ID A7EL25_SCLS1 Unreviewed; 832 AA.
AC A7EL25;
DT 11-SEP-2007, integrated into UniProtKB/TrEMBL.
DT 11-SEP-2007, sequence version 1.
DT 13-SEP-2023, entry version 71.
DE RecName: Full=Phosphoketolase {ECO:0008006|Google:ProtNLM};
GN ORFNames=SS1G_06022 {ECO:0000313|EMBL:EDO03541.1};
OS Sclerotinia sclerotiorum (strain ATCC 18683 / 1980 / Ss-1) (White mold)
OS (Whetzelinia sclerotiorum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Sclerotiniaceae; Sclerotinia.
OX NCBI_TaxID=665079 {ECO:0000313|EMBL:EDO03541.1, ECO:0000313|Proteomes:UP000001312};
RN [1] {ECO:0000313|Proteomes:UP000001312}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 18683 / 1980 / Ss-1 {ECO:0000313|Proteomes:UP000001312};
RX PubMed=21876677; DOI=.1371/journal.pgen.1002230;
RA Amselem J., Cuomo C.A., van Kan J.A., Viaud M., Benito E.P., Couloux A.,
RA Coutinho P.M., de Vries R.P., Dyer P.S., Fillinger S., Fournier E.,
RA Gout L., Hahn M., Kohn L., Lapalu N., Plummer K.M., Pradier J.M.,
RA Quevillon E., Sharon A., Simon A., ten Have A., Tudzynski B., Tudzynski P.,
RA Wincker P., Andrew M., Anthouard V., Beever R.E., Beffa R., Benoit I.,
RA Bouzid O., Brault B., Chen Z., Choquer M., Collemare J., Cotton P.,
RA Danchin E.G., Da Silva C., Gautier A., Giraud C., Giraud T., Gonzalez C.,
RA Grossetete S., Guldener U., Henrissat B., Howlett B.J., Kodira C.,
RA Kretschmer M., Lappartient A., Leroch M., Levis C., Mauceli E.,
RA Neuveglise C., Oeser B., Pearson M., Poulain J., Poussereau N.,
RA Quesneville H., Rascle C., Schumacher J., Segurens B., Sexton A., Silva E.,
RA Sirven C., Soanes D.M., Talbot N.J., Templeton M., Yandava C., Yarden O.,
RA Zeng Q., Rollins J.A., Lebrun M.H., Dickman M.;
RT "Genomic analysis of the necrotrophic fungal pathogens Sclerotinia
RT sclerotiorum and Botrytis cinerea.";
RL PLoS Genet. 7:E1002230-E1002230(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; CH476627; EDO03541.1; -; Genomic_DNA.
DR RefSeq; XP_001593100.1; XM_001593050.1.
DR AlphaFoldDB; A7EL25; -.
DR STRING; 665079.A7EL25; -.
DR EnsemblFungi; EDO03541; EDO03541; SS1G_06022.
DR GeneID; 5489213; -.
DR KEGG; ssl:SS1G_06022; -.
DR eggNOG; ENOG502QUUF; Eukaryota.
DR HOGENOM; CLU_013954_2_0_1; -.
DR InParanoid; A7EL25; -.
DR OMA; TMDHCLR; -.
DR OrthoDB; 5485390at2759; -.
DR Proteomes; UP000001312; 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:UP000001312};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT DOMAIN 29..389
FT /note="Xylulose 5-phosphate/Fructose 6-phosphate
FT phosphoketolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF09364"
FT DOMAIN 607..808
FT /note="Xylulose 5-phosphate/Fructose 6-phosphate
FT phosphoketolase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF09363"
SQ SEQUENCE 832 AA; 93973 MW; 027A4B257FC23BBD CRC64;
MAPASGEVEV ESISAYGVAR TTVDEKPLSA EEVKKYDAYF SACMYLCLGM LYLRENALLK
EPLKKEHLKA RLLGHWGSDA GQAFTYLHMN RLIKKYDLNA LFVSGPGHGA PAVLSNAYLE
GTYSEVYPDK AEDEEGMRKF FKQFSFPGGI GSHATPETPG SIHEGGELGY SISHAFGTVF
DNPNLITLTM VGDGEAETGP LATAWHSTKF LNPITDGAVL PVLHLNGYKI NNPTILARIS
HKELESLFIG YGWKPYFVEG SDLESMHQAM AGTLERCVVE IRKYQKEARE SGKAIRPRWP
MIVLRSPKGW TGPRKVDDKL LEGFWRAHQI PLPNVASNPE HLKVLEAWMR SYKPEEVFDK
EGKLLPELKE LAPVGNARMS ANPVGNGGIL RKPLDMPDFR KYAFENIEAG VSLLPSMSNM
AKLLRDVVAK NMHTFRLFGP DETESNKLGE VYKAGKKVWM GENFEEDADG GNLATEGRVM
EMLSEHTVEG WLEGYILSGR HGLLNSYEPF IHVIDSMVNQ HCKWIEKCNE VEWRVKMASL
NILLTATVWR QDHNGFTHQD PGFLDVVANK SPEVVRIYLP PDGNCLLSCM DHCLRSTNYV
NVIVADKQDH LQFLNMEDAL THCEKGLGIW DWASNDQGFE PDVIMAACGD VPTHESLAAT
ALLRELIPDL KIRFVNVVDL FKLIHHGDHP HGITDKDWIS IFTSNKPIIF NFHSYPWLVH
RLTYKRPGQV NIHVRGYKEK GNIDTPLELA IRNQTDRYSL AMDAVDRVER LSNKGAHVRE
KLLNMQILAR RDAFENGIDP VHIREWRWPF QRGGKDEEML NMLRLTSYKE KG
//
