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Ribokinase (RK) (EC 2.7.1.15)

 F4APV8_GLAS4            Unreviewed;       298 AA.
F4APV8;
28-JUN-2011, integrated into UniProtKB/TrEMBL.
28-JUN-2011, sequence version 1.
27-SEP-2017, entry version 38.
RecName: Full=Ribokinase {ECO:0000256|HAMAP-Rule:MF_01987};
Short=RK {ECO:0000256|HAMAP-Rule:MF_01987};
EC=2.7.1.15 {ECO:0000256|HAMAP-Rule:MF_01987};
Name=rbsK {ECO:0000256|HAMAP-Rule:MF_01987};
OrderedLocusNames=Glaag_0859 {ECO:0000313|EMBL:AEE21822.1};
Glaciecola sp. (strain 4H-3-7+YE-5).
Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
Alteromonadaceae; Glaciecola.
NCBI_TaxID=983545 {ECO:0000313|EMBL:AEE21822.1, ECO:0000313|Proteomes:UP000006544};
[1] {ECO:0000313|EMBL:AEE21822.1, ECO:0000313|Proteomes:UP000006544}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=4H-3-7+YE-5 {ECO:0000313|EMBL:AEE21822.1,
ECO:0000313|Proteomes:UP000006544};
PubMed=21705587; DOI=10.1128/JB.05468-11;
US DOE Joint Genome Institute;
Klippel B., Lochner A., Bruce D.C., Davenport K.W., Detter C.,
Goodwin L.A., Han J., Han S., Land M.L., Mikhailova N., Nolan M.,
Pennacchio L., Pitluck S., Tapia R., Woyke T., Wiebusch S., Basner A.,
Abe F., Horikoshi K., Keller M., Antranikian G.;
"Complete genome sequence of the marine, cellulose and xylan degrading
bacterium Glaciecola sp. 4H-3-7+YE-5.";
J. Bacteriol. 193:4547-4548(2011).
[2]
NUCLEOTIDE SEQUENCE.
STRAIN=4H-3-7+YE-5;
US DOE Joint Genome Institute;
Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L.,
Pitluck S., Davenport K., Detter J.C., Han C., Tapia R., Land M.,
Hauser L., Kyrpides N., Ivanova N., Mikhailova N., Pagani I.,
Piela B., Lochner A., Antranikian F.I., Woyke T.;
"Complete sequence of chromosome of Glaciecola sp. 4H-3-7+YE-5.";
Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases.
-!- FUNCTION: Catalyzes the phosphorylation of ribose at O-5 in a
reaction requiring ATP and magnesium. The resulting D-ribose-5-
phosphate can then be used either for sythesis of nucleotides,
histidine, and tryptophan, or as a component of the pentose
phosphate pathway. {ECO:0000256|HAMAP-Rule:MF_01987}.
-!- CATALYTIC ACTIVITY: ATP + D-ribose = ADP + D-ribose 5-phosphate.
{ECO:0000256|HAMAP-Rule:MF_01987}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000256|HAMAP-Rule:MF_01987};
Note=Requires a divalent cation, most likely magnesium in vivo, as
an electrophilic catalyst to aid phosphoryl group transfer. It is
the chelate of the metal and the nucleotide that is the actual
substrate. {ECO:0000256|HAMAP-Rule:MF_01987};
-!- ENZYME REGULATION: Activated by a monovalent cation that binds
near, but not in, the active site. The most likely occupant of the
site in vivo is potassium. Ion binding induces a conformational
change that may alter substrate affinity. {ECO:0000256|HAMAP-
Rule:MF_01987}.
-!- PATHWAY: Carbohydrate metabolism; D-ribose degradation; D-ribose
5-phosphate from beta-D-ribopyranose: step 2/2.
{ECO:0000256|HAMAP-Rule:MF_01987}.
-!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01987}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01987}.
-!- SIMILARITY: Belongs to the carbohydrate kinase PfkB family.
Ribokinase subfamily. {ECO:0000256|HAMAP-Rule:MF_01987}.
-!- CAUTION: Lacks conserved residue(s) required for the propagation
of feature annotation. {ECO:0000256|HAMAP-Rule:MF_01987}.
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EMBL; CP002526; AEE21822.1; -; Genomic_DNA.
RefSeq; WP_007989588.1; NC_015497.1.
ProteinModelPortal; F4APV8; -.
STRING; 983545.Glaag_0859; -.
