140365 {ECO:0000313|EMBL:EPQ52727.1};
OS Gloeophyllum trabeum (strain ATCC 11539 / FP-39264 / Madison 617) (Brown
OS rot fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Gloeophyllales; Gloeophyllaceae; Gloeophyllum.
OX NCBI_TaxID=670483 {ECO:0000313|EMBL:EPQ52727.1, ECO:0000313|Proteomes:UP000030669};
RN [1] {ECO:0000313|EMBL:EPQ52727.1, ECO:0000313|Proteomes:UP000030669}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 11539 {ECO:0000313|EMBL:EPQ52727.1,
RC ECO:0000313|Proteomes:UP000030669};
RX PubMed=22745431; DOI=10.1126/science.1221748;
RA Floudas D., Binder M., Riley R., Barry K., Blanchette R.A., Henrissat B.,
RA Martinez A.T., Otillar R., Spatafora J.W., Yadav J.S., Aerts A., Benoit I.,
RA Boyd A., Carlson A., Copeland A., Coutinho P.M., de Vries R.P.,
RA Ferreira P., Findley K., Foster B., Gaskell J., Glotzer D., Gorecki P.,
RA Heitman J., Hesse C., Hori C., Igarashi K., Jurgens J.A., Kallen N.,
RA Kersten P., Kohler A., Kuees U., Kumar T.K.A., Kuo A., LaButti K.,
RA Larrondo L.F., Lindquist E., Ling A., Lombard V., Lucas S., Lundell T.,
RA Martin R., McLaughlin D.J., Morgenstern I., Morin E., Murat C., Nagy L.G.,
RA Nolan M., Ohm R.A., Patyshakuliyeva A., Rokas A., Ruiz-Duenas F.J.,
RA Sabat G., Salamov A., Samejima M., Schmutz J., Slot J.C., St John F.,
RA Stenlid J., Sun H., Sun S., Syed K., Tsang A., Wiebenga A., Young D.,
RA Pisabarro A., Eastwood D.C., Martin F., Cullen D., Grigoriev I.V.,
RA Hibbett D.S.;
RT "The Paleozoic origin of enzymatic lignin decomposition reconstructed from
RT 31 fungal genomes.";
RL Science 336:1715-1719(2012).
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; KB469307; EPQ52727.1; -; Genomic_DNA.
DR RefSeq; XP_007868992.1; XM_007870801.1.
DR AlphaFoldDB; S7PZK2; -.
DR STRING; 670483.S7PZK2; -.
DR GeneID; 19304504; -.
DR KEGG; gtr:GLOTRDRAFT_140365; -.
DR eggNOG; ENOG502QUUF; Eukaryota.
DR HOGENOM; CLU_013954_2_0_1; -.
DR OMA; GCMDDRE; -.
DR OrthoDB; 5485390at2759; -.
DR Proteomes; UP000030669; 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:UP000030669};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT DOMAIN 35..392
FT /note="Xylulose 5-phosphate/Fructose 6-phosphate
FT phosphoketolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF09364"
FT DOMAIN 601..803
FT /note="Xylulose 5-phosphate/Fructose 6-phosphate
FT phosphoketolase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF09363"
SQ SEQUENCE 807 AA; 89193 MW; 2903646B55FE2E08 CRC64;
MPGQVLYEAN PPPDASHLPD ELLKLRVQLD VSNALSKEEV QAIQRFRRAA DYIAAAMIFL
KSNILLDKQL SHEDIKPRLL GHWGTCPGLV LVHAHLNRII KKTNLDAVYV IGPGHGAPGY
LSCLWLEDSL SKFYPEYSRD MQGLHRLITK FSLPGGFPSH INSETPGSIH EGGELGYALG
VAFGAVMDNP DLVAVCVVGD GEAETGPTAT AWHGYKYIDP AESGAVLPIV HVNGFKISER
TIYGTMDDKE LVALFSGYGY QVRFVEHLDN IDNDLAGSME WALGEIRKIQ QAARSGKPIV
KPRWPVLIMR TPKGWSAPKK VHGEFIEGSF HAHQVPLPKA GSDDEELAAL QAWLSSYGPK
ELFNPDGTVK PEVVEGVVPD NDDKKIGQRR EAMRMFCGLE VPAWREHGAD EGAMVSATGA
LGTFLEEVIR KNPSSFRIFS PDELESNKLS AVLKVTGRNF QWDVASRGKG GRVIEVLSEH
TCQAMLQGYT LTGRCGLFPS YEAFLGIVHT MMVQYSKFVK MAAQTKWHTH IGSLNYLETS
TWARQEHNGF SHQNPSMIGA MLNLKPTFSR VYLPPDANCM LSTMAHCLRA RGYINLVVGS
KQPTPVWLGR EEADRHCIAG ASVWKFASVE EGVDPDVVLV GIGVEMTFEV IAAASLLRQH
APQLRVRVVN VTDLMILGPE GSHPHALTDT DFYALFTTDR PVHFNYHGYP IELKGLLFGR
PGLSRVTIEG YREEGTTTSP FDMMLCNRTS RYHVAAAAIR GAALHNAKVA IDAHEKISYL
MHLSQKDRAY ILEHGTDPEG TYERPTF
//
