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
//