(data stored in SCRATCH zone)

SWISSPROT: Q5LW68_RUEPO

ID   Q5LW68_RUEPO            Unreviewed;       182 AA.
AC   Q5LW68;
DT   01-FEB-2005, integrated into UniProtKB/TrEMBL.
DT   01-FEB-2005, sequence version 1.
DT   08-MAY-2019, entry version 83.
DE   RecName: Full=Ribose 1,5-bisphosphate phosphokinase PhnN {ECO:0000256|HAMAP-Rule:MF_00836};
DE            EC=2.7.4.23 {ECO:0000256|HAMAP-Rule:MF_00836};
DE   AltName: Full=Ribose 1,5-bisphosphokinase {ECO:0000256|HAMAP-Rule:MF_00836};
GN   Name=phnN {ECO:0000256|HAMAP-Rule:MF_00836,
GN   ECO:0000313|EMBL:AAV93792.1};
GN   OrderedLocusNames=SPO0474 {ECO:0000313|EMBL:AAV93792.1};
OS   Ruegeria pomeroyi (strain ATCC 700808 / DSM 15171 / DSS-3)
OS   (Silicibacter pomeroyi).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Ruegeria.
OX   NCBI_TaxID=246200 {ECO:0000313|EMBL:AAV93792.1, ECO:0000313|Proteomes:UP000001023};
RN   [1] {ECO:0000313|EMBL:AAV93792.1, ECO:0000313|Proteomes:UP000001023}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700808 / DSM 15171 / DSS-3
RC   {ECO:0000313|Proteomes:UP000001023};
RX   PubMed=15602564; DOI=10.1038/nature03170;
RA   Moran M.A., Buchan A., Gonzalez J.M., Heidelberg J.F., Whitman W.B.,
RA   Kiene R.P., Henriksen J.R., King G.M., Belas R., Fuqua C., Brinkac L.,
RA   Lewis M., Johri S., Weaver B., Pai G., Eisen J.A., Rahe E.,
RA   Sheldon W.M., Ye W., Miller T.R., Carlton J., Rasko D.A.,
RA   Paulsen I.T., Ren Q., Daugherty S.C., Deboy R.T., Dodson R.J.,
RA   Durkin A.S., Madupu R., Nelson W.C., Sullivan S.A., Rosovitz M.J.,
RA   Haft D.H., Selengut J., Ward N.;
RT   "Genome sequence of Silicibacter pomeroyi reveals adaptations to the
RT   marine environment.";
RL   Nature 432:910-913(2004).
RN   [2] {ECO:0000313|EMBL:AAV93792.1, ECO:0000313|Proteomes:UP000001023}
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 700808 / DSM 15171 / DSS-3
RC   {ECO:0000313|Proteomes:UP000001023};
RX   PubMed=25780504; DOI=10.1186/1944-3277-9-11;
RA   Rivers A.R., Smith C.B., Moran M.A.;
RT   "An updated genome annotation for the model marine bacterium Ruegeria
RT   pomeroyi DSS-3.";
RL   Stand. Genomic Sci. 9:11-11(2014).
CC   -!- FUNCTION: Catalyzes the phosphorylation of ribose 1,5-bisphosphate
CC       to 5-phospho-D-ribosyl alpha-1-diphosphate (PRPP).
CC       {ECO:0000256|HAMAP-Rule:MF_00836}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=alpha-D-ribose 1,5-bisphosphate + ATP = 5-phospho-alpha-
CC         D-ribose 1-diphosphate + ADP; Xref=Rhea:RHEA:20109,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:58017, ChEBI:CHEBI:68688,
CC         ChEBI:CHEBI:456216; EC=2.7.4.23; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00836};
CC   -!- PATHWAY: Metabolic intermediate biosynthesis; 5-phospho-alpha-D-
CC       ribose 1-diphosphate biosynthesis; 5-phospho-alpha-D-ribose 1-
CC       diphosphate from D-ribose 5-phosphate (route II): step 3/3.
CC       {ECO:0000256|HAMAP-Rule:MF_00836}.
CC   -!- SIMILARITY: Belongs to the ribose 1,5-bisphosphokinase family.
CC       {ECO:0000256|HAMAP-Rule:MF_00836}.
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DR   EMBL; CP000031; AAV93792.1; -; Genomic_DNA.
DR   RefSeq; WP_011046235.1; NC_003911.12.
DR   STRING; 246200.SPO0474; -.
DR   EnsemblBacteria; AAV93792; AAV93792; SPO0474.
DR   KEGG; sil:SPO0474; -.
DR   eggNOG; ENOG4105MFQ; Bacteria.
DR   eggNOG; COG3709; LUCA.
DR   HOGENOM; HOG000037637; -.
DR   KO; K05774; -.
DR   OMA; MARLIWL; -.
DR   OrthoDB; 1724909at2; -.
DR   BioCyc; RPOM246200:G1G48-480-MONOMER; -.
DR   UniPathway; UPA00087; UER00175.
DR   Proteomes; UP000001023; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0033863; F:ribose 1,5-bisphosphate phosphokinase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006015; P:5-phosphoribose 1-diphosphate biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0019634; P:organic phosphonate metabolic process; ISS:TIGR.
DR   HAMAP; MF_00836; PhnN; 1.
DR   InterPro; IPR008145; GK/Ca_channel_bsu.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR012699; PhnN.
DR   SMART; SM00072; GuKc; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR02322; phosphon_PhnN; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q5LW68.
DR   SWISS-2DPAGE; Q5LW68.
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00836};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001023};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00836};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001023};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00836}.
FT   DOMAIN        3    181       GuKc. {ECO:0000259|SMART:SM00072}.
FT   NP_BIND      11     18       ATP. {ECO:0000256|HAMAP-Rule:MF_00836}.
SQ   SEQUENCE   182 AA;  19480 MW;  F4AA671D6D062E38 CRC64;
     MTQVPVIAVV GPSGVGKDSV MTALATRDPR VHLIRRVITR PEDAGGEAFT GVSRQEFEAM
     RAAGAFALSW EAHGLCYGVP MPSEVKQADA RALLVNLSRG VLLRAQEVFH PFAVLSLTAR
     PEVLAARLAA RGREDAAEQA RRLGRAGMAL PEGVRRVITV DNSGPLERTV DAVLAHLQRE
     SA
//

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