ID B2HD47_MYCMM Unreviewed; 800 AA.
AC B2HD47;
DT 10-JUN-2008, integrated into UniProtKB/TrEMBL.
DT 10-JUN-2008, sequence version 1.
DT 27-MAR-2024, entry version 75.
DE RecName: Full=Probable phosphoketolase {ECO:0000256|HAMAP-Rule:MF_01403};
DE EC=4.1.2.- {ECO:0000256|HAMAP-Rule:MF_01403};
GN Name=xfp {ECO:0000313|EMBL:ACC41184.1};
GN OrderedLocusNames=MMAR_2742 {ECO:0000313|EMBL:ACC41184.1};
OS Mycobacterium marinum (strain ATCC BAA-535 / M).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium ulcerans group.
OX NCBI_TaxID=216594 {ECO:0000313|EMBL:ACC41184.1, ECO:0000313|Proteomes:UP000001190};
RN [1] {ECO:0000313|EMBL:ACC41184.1, ECO:0000313|Proteomes:UP000001190}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-535 / M {ECO:0000313|Proteomes:UP000001190};
RX PubMed=18403782; DOI=10.1101/gr.075069.107;
RA Stinear T.P., Seemann T., Harrison P.F., Jenkin G.A., Davies J.K.,
RA Johnson P.D., Abdellah Z., Arrowsmith C., Chillingworth T., Churcher C.,
RA Clarke K., Cronin A., Davis P., Goodhead I., Holroyd N., Jagels K.,
RA Lord A., Moule S., Mungall K., Norbertczak H., Quail M.A.,
RA Rabbinowitsch E., Walker D., White B., Whitehead S., Small P.L., Brosch R.,
RA Ramakrishnan L., Fischbach M.A., Parkhill J., Cole S.T.;
RT "Insights from the complete genome sequence of Mycobacterium marinum on the
RT evolution of Mycobacterium tuberculosis.";
RL Genome Res. 18:729-741(2008).
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000256|ARBA:ARBA00001964,
CC ECO:0000256|HAMAP-Rule:MF_01403};
CC -!- SIMILARITY: Belongs to the XFP family. {ECO:0000256|ARBA:ARBA00005623,
CC ECO:0000256|HAMAP-Rule:MF_01403}.
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DR EMBL; CP000854; ACC41184.1; -; Genomic_DNA.
DR RefSeq; WP_012394452.1; NC_010612.1.
DR AlphaFoldDB; B2HD47; -.
DR STRING; 216594.MMAR_2742; -.
DR KEGG; mmi:MMAR_2742; -.
DR eggNOG; COG3957; Bacteria.
DR HOGENOM; CLU_013954_2_0_11; -.
DR OrthoDB; 9768449at2; -.
DR Proteomes; UP000001190; Chromosome.
DR GO; GO:0016832; F:aldehyde-lyase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProt.
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 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, ECO:0000256|HAMAP-Rule:MF_01403};
KW Reference proteome {ECO:0000313|Proteomes:UP000001190};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052, ECO:0000256|HAMAP-
KW Rule:MF_01403}.
FT DOMAIN 14..375
FT /note="Xylulose 5-phosphate/Fructose 6-phosphate
FT phosphoketolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF09364"
FT DOMAIN 590..790
FT /note="Xylulose 5-phosphate/Fructose 6-phosphate
FT phosphoketolase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF09363"
FT REGION 776..800
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 800 AA; 89177 MW; AF1CFAFB6B7A2C4F CRC64;
MSPENRATSE PAPLSDDDLA LIDAYWRAAN YLSVGQIYLL SNPLLAEPLV PTHVKPRLLG
HWGTTPGLNL IYAHLNRIIR ERDANVIYVT GPGHGGPGLV ANAYLEGTYS EVYSAIAENT
DGMRRLFRQF SFPGGIPSHV AAQTPGSIHE GGELGYALVH AYGAAFDNPD LVVACVVGDG
EAETGPLATS WHSNKFLNPA IDGAVLPILH LNGYKIANPT VLARIPHDEL ESLLRGYGYR
PITVAGDDPP RVHQQLAGAL DEAFDEIAAI QLAARTGGDI KRPVWPMIVL RTPKGWTGPK
VVDGKKVEGT WRSHQVPLAD THDNAQHRDQ LEEWLRSYRP HELFDDHGKL RAQLRAMAPS
GNRRMSANPH ANGGLLLRDL DLPDFRDYAV QVNSPGTEIH EATRVLGTFL RDVIRRNPDR
FRLMGPDETA SNRLSAVFEA TGRTWLSETT ADDDHLSAEG RVMEVLSEHL CQGWLEGYLL
TGRHGMFDCY EAFVHIVDSM FNQHTKWLST SRELPWRRPI ASLNYLLSSH VWRQDHNGAS
HQDPGFIDLV ANKRPEVVRV YLPPDGNTLL SVADHCLRSR NYVNVIVAGK QPALAYLDMD
EAIAHCTRGL GIWQWASTAS GEPDVVLACA GDIPTLETLA AADILRRELP DLGVRVVNIV
DIMRLQPESE HPHGLPDREF DALFTRDKPV IFAYHGYPWL IHRLAYRRAN HARIHVRGFK
ERGTTTTPFD MVMLNDLDRF HLVIDVIDRV VGLSSRAAVL RQRMADARLA ARQYTREHGE
DDPRIADWAW EPSEQSELGE
//
