ID E5R3R5_ARTGP Unreviewed; 817 AA.
AC E5R3R5;
DT 08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT 08-FEB-2011, sequence version 1.
DT 24-JAN-2024, entry version 40.
DE SubName: Full=Xylulose-5-phosphate/fructose-6-phosphate phosphoketolase {ECO:0000313|EMBL:EFQ97975.1};
GN ORFNames=MGYG_01011 {ECO:0000313|EMBL:EFQ97975.1};
OS Arthroderma gypseum (strain ATCC MYA-4604 / CBS 118893) (Microsporum
OS gypseum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Nannizzia.
OX NCBI_TaxID=535722 {ECO:0000313|Proteomes:UP000002669};
RN [1] {ECO:0000313|Proteomes:UP000002669}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4604 / CBS 118893 {ECO:0000313|Proteomes:UP000002669};
RX PubMed=22951933; DOI=10.1128/mbio.00259-12;
RA Martinez D.A., Oliver B.G., Graeser Y., Goldberg J.M., Li W.,
RA Martinez-Rossi N.M., Monod M., Shelest E., Barton R.C., Birch E.,
RA Brakhage A.A., Chen Z., Gurr S.J., Heiman D., Heitman J., Kosti I.,
RA Rossi A., Saif S., Samalova M., Saunders C.W., Shea T., Summerbell R.C.,
RA Xu J., Young S., Zeng Q., Birren B.W., Cuomo C.A., White T.C.;
RT "Comparative genome analysis of Trichophyton rubrum and related
RT dermatophytes reveals candidate genes involved in infection.";
RL MBio 3:E259-E259(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; DS989822; EFQ97975.1; -; Genomic_DNA.
DR RefSeq; XP_003176927.1; XM_003176879.1.
DR AlphaFoldDB; E5R3R5; -.
DR STRING; 535722.E5R3R5; -.
DR GeneID; 10032249; -.
DR VEuPathDB; FungiDB:MGYG_01011; -.
DR eggNOG; ENOG502QUUF; Eukaryota.
DR HOGENOM; CLU_013954_2_0_1; -.
DR InParanoid; E5R3R5; -.
DR OMA; GCMDDRE; -.
DR OrthoDB; 5485390at2759; -.
DR Proteomes; UP000002669; 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:UP000002669};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT DOMAIN 35..390
FT /note="Xylulose 5-phosphate/Fructose 6-phosphate
FT phosphoketolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF09364"
FT DOMAIN 599..794
FT /note="Xylulose 5-phosphate/Fructose 6-phosphate
FT phosphoketolase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF09363"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..18
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 817 AA; 90946 MW; 84F51CC36FD649E2 CRC64;
MPGQVLDGPN PRPPPSHLPD SVDELRVQLQ TVKLDDNVRR SLEKFRRATD YIAAAMIFLQ
SNAYLKRPVK PEDIKPRLLG HWGTCPGLNL VYSHLTYLIR SHDLDMLFVT GPGHGAPAIL
ASLWVEGSLG KFYPKYANDT NGLTKLITQF STTGGFPSHI NAETPGAIHE GGELGYALAV
SFGSVMDNPD LITAVVVGDG EAESGPCTAS WNGIKYIDPA ESGAVLPILH LNGFKISERT
IYGCMDDREL VSLFSGFGYQ TRIVEGLDDI DTNLNSSLEW ALAEIRRIQK AARSGSPIMK
PRWPMLILRT PKGWTGPKSI HGKIVEGSYA AHQVPLPEAG KDSEELQALQ EWLSSYKPEE
LFNEHGDVID DIKSILPGKD SKRMGQRKEV CDTFEKLKMP DWRRYTVPKG SQESSMKTIS
HFMGQILVDN PHSMRIFSPD ELESNKLGAV LEKTGRNFQC DQFSNAQGGR VIEVLSEHMC
QGFLQGYSLT GRTGIFPSYE SFLGIIHTMM VQYSKFNKMG METNWRRALP SINYIETSTW
ARQEHNGFSH QNPSFISAVL NLKPNAARVY LPPDANTFLS TLSHCLQSKN YINLMIGSKQ
PTQIYLSAEE AESHCRAGGS VWGFASTDDG LDPDVVLVGI GTEVTFEVIH AASILRKVVP
DLRVRVVNVT DLMILGSERS HPHSLSDETF DALFTADRPV HFNYHGYETE LKGLLFGRPR
VDRISIACYM EEGSTTTPFD MMLLNRVSRF HVAKAAVLGA SRRNEKVRIR QQELLAAFEH
EIRSARKYII ENHKGESSSP LFSLDLLSSR SIDETAC
//
