ID D7AUN8_NOCDD Unreviewed; 782 AA.
AC D7AUN8;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 27-MAR-2024, entry version 68.
DE RecName: Full=Probable phosphoketolase {ECO:0000256|HAMAP-Rule:MF_01403};
DE EC=4.1.2.- {ECO:0000256|HAMAP-Rule:MF_01403};
GN OrderedLocusNames=Ndas_2196 {ECO:0000313|EMBL:ADH67618.1};
OS Nocardiopsis dassonvillei (strain ATCC 23218 / DSM 43111 / CIP 107115 / JCM
OS 7437 / KCTC 9190 / NBRC 14626 / NCTC 10488 / NRRL B-5397 / IMRU 509)
OS (Actinomadura dassonvillei).
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Nocardiopsaceae; Nocardiopsis.
OX NCBI_TaxID=446468 {ECO:0000313|EMBL:ADH67618.1, ECO:0000313|Proteomes:UP000002219};
RN [1] {ECO:0000313|EMBL:ADH67618.1, ECO:0000313|Proteomes:UP000002219}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 23218 / DSM 43111 / CIP 107115 / JCM 7437 / KCTC 9190 /
RC NBRC 14626 / NCTC 10488 / NRRL B-5397 / IMRU 509
RC {ECO:0000313|Proteomes:UP000002219};
RX PubMed=21304737; DOI=10.4056/sigs.1363462;
RA Sun H., Lapidus A., Nolan M., Lucas S., Del Rio T.G., Tice H., Cheng J.F.,
RA Tapia R., Han C., Goodwin L., Pitluck S., Pagani I., Ivanova N.,
RA Mavromatis K., Mikhailova N., Pati A., Chen A., Palaniappan K., Land M.,
RA Hauser L., Chang Y.J., Jeffries C.D., Djao O.D., Rohde M., Sikorski J.,
RA Goker M., Woyke T., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA Kyrpides N.C., Klenk H.P.;
RT "Complete genome sequence of Nocardiopsis dassonvillei type strain (IMRU
RT 509).";
RL Stand. Genomic Sci. 3:325-336(2010).
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; CP002040; ADH67618.1; -; Genomic_DNA.
DR RefSeq; WP_013153225.1; NC_014210.1.
DR AlphaFoldDB; D7AUN8; -.
DR STRING; 446468.Ndas_2196; -.
DR KEGG; nda:Ndas_2196; -.
DR eggNOG; COG3957; Bacteria.
DR HOGENOM; CLU_013954_2_0_11; -.
DR OrthoDB; 9768449at2; -.
DR Proteomes; UP000002219; Chromosome 1.
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:UP000002219};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052, ECO:0000256|HAMAP-
KW Rule:MF_01403}.
FT DOMAIN 4..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; 87777 MW; 29C879583969BECE CRC64;
MALQEDELRG VDAYWRAANY LSVGQIYLLD NPLLREELRP EHIKPRLLGH WGTTPGLNFC
YAHLNRAIRD RDLEMMYVMG PGHGGPAAVA NAWLEGTYSE VYRHVNQDVE GMRRLFRQFS
FPGGVPSHVA PETPGSIHEG GELGYSLAHA QGAAFDNPDL VVACVVGDGE AETGPLAGSW
RGNAFLDPVH DGAVLPILHL NGYKIANPTV LARIPERELL SYFEGLGYRP LLVSGEDPEY
MHRRMAEAVD EALEEIARIQ HRARVSGVRG RAVWPVVILR SPKGWTGPAE VDGVPVEGTW
RSHQVPLGQV RSDEGHLRQL EEWMRSYRPE ELFEESGAPV AEVRAQAPEG ERRMSASPHA
NGGVLRRELV LPDFRGYAVD VGRNGTQTGE ATRVLGRFLR DVIRSNPRTF RLMGPDETAS
NRLDAVFEAS DKEWQAERLA TDEHLGPGGR VMEVLSEHLC QGWLEGYLLT GRHGLFGCYE
AFVHIVDSMF NQHAKWLKVS RDLPWRRPIS SLNYLLTSHV WRQDHNGFTH QDPGFLDVVL
NKPAEVVRVY LPPDANTLLS VADHCLRSSD YVNVVVAGKQ PGLGYLSMEE AVAHCARGIG
IWEWASTDGG ADPDVVLACA GDVPTLEVLA AADLVRRWLP GVRVRVVNVV DLMRLLPDSD
HPHGLPDAEY DALFTTDKPV VFAFHGYPWL VHRLTYRRAG HANLHVRGYR ERGTTTTPFD
MVMLNDLDRF HLVMDVIDRV PGLGQRSAQV RQRMVDERLR HRAHTREFGE DPAEIREWVW
RY
//
