(data stored in ACNUC7421 zone)

SWISSPROT: Q5LWG8_RUEPO

ID   Q5LWG8_RUEPO            Unreviewed;       290 AA.
AC   Q5LWG8;
DT   01-FEB-2005, integrated into UniProtKB/TrEMBL.
DT   01-FEB-2005, sequence version 1.
DT   08-MAY-2019, entry version 78.
DE   RecName: Full=Ribokinase {ECO:0000256|HAMAP-Rule:MF_01987};
DE            Short=RK {ECO:0000256|HAMAP-Rule:MF_01987};
DE            EC=2.7.1.15 {ECO:0000256|HAMAP-Rule:MF_01987};
GN   Name=rbsK {ECO:0000256|HAMAP-Rule:MF_01987,
GN   ECO:0000313|EMBL:AAV93344.1};
GN   OrderedLocusNames=SPO0013 {ECO:0000313|EMBL:AAV93344.1};
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:AAV93344.1, ECO:0000313|Proteomes:UP000001023};
RN   [1] {ECO:0000313|EMBL:AAV93344.1, 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:AAV93344.1, 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 at O-5 in a
CC       reaction requiring ATP and magnesium. The resulting D-ribose-5-
CC       phosphate can then be used either for sythesis of nucleotides,
CC       histidine, and tryptophan, or as a component of the pentose
CC       phosphate pathway. {ECO:0000256|HAMAP-Rule:MF_01987}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + D-ribose = ADP + D-ribose 5-phosphate + H(+);
CC         Xref=Rhea:RHEA:13697, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:47013, ChEBI:CHEBI:78346, ChEBI:CHEBI:456216;
CC         EC=2.7.1.15; Evidence={ECO:0000256|HAMAP-Rule:MF_01987};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01987};
CC       Note=Requires a divalent cation, most likely magnesium in vivo, as
CC       an electrophilic catalyst to aid phosphoryl group transfer. It is
CC       the chelate of the metal and the nucleotide that is the actual
CC       substrate. {ECO:0000256|HAMAP-Rule:MF_01987};
CC   -!- ACTIVITY REGULATION: Activated by a monovalent cation that binds
CC       near, but not in, the active site. The most likely occupant of the
CC       site in vivo is potassium. Ion binding induces a conformational
CC       change that may alter substrate affinity. {ECO:0000256|HAMAP-
CC       Rule:MF_01987}.
CC   -!- PATHWAY: Carbohydrate metabolism; D-ribose degradation; D-ribose
CC       5-phosphate from beta-D-ribopyranose: step 2/2.
CC       {ECO:0000256|HAMAP-Rule:MF_01987}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01987}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01987}.
CC   -!- SIMILARITY: Belongs to the carbohydrate kinase PfkB family.
CC       Ribokinase subfamily. {ECO:0000256|HAMAP-Rule:MF_01987}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|HAMAP-Rule:MF_01987}.
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DR   EMBL; CP000031; AAV93344.1; -; Genomic_DNA.
DR   RefSeq; WP_011045785.1; NC_003911.12.
DR   STRING; 246200.SPO0013; -.
DR   EnsemblBacteria; AAV93344; AAV93344; SPO0013.
DR   KEGG; sil:SPO0013; -.
DR   eggNOG; ENOG4108RVA; Bacteria.
DR   eggNOG; COG0524; LUCA.
DR   HOGENOM; HOG000235950; -.
DR   KO; K00852; -.
DR   OMA; TFCGYFA; -.
DR   OrthoDB; 1030724at2; -.
DR   BioCyc; RPOM246200:G1G48-13-MONOMER; -.
DR   UniPathway; UPA00916; UER00889.
DR   Proteomes; UP000001023; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004747; F:ribokinase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0019303; P:D-ribose catabolic process; IEA:UniProtKB-UniRule.
DR   CDD; cd01174; ribokinase; 1.
DR   Gene3D; 3.40.1190.20; -; 1.
DR   HAMAP; MF_01987; Ribokinase; 1.
DR   InterPro; IPR011877; D_ribokin.
DR   InterPro; IPR011611; PfkB_dom.
DR   InterPro; IPR002139; Ribo/fructo_kinase.
DR   InterPro; IPR029056; Ribokinase-like.
DR   Pfam; PF00294; PfkB; 1.
DR   PRINTS; PR00990; RIBOKINASE.
DR   SUPFAM; SSF53613; SSF53613; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q5LWG8.
DR   SWISS-2DPAGE; Q5LWG8.
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_01987};
KW   Carbohydrate metabolism {ECO:0000256|HAMAP-Rule:MF_01987};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001023};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01987};
KW   Kinase {ECO:0000256|HAMAP-Rule:MF_01987,
KW   ECO:0000256|SAAS:SAAS00446051, ECO:0000313|EMBL:AAV93344.1};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_01987};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_01987};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01987};
KW   Potassium {ECO:0000256|HAMAP-Rule:MF_01987};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001023};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_01987,
KW   ECO:0000256|SAAS:SAAS00061368, ECO:0000313|EMBL:AAV93344.1}.
FT   DOMAIN        5    280       PfkB. {ECO:0000259|Pfam:PF00294}.
FT   NP_BIND     205    210       ATP. {ECO:0000256|HAMAP-Rule:MF_01987}.
FT   NP_BIND     238    239       ATP. {ECO:0000256|HAMAP-Rule:MF_01987}.
FT   REGION       10     12       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_01987}.
FT   REGION       38     42       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_01987}.
FT   ACT_SITE    239    239       Proton acceptor. {ECO:0000256|HAMAP-Rule:
FT                                MF_01987}.
FT   METAL       233    233       Potassium. {ECO:0000256|HAMAP-Rule:
FT                                MF_01987}.
FT   METAL       235    235       Potassium; via carbonyl oxygen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01987}.
FT   METAL       269    269       Potassium; via carbonyl oxygen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01987}.
FT   METAL       272    272       Potassium; via carbonyl oxygen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01987}.
FT   METAL       274    274       Potassium; via carbonyl oxygen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01987}.
FT   BINDING     136    136       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01987}.
FT   BINDING     179    179       ATP. {ECO:0000256|HAMAP-Rule:MF_01987}.
FT   BINDING     239    239       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01987}.
SQ   SEQUENCE   290 AA;  30535 MW;  F27F70CDD4906D50 CRC64;
     MAIWNLGSIN ADMVYAVPHL PGPGETLAAS GLERFLGGKG ANMSVAAARA GSQVRHIGAV
     GPEGRWAIDR LTEYGVDTRH IATLEAPTGH AIIAVEPGGE NLIVLLPGAN RAISPERVGS
     VLLDAAPGDL LVMQNETSAQ VEAARLGRER GLTVCYAAAP FDAQAVRDVL PWLDFLILNA
     VEAEQLQEAT GLTPDQLPVS HVIVTLGSKG ARHFDTDKGI STEYPAYRVK AVDTTGAGDT
     FTGYVLSGMD RGLPMPQAIT QAMRAAALMV MRHGTADVIP DLKEVLAARF
//

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