ID F6IDY5_9SPHN Unreviewed; 296 AA.
AC F6IDY5;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE SubName: Full=Ribose-phosphate pyrophosphokinase {ECO:0000313|EMBL:CCA90510.1};
DE EC=2.7.6.1 {ECO:0000313|EMBL:CCA90510.1};
GN ORFNames=PP1Y_Mpl6065 {ECO:0000313|EMBL:CCA90510.1};
OS Novosphingobium sp. PP1Y.
OG Plasmid Mpl {ECO:0000313|EMBL:CCA90510.1,
OG ECO:0000313|Proteomes:UP000009242}.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Novosphingobium.
OX NCBI_TaxID=702113 {ECO:0000313|EMBL:CCA90510.1, ECO:0000313|Proteomes:UP000009242};
RN [1] {ECO:0000313|EMBL:CCA90510.1, ECO:0000313|Proteomes:UP000009242}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=sp. PP1Y {ECO:0000313|Proteomes:UP000009242};
RC PLASMID=Mpl {ECO:0000313|EMBL:CCA90510.1,
RC ECO:0000313|Proteomes:UP000009242};
RX PubMed=21685292; DOI=10.1128/JB.05349-11;
RA D'Argenio V., Petrillo M., Cantiello P., Naso B., Cozzuto L., Notomista E.,
RA Paolella G., Di Donato A., Salvatore F.;
RT "De novo sequencing and assembly of the whole genome of Novosphingobium sp.
RT strain PP1Y.";
RL J. Bacteriol. 193:4296-4296(2011).
CC -!- SIMILARITY: Belongs to the ribose-phosphate pyrophosphokinase family.
CC {ECO:0000256|RuleBase:RU004324}.
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DR EMBL; FR856861; CCA90510.1; -; Genomic_DNA.
DR RefSeq; WP_013836752.1; NC_015583.1.
DR AlphaFoldDB; F6IDY5; -.
DR KEGG; npp:PP1Y_Mpl6065; -.
DR eggNOG; COG0462; Bacteria.
DR HOGENOM; CLU_033546_2_2_5; -.
DR OrthoDB; 324294at2; -.
DR Proteomes; UP000009242; Plasmid Mpl.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0004749; F:ribose phosphate diphosphokinase activity; IEA:InterPro.
DR GO; GO:0009165; P:nucleotide biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd06223; PRTases_typeI; 1.
DR Gene3D; 3.40.50.2020; -; 2.
DR InterPro; IPR029099; Pribosyltran_N.
DR InterPro; IPR000836; PRibTrfase_dom.
DR InterPro; IPR029057; PRTase-like.
DR InterPro; IPR005946; Rib-P_diPkinase.
DR NCBIfam; TIGR01251; ribP_PPkin; 1.
DR PANTHER; PTHR10210; RIBOSE-PHOSPHATE DIPHOSPHOKINASE FAMILY MEMBER; 1.
DR PANTHER; PTHR10210:SF119; RIBOSE-PHOSPHATE PYROPHOSPHOKINASE; 1.
DR Pfam; PF00156; Pribosyltran; 1.
DR Pfam; PF13793; Pribosyltran_N; 1.
DR SMART; SM01400; Pribosyltran_N; 1.
DR SUPFAM; SSF53271; PRTase-like; 2.
PE 3: Inferred from homology;
KW Kinase {ECO:0000313|EMBL:CCA90510.1};
KW Nucleotide biosynthesis {ECO:0000256|ARBA:ARBA00022727,
KW ECO:0000256|RuleBase:RU004324}; Plasmid {ECO:0000313|EMBL:CCA90510.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000009242};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000313|EMBL:CCA90510.1}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..296
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003341626"
FT DOMAIN 13..113
FT /note="Ribose-phosphate pyrophosphokinase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF13793"
FT DOMAIN 142..253
FT /note="Phosphoribosyltransferase"
FT /evidence="ECO:0000259|Pfam:PF00156"
SQ SEQUENCE 296 AA; 30630 MW; 065133119E31B20D CRC64;
MNALVLGFAH SLSSAQALAA QLGLPCDKVG VHRFPDLESL VQVPRSAPTV ILHRSLNDPN
AKLIELILAA SAARDGGARR VVLVAPYLAY MRQDMAFKPG EAVSQRVIGQ LIAAHFDGIV
TVDPHLHRVA TLAQAVPGIP AIALSAAPVL ASAIEAGQDP VIVGPDSEAR QWIESIARPL
GLDMLLGSKE RFGDRKVALS IAGIEKAKGR SAILVDDVIS SGETLIAAAG ALRKAGAQRI
EALATHCLAS SEDLARMTAS GIARIVSTDS IPGPTCGPTL APLLADALKS SGLLQT
//
