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Database: UniProt
Entry: R1IAQ3_9PSEU
LinkDB: R1IAQ3_9PSEU
Original site: R1IAQ3_9PSEU 
ID   R1IAQ3_9PSEU            Unreviewed;       781 AA.
AC   R1IAQ3;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   24-JAN-2024, entry version 35.
DE   RecName: Full=Probable phosphoketolase {ECO:0000256|HAMAP-Rule:MF_01403};
DE            EC=4.1.2.- {ECO:0000256|HAMAP-Rule:MF_01403};
GN   ORFNames=H480_05334 {ECO:0000313|EMBL:EOD69606.1};
OS   Amycolatopsis vancoresmycina DSM 44592.
OC   Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; Amycolatopsis.
OX   NCBI_TaxID=1292037 {ECO:0000313|EMBL:EOD69606.1, ECO:0000313|Proteomes:UP000014139};
RN   [1] {ECO:0000313|EMBL:EOD69606.1, ECO:0000313|Proteomes:UP000014139}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44592 {ECO:0000313|EMBL:EOD69606.1,
RC   ECO:0000313|Proteomes:UP000014139};
RA   Kumar S., Kaur N., Kaur C., Raghava G.P.S., Mayilraj S.;
RT   "Draft genome sequence of Amycolatopsis vancoresmycina strain DSM 44592T.";
RL   Submitted (FEB-2013) 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:EOD69606.1}.
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DR   EMBL; AOUO01000054; EOD69606.1; -; Genomic_DNA.
DR   RefSeq; WP_003061237.1; NZ_AOUO01000054.1.
DR   AlphaFoldDB; R1IAQ3; -.
DR   PATRIC; fig|1292037.4.peg.1043; -.
DR   eggNOG; COG3957; Bacteria.
DR   OrthoDB; 9768449at2; -.
DR   Proteomes; UP000014139; 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          15..361
FT                   /note="Xylulose 5-phosphate/Fructose 6-phosphate
FT                   phosphoketolase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF09364"
FT   DOMAIN          578..779
FT                   /note="Xylulose 5-phosphate/Fructose 6-phosphate
FT                   phosphoketolase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF09363"
SQ   SEQUENCE   781 AA;  86366 MW;  9B5A940BCFA9F88B CRC64;
     MTALDARPAV LGRPELAQVD ALWRAANYLS AGQIYLMANP LLREQLRPEH VKPRLLGHWG
     TSPGLNFVYA HLNRAILAHD LNAMLVTGPG HGGPALLANT WLEGSYTEAW PEVTRDAAGM
     AELFRQFSFP GGVPSHVAPQ VPGSIHEGGE LGYSLAHAFG AAFDNPGLLV ACVVGDGEAE
     TGPLATSWHA NKFLDPARDG AVLPILHLNG YKIANPTVLS RIPPAELDAL LRGYGYSPIY
     VEGSDPQSMH QAMAAALDSA IATLAERRGV WPMIVLRSPK GWTGPSVVDG KPVEGTWRAH
     QVPLAEVRTN PDHLKQLEDW LRSYRPAELF DESGRPVADV TAMIPAGDRR MGANPHANGG
     ILLRPLTLPD TSAHAVAVSA PGVTVAEPTR VLGRFLRDVF ALNADRANFR LFGPDETASN
     RLDAVYDVTA KEWQAAIEPV DEHLARDGRV LEVLSEHLCQ GWLEGYLLSG RHGLFSCYEA
     FVHIVDSMVN QHIKWLRVHR QIPWRRPVAS LNYLLTSHVW RQDHNGFSHQ DPGFVDHVAN
     KSAEVVRVYF PPDTNTLLEV AAHCLRSRDY VNVVVAGKND TPNWLDAEQA ALHCARGVSI
     WEWASTHTDR EPDVVLACAG DAPTLEVMAA AKILRQELPS LAVRVVNVVD LMRLQPESEH
     PHGLSDRGYD ALFTPDRPVI FAYHGYPWLI HRLAYRRTGH HELHVRGYTE HGTTTTPFDM
     LVLNHLDRFQ LVIDVLDRIP GLAATAGVLR QRMTEAQGRH RRYIRTHGED LPEVRNWTWE
     G
//
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