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Database: UniProt
Entry: A0A171DPU5_9ACTN
LinkDB: A0A171DPU5_9ACTN
Original site: A0A171DPU5_9ACTN 
ID   A0A171DPU5_9ACTN        Unreviewed;       782 AA.
AC   A0A171DPU5;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   RecName: Full=Probable phosphoketolase {ECO:0000256|HAMAP-Rule:MF_01403};
DE            EC=4.1.2.- {ECO:0000256|HAMAP-Rule:MF_01403};
GN   ORFNames=PS9374_06771 {ECO:0000313|EMBL:GAT71080.1};
OS   Planomonospora sphaerica.
OC   Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC   Streptosporangiaceae; Planomonospora.
OX   NCBI_TaxID=161355 {ECO:0000313|EMBL:GAT71080.1, ECO:0000313|Proteomes:UP000077701};
RN   [1] {ECO:0000313|EMBL:GAT71080.1, ECO:0000313|Proteomes:UP000077701}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 9374 {ECO:0000313|EMBL:GAT71080.1,
RC   ECO:0000313|Proteomes:UP000077701};
RA   Dohra H., Suzuki T., Inoue Y., Kodani S.;
RT   "Draft Genome Sequence of Planomonospora sphaerica JCM9374, a Rare
RT   Actinomycete.";
RL   Genome Announc. 4:e00779-16(2016).
RN   [2] {ECO:0000313|Proteomes:UP000077701}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 9374 {ECO:0000313|Proteomes:UP000077701};
RA   Suzuki T., Dohra H., Kodani S.;
RT   "Planomonospora sphaerica JCM9374 whole genome shotgun sequence.";
RL   Submitted (APR-2016) 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:GAT71080.1}.
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DR   EMBL; BDCX01000021; GAT71080.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A171DPU5; -.
DR   STRING; 161355.PS9374_06771; -.
DR   Proteomes; UP000077701; 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   Reference proteome {ECO:0000313|Proteomes:UP000077701};
KW   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052, ECO:0000256|HAMAP-
KW   Rule:MF_01403}.
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..780
FT                   /note="Xylulose 5-phosphate/Fructose 6-phosphate
FT                   phosphoketolase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF09363"
SQ   SEQUENCE   782 AA;  87362 MW;  36F0C99E4F381E75 CRC64;
     MIKGKAGTVI PMEKLQRIDA YWRAANYLSV GQIYLLDNPL LTEPLAVEHI KPRLLGHWGT
     TPGLNFCFAH LNRIIAERDQ DMIYIAGPGH GGPAAVAHAW LEGSYTEKYP DITQDAAGMR
     KLFRQFSFPG GVPSHVAPET PGSIHEGGEL GYALAHAYGA AFDNPELVVA CIVGDGEAET
     GPLAASWHSN KFLDPYRDGV VLPVLHLNGY KIANPTVLAR IPEEELLKLM EGYGYRPHIV
     SGDDPAAMHE LMQNTLNTVF DQIAEFKDGR ATRLPMIILR TPKGWTGPRE VDGLPVEGTW
     RSHQVPLSNV RGNDEYRRLL EEWMRSYRPE ELFDADGRPL PEILQTVPAG TRRMSASPHA
     NGGEILRPLA LPDFRDYAVD VKTPAAQQTE PTRVLGAFLR DIIAANPRTF RLMGPDETAS
     NRLGAVFETT GRTWNAEILP TDTDLAAGGR VMEVLSEHLC QGWLEGYLLT GRHGLFNCYE
     AFIHIIDAMF NQHAKWLDAC HDIPWRRPVA SLNYLLSSHV WRQDHNGFSH QDPGFLDVVV
     NKKADVVRVY LPPDANTLLS VGDHCLRSHD YVNVVVAGKQ PVLDLFTMDE AIAHCTRGLG
     IIEWASNDAG DDPDVILACA GDVPTLETLA AAALLHEHLP ELKVRVINVV DLMRLQPPSE
     HPHGMSDAQF DALFTPDKPV IFDFHGYPWL IHRLTYRRAG HHNIHVRGYK EEGTTTTPFD
     MAMLNDIDRY HLVMDVIDRV PGLGTRAAHL RQQMSDARLR ARAHTREHGE DLPEIRDWTW
     TR
//
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