ID A0A0M8SEC7_9ACTN Unreviewed; 780 AA.
AC A0A0M8SEC7;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE RecName: Full=Probable phosphoketolase {ECO:0000256|HAMAP-Rule:MF_01403};
DE EC=4.1.2.- {ECO:0000256|HAMAP-Rule:MF_01403};
GN ORFNames=ADK54_42220 {ECO:0000313|EMBL:KOU33464.1};
OS Streptomyces sp. WM6378.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1415557 {ECO:0000313|EMBL:KOU33464.1, ECO:0000313|Proteomes:UP000037774};
RN [1] {ECO:0000313|Proteomes:UP000037774}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WM6378 {ECO:0000313|Proteomes:UP000037774};
RA Ju K.-S., Doroghazi J.R., Metcalf W.W.;
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KOU33464.1}.
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DR EMBL; LGDD01000358; KOU33464.1; -; Genomic_DNA.
DR RefSeq; WP_053731151.1; NZ_LGDD01000358.1.
DR AlphaFoldDB; A0A0M8SEC7; -.
DR PATRIC; fig|1415557.3.peg.9317; -.
DR OrthoDB; 9768449at2; -.
DR Proteomes; UP000037774; Unassembled WGS sequence.
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 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 Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052, ECO:0000256|HAMAP-
KW Rule:MF_01403}.
FT DOMAIN 7..359
FT /note="Xylulose 5-phosphate/Fructose 6-phosphate
FT phosphoketolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF09364"
FT DOMAIN 576..778
FT /note="Xylulose 5-phosphate/Fructose 6-phosphate
FT phosphoketolase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF09363"
SQ SEQUENCE 780 AA; 86095 MW; EC1C79ECF2D4445C CRC64;
MTKDRPVNLA ALDAHWRAAN YLAAGQIYLM SNPLLTEPLR PEHIKPRLLG HWGTSPGLNL
VHTHLNRVIK DRGLDAVCIW GPGHGGPAVL ANSWLDGSYA QTYPDVSRDA AGMARLFRQF
SFPGGVPSHV APETPGSIHE GGELGYSLAH AYGAAFDNPG LLVACVIGDG EAETGPLAAS
WHANKFLDPV HDGAVLPILH LNGYKIANPT VLSRIPEDEL DSLLTGYGYE PLHVTGSDPG
KVHLAMARAM DHALERIAEG RQRSGRPRWP MIVLRTPKGW TGPAEVDGVP VEGTWRSHQV
PLANVRENPD HLRQLEAWLR SYRPEELFDG EGRPTAQVLA CVPDGDLRLG ANPHANGGLL
TRALPVPPLE HFAVPVDKPG ATQHEPTRVL GGLLAQVMAD TAGRRDFRVV GPDETESNRL
GALFEVTGKA WQAETLDTDE NLSSDGRVME ILSEHVCQGW LEGYNLTGRH GLFSCYEAFV
HIVDSMVNQH IKWLKTSRHL PWRAPIPSLN YLLTSHVWRQ DHNGFSHQDP GFVDHVLNKS
PDVVRVYLPP DANTLLSVAD HVLCSRDYVN VIVAGKQPCF DWLSLDQARA HCARGAGIWE
WAGTEDGTRE PDVVLACAGD VPTLEVLAAA ALLRRHLPDL AVRVVNVVDL AKLLPREEHP
HGMGDLEYDA LFTRDKPVIF AYHGYPWLIH RLAYRRAGHA HLHVRGYKES GTTTTPFDMV
VRNDLDRYRL VMDVIDRVPG LAARAAAVRQ TMADTRTRHH AWIREHGTDL PEIADWTWTG
//