EnsemblBacteria; AEE21822; AEE21822; Glaag_0859.
KEGG; gag:Glaag_0859; -.
eggNOG; ENOG4108RVA; Bacteria.
eggNOG; COG0524; LUCA.
KO; K00852; -.
OrthoDB; POG091H05S4; -.
BioCyc; GSP983545:GH3Q-879-MONOMER; -.
UniPathway; UPA00916; UER00889.
Proteomes; UP000006544; Chromosome.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0004747; F:ribokinase activity; IEA:UniProtKB-UniRule.
GO; GO:0019303; P:D-ribose catabolic process; IEA:UniProtKB-UniRule.
CDD; cd01174; ribokinase; 1.
Gene3D; 3.40.1190.20; -; 1.
HAMAP; MF_01987; Ribokinase; 1.
InterPro; IPR011877; D_ribokin.
InterPro; IPR011611; PfkB_dom.
InterPro; IPR002139; Ribo/fructo_kinase.
InterPro; IPR029056; Ribokinase-like.
Pfam; PF00294; PfkB; 1.
PRINTS; PR00990; RIBOKINASE.
SUPFAM; SSF53613; SSF53613; 1.
3: Inferred from homology;
ATP-binding {ECO:0000256|HAMAP-Rule:MF_01987};
Carbohydrate metabolism {ECO:0000256|HAMAP-Rule:MF_01987};
Complete proteome {ECO:0000313|Proteomes:UP000006544};
Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01987};
Kinase {ECO:0000256|HAMAP-Rule:MF_01987,
ECO:0000256|SAAS:SAAS00644883};
Magnesium {ECO:0000256|HAMAP-Rule:MF_01987};
Metal-binding {ECO:0000256|HAMAP-Rule:MF_01987};
Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01987};
Potassium {ECO:0000256|HAMAP-Rule:MF_01987};
Transferase {ECO:0000256|HAMAP-Rule:MF_01987,
ECO:0000256|SAAS:SAAS00644883}.
DOMAIN 6 285 PfkB. {ECO:0000259|Pfam:PF00294}.
NP_BIND 211 216 ATP. {ECO:0000256|HAMAP-Rule:MF_01987}.
NP_BIND 242 243 ATP. {ECO:0000256|HAMAP-Rule:MF_01987}.
REGION 10 12 Substrate binding. {ECO:0000256|HAMAP-
Rule:MF_01987}.
REGION 38 42 Substrate binding. {ECO:0000256|HAMAP-
Rule:MF_01987}.
ACT_SITE 243 243 Proton acceptor. {ECO:0000256|HAMAP-
Rule:MF_01987}.
METAL 237 237 Potassium. {ECO:0000256|HAMAP-
Rule:MF_01987}.
METAL 239 239 Potassium; via carbonyl oxygen.
{ECO:0000256|HAMAP-Rule:MF_01987}.
METAL 273 273 Potassium; via carbonyl oxygen.
{ECO:0000256|HAMAP-Rule:MF_01987}.
METAL 276 276 Potassium; via carbonyl oxygen.
{ECO:0000256|HAMAP-Rule:MF_01987}.
METAL 278 278 Potassium; via carbonyl oxygen.
{ECO:0000256|HAMAP-Rule:MF_01987}.
METAL 282 282 Potassium. {ECO:0000256|HAMAP-
Rule:MF_01987}.
BINDING 136 136 Substrate. {ECO:0000256|HAMAP-
Rule:MF_01987}.
BINDING 179 179 ATP. {ECO:0000256|HAMAP-Rule:MF_01987}.
BINDING 243 243 Substrate. {ECO:0000256|HAMAP-
Rule:MF_01987}.
SEQUENCE 298 AA; 32010 MW; 7D21A3633A60F439 CRC64;
MAVINFGSIN VDHVYQVDHF VQPGETLAST NYQCLLGGKG ANQSIALAKA GADVRHVGRI
NESDANFKQV MIKHNINCKY VACTESPSGH AIIQVTPTGE NAIVLFGGAN HEISPKDVMA
ALDGAKSSDW VLTQNETSSI DEVLKQAKEA GLKVAFNPAP MTDSVKQLPV DCIDLLIVNE
VEAEEISGHK DIDAMEKYFH ANWPNCEIII TLGKAGVCML KNERRIEVDA FVVDAVDTTA
AGDTFIGFFL SAYSEHTDAK TALTRACAAS ALAVTQVGAA QSIPDEEQVN RFLAKHHS


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