ID   A0A0J8RMJ5_COCIT        Unreviewed;       806 AA.
AC   A0A0J8RMJ5;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   SubName: Full=Phosphoketolase {ECO:0000313|EMBL:KMU85184.1};
GN   ORFNames=CIHG_02966 {ECO:0000313|EMBL:KMU85184.1};
OS   Coccidioides immitis H538.4.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Onygenaceae; Coccidioides.
OX   NCBI_TaxID=396776 {ECO:0000313|EMBL:KMU85184.1, ECO:0000313|Proteomes:UP000054563};
RN   [1] {ECO:0000313|Proteomes:UP000054563}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=H538.4 {ECO:0000313|Proteomes:UP000054563};
RX   PubMed=20516208; DOI=10.1101/gr.103911.109;
RA   Neafsey D.E., Barker B.M., Sharpton T.J., Stajich J.E., Park D.J.,
RA   Whiston E., Hung C.-Y., McMahan C., White J., Sykes S., Heiman D.,
RA   Young S., Zeng Q., Abouelleil A., Aftuck L., Bessette D., Brown A.,
RA   FitzGerald M., Lui A., Macdonald J.P., Priest M., Orbach M.J.,
RA   Galgiani J.N., Kirkland T.N., Cole G.T., Birren B.W., Henn M.R.,
RA   Taylor J.W., Rounsley S.D.;
RT   "Population genomic sequencing of Coccidioides fungi reveals recent
RT   hybridization and transposon control.";
RL   Genome Res. 20:938-946(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}.
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DR   EMBL; DS016987; KMU85184.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0J8RMJ5; -.
DR   STRING; 396776.A0A0J8RMJ5; -.
DR   VEuPathDB; FungiDB:CIHG_02966; -.
DR   eggNOG; ENOG502QUUF; Eukaryota.
DR   Proteomes; UP000054563; 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:UP000054563};
KW   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT   DOMAIN          35..394
FT                   /note="Xylulose 5-phosphate/Fructose 6-phosphate
FT                   phosphoketolase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF09364"
FT   DOMAIN          599..803
FT                   /note="Xylulose 5-phosphate/Fructose 6-phosphate
FT                   phosphoketolase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF09363"
SQ   SEQUENCE   806 AA;  90366 MW;  EA23C93C53D54C10 CRC64;
     MPGEVIDKPD PKAPPSHLPS SLDELIVRLQ VSPLSKDALD SLVKFRRTAD YIAAAMIFLR
     DNAYLKRKLT FDDVKPRLLG HWGTCPGLNF IYSHLNYLIC EHNLDILAVI GPGHGAPALL
     ACLWMEGSLE KFYPDYSRDT SGLTKLITTF STTGGFPSHI NAETPGAIHE GGELGYALAV
     SFGAVMDKPD MIVACIVGDG EAESGPCTAS WHSYKYIDPA ESGAVIPILH LNGFKISERT
     IYGCMDDREL LALFSGFGYQ AVIVGNLDNI DAEFSTALNW TLSEIRIIQN AARSGKPIMK
     PRWPMIILRT PKGWTGPKKI HGKIVEGSFH AHQVPLPAAK KDGEELNALQ EWLLSYKPNE
     LFQENGDVTD EINFILPKEH SQRMGQRPEA YKSLQKIAIP DWKQFAVDTG SHESSMKTIG
     RLIDQLFLDN PHSARLFSPD ELESNKLDQA LAHTIRNFQW DQFSNARGGR VIEVLSEHMC
     QGFLQGYTLT GRLGIFPSYE SFLGIIHTMM VQYAKFNKMA RETTWHRDLY SLNYIETSTW
     TRQEHNGFSH QNPSFIGAVL NLKPDYARVY LPPDANTFLS TLAHCLKSKN YVNLMIGSKQ
     PTPVYLSAEE AESHCRAGGS VWKFASTDDG LDPDVVIVGI GTELTFEVIQ AAAMLRKRVP
     ELRVRMVNVT DLMILGVENR HPHSLSEEAF EALFTPNVPV HFNYHGYETE LKGLLFGRPK
     LHRVSIASYK EEGSTTTPFN MMLVNGVSRF HVAKAAVKGG SLRNERVKLK YQELLTEFDH
     EINSLSQYIL ENQKDPDDMY DMPKFE
//