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Database: UniProt
Entry: H5X0S7_9PSEU
LinkDB: H5X0S7_9PSEU
Original site: H5X0S7_9PSEU 
ID   H5X0S7_9PSEU            Unreviewed;       790 AA.
AC   H5X0S7;
DT   18-APR-2012, integrated into UniProtKB/TrEMBL.
DT   18-APR-2012, sequence version 1.
DT   24-JAN-2024, entry version 36.
DE   SubName: Full=Phosphoketolase {ECO:0000313|EMBL:EHR50873.1};
GN   ORFNames=SacmaDRAFT_2631 {ECO:0000313|EMBL:EHR50873.1};
OS   Saccharomonospora marina XMU15.
OC   Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; Saccharomonospora.
OX   NCBI_TaxID=882083 {ECO:0000313|EMBL:EHR50873.1, ECO:0000313|Proteomes:UP000004926};
RN   [1] {ECO:0000313|EMBL:EHR50873.1, ECO:0000313|Proteomes:UP000004926}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=XMU15 {ECO:0000313|EMBL:EHR50873.1,
RC   ECO:0000313|Proteomes:UP000004926};
RX   PubMed=22768369; DOI=10.4056/sigs.2655905;
RA   Klenk H.P., Lu M., Lucas S., Lapidus A., Copeland A., Pitluck S.,
RA   Goodwin L.A., Han C., Tapia R., Brambilla E.M., Potter G., Land M.,
RA   Ivanova N., Rohde M., Goker M., Detter J.C., Li W.J., Kyrpides N.C.,
RA   Woyke T.;
RT   "Genome sequence of the ocean sediment bacterium Saccharomonospora marina
RT   type strain (XMU15(T)).";
RL   Stand. Genomic Sci. 6:265-275(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; CM001439; EHR50873.1; -; Genomic_DNA.
DR   RefSeq; WP_009154258.1; NZ_CM001439.1.
DR   AlphaFoldDB; H5X0S7; -.
DR   SMR; H5X0S7; -.
DR   STRING; 882083.SacmaDRAFT_2631; -.
DR   eggNOG; COG3957; Bacteria.
DR   HOGENOM; CLU_013954_2_0_11; -.
DR   OrthoDB; 9768449at2; -.
DR   Proteomes; UP000004926; Chromosome.
DR   GO; GO:0016832; F:aldehyde-lyase activity; IEA:InterPro.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProt.
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: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.
DR   PROSITE; PS60003; PHOSPHOKETOLASE_2; 1.
PE   3: Inferred from homology;
KW   Lyase {ECO:0000256|ARBA:ARBA00023239};
KW   Reference proteome {ECO:0000313|Proteomes:UP000004926};
KW   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT   DOMAIN          26..370
FT                   /note="Xylulose 5-phosphate/Fructose 6-phosphate
FT                   phosphoketolase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF09364"
FT   DOMAIN          587..788
FT                   /note="Xylulose 5-phosphate/Fructose 6-phosphate
FT                   phosphoketolase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF09363"
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   790 AA;  87744 MW;  8434733A2AB5FF3A CRC64;
     MTPRTPTTVD RPTRGDAAGS EGDRAAELAR VDAWWRAANY LSVGQVFLLE NPLLAEPLSP
     EHIKPRLLGH WGTVPGLTLT YAHLNRVIAK QRRRLLFVAG PGHGAAGLNA AAWLEGTYSE
     YYPDVGQDVE GMRRLFRQFS FPGGVPSHAS PHLPGSFHEG GELGYSLAHA TGAAFDNPDL
     VVACVIGDGE AETGPLAASW HAPAFLNPES DGTVLPILHL NEYKIANPTL LARLPQRQLA
     ELLRGHGWEP VEVSGDNAYA VHEAYATALD ECFELITRRR HPMIVLRTPK GWTGPDTLDG
     KPIEGNWRSH QVPLPAARHD PHQLAQLESW LRSYRPGELF DGSGAPAREI REANPSAELR
     MSAQPAAHGQ VQRALRLPEI AEHAVDVPAP GRRYAESTRA LGRYLRDVLA LNADQRNMLL
     FAPDEHASNR LDAVFDVTGR RWLLPTRSGD DHLDPRGRVV EVLSEHLCQG WLEGYLLTGR
     HGMFSSYEAF THIVDSMVAQ HAKWMHMAAE VPWRRPVPSL NYLLTSHVWR QDHNGASHQD
     PGFIDHILSK RPEVSRVYLP PDANCLLHVT EHCLRSNGLV NVIVAGKQPE LQYLDLDAAR
     AHTEQGLGIW EWASSDTESG TDVVIACAGD VPTQEALAAV QVLRGLVPDL RVRFVNVVDI
     TRLAAPQRHP HGISDREYSA IFTGEAPVIF AFHGYPWLIH ELTYNRPGHE HMHVRGFGDK
     GTTTTPFDMC VLNEIDRFHL ALAALERIPR MAGRLGHLRQ HLLGELARHH DHIRRTGEDM
     LEVRAWTWGS
//
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