ID   G1BWI9_9BACT            Unreviewed;       789 AA.
AC   G1BWI9;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   24-JAN-2024, entry version 26.
DE   SubName: Full=Putative phosphoketolase {ECO:0000313|EMBL:AEH40993.1};
OS   Candidatus Methylacidiphilum fumarolicum.
OC   Bacteria; Verrucomicrobiota; Methylacidiphilae; Methylacidiphilales;
OC   Methylacidiphilaceae; Methylacidiphilum (ex Ratnadevi et al. 2023).
OX   NCBI_TaxID=591154 {ECO:0000313|EMBL:AEH40993.1};
RN   [1] {ECO:0000313|EMBL:AEH40993.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=SolV {ECO:0000313|EMBL:AEH40993.1};
RX   PubMed=21725016; DOI=10.1128/JB.00407-11;
RA   Khadem A.F., Pol A., Wieczorek A., Mohammadi S.S., Francoijs K.J.,
RA   Stunnenberg H.G., Jetten M.S., Op den Camp H.J.;
RT   "Autotrophic methanotrophy in verrucomicrobia: Methylacidiphilum
RT   fumariolicum SolV uses the Calvin-Benson-Bassham cycle for carbon dioxide
RT   Fixation.";
RL   J. Bacteriol. 193:4438-4446(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; JF706257; AEH40993.1; -; Genomic_DNA.
DR   RefSeq; WP_009058931.1; NZ_OX458932.1.
DR   AlphaFoldDB; G1BWI9; -.
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   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.
PE   3: Inferred from homology;
KW   Lyase {ECO:0000256|ARBA:ARBA00023239}.
FT   DOMAIN          13..364
FT                   /note="Xylulose 5-phosphate/Fructose 6-phosphate
FT                   phosphoketolase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF09364"
FT   DOMAIN          579..783
FT                   /note="Xylulose 5-phosphate/Fructose 6-phosphate
FT                   phosphoketolase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF09363"
SQ   SEQUENCE   789 AA;  88712 MW;  05CA0F0B56FAC3A2 CRC64;
     MAPDIENIDL HIDYWNAANY LAAAQFYLKE NPLLLVPLRP EHLKPRIRGH WGSAPGLNLV
     YVQLNRLIQK TNAQFLFITG PGHCSSAILA NLYLEGTYSE FYPEISQDLD GLTLFCRQFS
     SPGGVPSHVS AMTPGSIHEG GELGYSLLHA FGAVFDHPEL IAAAVVSDGE AETGPLAASW
     QSINFLNPAR DGAVLPIFHV NDGKLSGPTI FGRMEDKDIA MFFSGMGYEP LFVCGNDPRQ
     VHTELGVALE KAYATIRQIQ QEAKEKGVHS KPRWPMIVLR TPDGWTGPKE VDGVKIEGTY
     RSHRSPLMDA RENPEHLKLL ESWLKSYHPE KLFDESGKLR KDLSNLAPKG SLRMGASPYA
     NGGSLLVDLV LPDYTEYQVG VKQPGNTVSE PTHVLGKYLR DVLRRNPTNF RIFCPDETDS
     NRLSAVFEVT NRCFVARTNP DDDHLSADGR IMEILSEHCC QGWLEGYLLS GRHGLLVSYE
     AFAMILDSMA SQHAKWLKLY REIPWRKPIA SLNYLLSSHV WRQEYDGYTH QGPGFIDTLI
     NKKGNVIRIY LPPDTNTLLS VMDHCLRSRN YVNLIIAEKQ PALNWLNMEE ARAHCARGAS
     IWTWASNDEG NPNIILGCAG DVPTLETVAA SWLLQKHFPE LKVKVVNVVD LMTLSPPAYH
     PHGMDEQRFI HLFSATQPVL FAFHGYPRMV HDLIHGRPNP ARFHVRGYQE EGTTTTSFDM
     VVLNKMSRYH LAIDAIKYAL KGVPHLRTKG ENLIVFFERK IAEHTTYVRA HLDDMPEIKN
     WTWSNPSAS
//