ID A0A0A1GW71_9LACO Unreviewed; 791 AA.
AC A0A0A1GW71;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 24-JAN-2024, entry version 33.
DE RecName: Full=Probable phosphoketolase {ECO:0000256|HAMAP-Rule:MF_01403};
DE EC=4.1.2.- {ECO:0000256|HAMAP-Rule:MF_01403};
GN Name=xpk {ECO:0000313|EMBL:BAP86507.1};
GN ORFNames=LOOC260_120010 {ECO:0000313|EMBL:BAP86507.1};
OS Paucilactobacillus hokkaidonensis JCM 18461.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Paucilactobacillus.
OX NCBI_TaxID=1291742 {ECO:0000313|EMBL:BAP86507.1, ECO:0000313|Proteomes:UP000031620};
RN [1] {ECO:0000313|EMBL:BAP86507.1, ECO:0000313|Proteomes:UP000031620}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LOOC260 {ECO:0000313|EMBL:BAP86507.1,
RC ECO:0000313|Proteomes:UP000031620};
RA Tanizawa Y., Tohno M., Kaminuma E., Nakamura Y., Arita M.;
RT "Complete genome sequence and analysis of Lactobacillus hokkaidonensis
RT LOOC260T.";
RL Submitted (NOV-2014) 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}.
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DR EMBL; AP014680; BAP86507.1; -; Genomic_DNA.
DR RefSeq; WP_041094629.1; NZ_AP014680.1.
DR AlphaFoldDB; A0A0A1GW71; -.
DR STRING; 1291742.LOOC260_120010; -.
DR KEGG; lho:LOOC260_120010; -.
DR HOGENOM; CLU_013954_2_0_9; -.
DR Proteomes; UP000031620; Chromosome.
DR GO; GO:0016832; F:aldehyde-lyase activity; IEA:UniProtKB-UniRule.
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 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 PANTHER; PTHR31273; PHOSPHOKETOLASE-RELATED; 1.
DR PANTHER; PTHR31273:SF1; 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.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_01403};
KW Thiamine pyrophosphate {ECO:0000256|HAMAP-Rule:MF_01403}.
FT DOMAIN 7..370
FT /note="Xylulose 5-phosphate/Fructose 6-phosphate
FT phosphoketolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF09364"
FT DOMAIN 587..787
FT /note="Xylulose 5-phosphate/Fructose 6-phosphate
FT phosphoketolase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF09363"
FT COILED 247..274
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 791 AA; 89443 MW; 3E2B41D6AAC9DCC0 CRC64;
MAVDYDSKEY LESVDAYWRA ANYLSVGQLF LKDNPLLQSD LKASDVKVKP IGHWGTIVPQ
NFIYAHLNRA IKKYDLNMFY IEGSGHGGQV MVSNSYLDGS YSDIYPDVSQ DLEGMKHLFK
QFSFPGGVAS HAAPETPGSI HEGGELGYSL SHGVGAILDN PDVIAAVEIG DGEAETGPLA
ASWFSDKFIN PINDGAVLPI LQVNGFKISN PTIVSRMSDA DLTKYFEGMG WDPLFVNVYD
KPVSQAHEEM AKTVDEAVEK IKAIQKNARD NNDDSLPVWP MIVLRAPKGW TGPKENLDGE
PIENSFRAHQ IPIPVDQNHM EHKELLINWL KSYKPEELFN EDGTVKDEIK AIIPAGNSRM
AVNPITNGGI NPEPLKLPDY REFAVDNKVP GKEVKEDMAV WSQWLGAVIK KNPTTFRAFG
PDESMSNRLY GIFDVTNRQW MEEIKEPNDQ YVAHAGRLID SQLSEHQAEG WLEGYVLTGR
HGLFATYESF GRVVDSMLTQ HMKWLRKAKE QNWRHDYPSL NFINTSTVFQ QDHNGYTHQD
PGMLTHMAEK KADLVREYLP ADANTLLAVG NKAFTEREVI NIITTSKHPR QQWFSIDEAT
QLVNNGLGYV DWASTDQGLK PDIVFAAAGT EPTLESLAAI DILHDEFPEL KIRFINVVDI
LKLRTQKKDP RGLTDDEFDR YFTTDAPIIF AFHGFEDMIE SIFFDRHNHN INIHGYRENG
DITTPFDMRV LNQLDRFDLA KDAILSVPAY AEKSAYFAQR MDDMIAKHNH FIRTEGTDLP
EVMNWQWKGL K
//