ID A0A0D5ADS2_9NOCA Unreviewed; 796 AA.
AC A0A0D5ADS2;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE SubName: Full=Xylulose-5-phosphate phosphoketolase {ECO:0000313|EMBL:AJW40938.1};
GN ORFNames=NY08_2928 {ECO:0000313|EMBL:AJW40938.1};
OS Rhodococcus sp. B7740.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Rhodococcus.
OX NCBI_TaxID=1564114 {ECO:0000313|EMBL:AJW40938.1, ECO:0000313|Proteomes:UP000032410};
RN [1] {ECO:0000313|EMBL:AJW40938.1, ECO:0000313|Proteomes:UP000032410}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B7740 {ECO:0000313|EMBL:AJW40938.1};
RX PubMed=25931596;
RA Zhang D., Li L., Zhu S., Zhang N., Yang J., Ma X., Chen J.;
RT "Complete Genome Sequence of Rhodococcus sp. B7740, a Carotenoid-Producing
RT Bacterium Isolated from the Arctic Sea.";
RL Genome Announc. 3:0-0(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}.
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DR EMBL; CP010797; AJW40938.1; -; Genomic_DNA.
DR RefSeq; WP_045196938.1; NZ_CP010797.1.
DR AlphaFoldDB; A0A0D5ADS2; -.
DR STRING; 1564114.NY08_2928; -.
DR KEGG; rhb:NY08_2928; -.
DR PATRIC; fig|1564114.4.peg.2885; -.
DR HOGENOM; CLU_013954_2_0_11; -.
DR Proteomes; UP000032410; Chromosome.
DR GO; GO:0016832; F:aldehyde-lyase activity; IEA:InterPro.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProt.
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 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};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT DOMAIN 13..371
FT /note="Xylulose 5-phosphate/Fructose 6-phosphate
FT phosphoketolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF09364"
FT DOMAIN 591..795
FT /note="Xylulose 5-phosphate/Fructose 6-phosphate
FT phosphoketolase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF09363"
SQ SEQUENCE 796 AA; 87774 MW; FA8B6F3F0E19BFE0 CRC64;
MTTPTVDTTY DSEKLDADLR YWAAANYLTV AQIYLQDNVL LRRPLEAEHI KPRLLGHWGT
SPGLSMIYTL LNRVIRRTHS DWLYVTGPGH GGPAMVANTY LEGTYSEIYP DISLDSDGVR
RLCRQFSTPG GIPSHVSVQT PGSIHEGGEL GYALVHAAGA AFDNPDLIVA CVVGDGEAET
GPLSGSWKIP AFLNPVRDGA VLPILHLNDG KISGPTVLGR SADLAVERFL RSQGWTPIFV
EGTDPREVFP ALESALTRAH DAIGRVRHAA RGGNPRGDIA WPAIVLRTPK GWTGPHEVDG
KRIEGTHWAH QVPLSGVQEN PAHLELLEKW LLSYDPRSLF DDNGAPVASI RELVPSGTER
LGATPYANGG VLLQPLVIRD LENYALTVES PGRTSHETTT VLGEMMRDIY LDNAQPNGGG
NFRLFCPDET ASNRLQAVFE ATDRCWQLPT TEFDDDLGPD GRVMEVLSEH LCEGWLEAYL
LSGRHGLFAS YEAFAMVSVS MLIQHTKWLQ HAATLPWRAP VASLNVLLTS TCWRNDHNGF
SHQGPGLIDA VIPLAPDVVR VWLPPDSNTL LAVADHCFRS RGHVNVLVVD KQSHPQYLTL
PEARAHAAAG ASRWDWAGTE VADADEDPAI VLACAGDVPT EETLAAADLL RTWTPELRVR
VVNVIDLMAL LPVVDHPHGF SDEQFVDLFT ASVDVVFAFH GYPRAVHQLV HGRPEPQRFH
VRGFIEQGTT TTPFDMVVLN KISRYHLALA ALDRAHTAPA GAEELRQHCQ DRLARHDAYI
REHFEDLPEI RQWRWS
//
