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Database: UniProt
Entry: A0A0R2H5X8_9LACO
LinkDB: A0A0R2H5X8_9LACO
Original site: A0A0R2H5X8_9LACO 
ID   A0A0R2H5X8_9LACO        Unreviewed;       797 AA.
AC   A0A0R2H5X8;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   SubName: Full=Phosphoketolase {ECO:0000313|EMBL:KRN44996.1};
GN   ORFNames=IV41_GL001864 {ECO:0000313|EMBL:KRN44996.1};
OS   Limosilactobacillus ingluviei.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Limosilactobacillus.
OX   NCBI_TaxID=148604 {ECO:0000313|EMBL:KRN44996.1, ECO:0000313|Proteomes:UP000051639};
RN   [1] {ECO:0000313|EMBL:KRN44996.1, ECO:0000313|Proteomes:UP000051639}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 14792 {ECO:0000313|EMBL:KRN44996.1,
RC   ECO:0000313|Proteomes:UP000051639};
RX   PubMed=26415554; DOI=10.1038/ncomms9322;
RA   Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X.,
RA   Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E.,
RA   Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., Ritari J.,
RA   Douillard F.P., Paul Ross R., Yang R., Briner A.E., Felis G.E.,
RA   de Vos W.M., Barrangou R., Klaenhammer T.R., Caufield P.W., Cui Y.,
RA   Zhang H., O'Toole P.W.;
RT   "Expanding the biotechnology potential of lactobacilli through comparative
RT   genomics of 213 strains and associated genera.";
RL   Nat. Commun. 6:8322-8322(2015).
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}.
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:KRN44996.1}.
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DR   EMBL; JQBA01000007; KRN44996.1; -; Genomic_DNA.
DR   RefSeq; WP_019206611.1; NZ_JQBA01000007.1.
DR   AlphaFoldDB; A0A0R2H5X8; -.
DR   STRING; 1203076.GCA_000312405_01573; -.
DR   GeneID; 82934340; -.
DR   PATRIC; fig|148604.4.peg.1922; -.
DR   eggNOG; COG3957; Bacteria.
DR   OrthoDB; 9768449at2; -.
DR   Proteomes; UP000051639; Unassembled WGS sequence.
DR   GO; GO:0016832; F:aldehyde-lyase activity; IEA:InterPro.
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   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   SUPFAM; SSF52922; TK C-terminal domain-like; 1.
DR   PROSITE; PS60002; PHOSPHOKETOLASE_1; 1.
PE   3: Inferred from homology;
KW   Lyase {ECO:0000256|ARBA:ARBA00023239};
KW   Reference proteome {ECO:0000313|Proteomes:UP000051639}.
FT   DOMAIN          7..377
FT                   /note="Xylulose 5-phosphate/Fructose 6-phosphate
FT                   phosphoketolase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF09364"
FT   DOMAIN          593..793
FT                   /note="Xylulose 5-phosphate/Fructose 6-phosphate
FT                   phosphoketolase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF09363"
SQ   SEQUENCE   797 AA;  90220 MW;  437AE43BE4230BF5 CRC64;
     MAVDYDSKAY LENVDAYWRA ANYLSVGTLF LMNNPLLRRD LKAEDVKPKP IGHWGTIVPQ
     NFIYAHLNRV IKKYGVKMFY IEGSGHGGQV MVNNSYLDGS YTEIYPEITQ DEAGMAKLFK
     HFSFPGGTAS HAAPETPGSL HEGGELGYAL SHGVGAILDN PDQIAAVEIG DGEFETGPLA
     ASWFSNRFIN PVTDGAVLPI LQVNGFKISN PTMIARMSDE EVTKYFEGLG WKPYFVSAYK
     GGDFDALKDH MEVHAEMAKV MDEAIEEIQA IQKKAREDND GSMAQWPVII FRVPKGWTGP
     TKDLDGNPIE NSFRAHQIPI PVAQDAMEHK DMLVDWMKSY KPEELFDETG YPVDAVRANV
     PAAELRMAIN PETNGGANQK ALRMPNYRDF AVEVRDGNMH QDMIEWGKYI AKMMELNPNN
     FRGFGPDESK SNRLYAALDG SKRTWTADVH EPNDEDLAVN GRIIDSQLSE HQAEGFLEGY
     TLTGRHGYFA TYESFGRVVD SMLTQHMKWM RKAKEQYWRN DYPALTFVDT STVFQQDHNG
     YTHQDPGLLT HLYEKERPDM IGEYLPADTN TLLAVSDKIF REKEKINVLV TSKHPRQQWF
     SIDEATELVA NGLGYVDWAS TDQGEEPDVV FAASGTEPTE EVFAAVELLH DAFPELKIRV
     INVVDVMKLM TLDKNPEGMS DADFDRYFTA DKPVVFAWHG FRDMVQSLFF PRHNRNVHIH
     SYIENGDITT PFDMRVLNEL DRYHLAKDAI LSVAGYEQKG AAFAQKMDDM VAKHNHYIRT
     YGDDMPEVKD WTWKGLK
//
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