ID A0A0A2VWF4_BEABA Unreviewed; 818 AA.
AC A0A0A2VWF4;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE SubName: Full=Putative phosphoketolase {ECO:0000313|EMBL:KGQ05099.1};
GN ORFNames=BBAD15_g9637 {ECO:0000313|EMBL:KGQ05099.1};
OS Beauveria bassiana D1-5.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Cordycipitaceae; Beauveria.
OX NCBI_TaxID=1245745 {ECO:0000313|EMBL:KGQ05099.1, ECO:0000313|Proteomes:UP000030106};
RN [1] {ECO:0000313|EMBL:KGQ05099.1, ECO:0000313|Proteomes:UP000030106}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=D1-5 {ECO:0000313|EMBL:KGQ05099.1,
RC ECO:0000313|Proteomes:UP000030106};
RA Li Q., Wang L., Zhang Z., Wang Q., Ren J., Wang M., Xu W., Wang J., Lu Y.,
RA Du Q., Sun Z.;
RT "Genome sequencing and analysis of entomopathogenic fungi Beauveria
RT bassiana D1-5.";
RL Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases.
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:KGQ05099.1}.
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DR EMBL; ANFO01000973; KGQ05099.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0A2VWF4; -.
DR STRING; 1245745.A0A0A2VWF4; -.
DR eggNOG; ENOG502QUUF; Eukaryota.
DR HOGENOM; CLU_013954_2_0_1; -.
DR Proteomes; UP000030106; 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:UP000030106};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT DOMAIN 35..399
FT /note="Xylulose 5-phosphate/Fructose 6-phosphate
FT phosphoketolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF09364"
FT DOMAIN 604..811
FT /note="Xylulose 5-phosphate/Fructose 6-phosphate
FT phosphoketolase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF09363"
SQ SEQUENCE 818 AA; 90907 MW; 11F82A64CFD4CF89 CRC64;
MPGEVISEAN PPPMPSHLPS SVMSFAAKVP PRDLDKSTLE GLRNFQKAAC YIAGAMTFLR
DNVLLERDLE TNDIKPRLLG HWGTCPGLIL IWSHVNHLVQ RHGIDTIIVV GPGHGAPAVL
ASLWIEGSLA KFYPDKYDVD KRGLHNLITR FSVPGGFPRL TESSHINAET PGAIHEGGEL
GYALAVSFGA VMDRPDLLVT CIVGDGEAET GPTAAAWHAI KYIDPAESGA VLPILHVNGF
KISERTIFGC MDNKELVSLF SGYGYHVCIV ETLDKIDQEL FSAMEWAVGE IREIQKQARS
GSPISKPRWP MIALRTPKGW SGPKKVDGEF IEGSFRSHQV PVPDAKKNPD HLRIVQDWLG
SYGINTLLKD GKPSESVLST LPVDASKRLG QNKLAYDSYR LLKMPAWQEF GITKDRAASS
MKITGGLLKQ IAIDNPKTFR MFSPDELESN KLNAILDASG RNFQWDQYSR AQGGRVIEIL
SEHCCQGFMQ GYTLTGRTAL FPSYESFLGI IHTMMAQYSK FNKVARDVRW RGDLASINYI
ETSTWARQEH NGFSHQQPSF IGAVLSLKAE AARVYLPPDA NCFLSTVDHC LQSKNKVNLM
IGSKQPTAVY LTPDEAAQHC QKGASIWEFA SSDGEPDVIL VGVGVEVTFE VIKAAELLLQ
MAPDLLRVRV VNVTDLFVLA PEARHPHALT HDDFAALFTR DKPVYFNYHG YAQELQGLLF
GHCNTHRMTV RGYNEEGTTT TPFDMMLVNN LSRFDIAQWA LERAAESGPT CNAQKQKQKQ
TRELIKQVVL QKDAVKSYII DNGTDPDDTY QREQFRRK
//