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Ribokinase (RK) (EC 2.7.1.15)

 A0A0R1PQK7_9LACO        Unreviewed;       302 AA.
A0A0R1PQK7;
20-JAN-2016, integrated into UniProtKB/TrEMBL.
20-JAN-2016, sequence version 1.
27-SEP-2017, entry version 12.
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};
ORFNames=FD33_GL000015 {ECO:0000313|EMBL:KRL30792.1};
Lactobacillus paralimentarius DSM 13238 = JCM 10415.
Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
Lactobacillus.
NCBI_TaxID=1122151 {ECO:0000313|EMBL:KRL30792.1, ECO:0000313|Proteomes:UP000051908};
[1] {ECO:0000313|EMBL:KRL30792.1, ECO:0000313|Proteomes:UP000051908}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=DSM 13238 {ECO:0000313|EMBL:KRL30792.1,
ECO:0000313|Proteomes:UP000051908};
PubMed=26415554; DOI=10.1038/ncomms9322;
Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X.,
Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E.,
Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O.,
Ritari J., Douillard F.P., Paul Ross R., Yang R., Briner A.E.,
Felis G.E., de Vos W.M., Barrangou R., Klaenhammer T.R.,
Caufield P.W., Cui Y., Zhang H., O'Toole P.W.;
"Expanding the biotechnology potential of lactobacilli through
comparative genomics of 213 strains and associated genera.";
Nat. Commun. 6:8322-8322(2015).
-!- 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}.
-!- CAUTION: The sequence shown here is derived from an
EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
preliminary data. {ECO:0000313|EMBL:KRL30792.1}.
-----------------------------------------------------------------------
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-----------------------------------------------------------------------
EMBL; AZES01000078; KRL30792.1; -; Genomic_DNA.
RefSeq; WP_025084877.1; NZ_BAMH01000011.1.
EnsemblBacteria; KRL30792; KRL30792; FD33_GL000015.
PATRIC; fig|1122151.5.peg.16; -.
UniPathway; UPA00916; UER00889.
Proteomes; UP000051908; Unassembled WGS sequence.
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.
TIGRFAMs; TIGR02152; D_ribokin_bact; 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:UP000051908};
Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01987};
Kinase {ECO:0000256|HAMAP-Rule:MF_01987,
ECO:0000256|SAAS:SAAS00644883, ECO:0000313|EMBL:KRL30792.1};
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, ECO:0000313|EMBL:KRL30792.1}.
DOMAIN 1 295 PfkB. {ECO:0000259|Pfam:PF00294}.
NP_BIND 221 226 ATP. {ECO:0000256|HAMAP-Rule:MF_01987}.
NP_BIND 252 253 ATP. {ECO:0000256|HAMAP-Rule:MF_01987}.
REGION 11 13 Substrate binding. {ECO:0000256|HAMAP-
Rule:MF_01987}.
REGION 39 43 Substrate binding. {ECO:0000256|HAMAP-
Rule:MF_01987}.
ACT_SITE 253 253 Proton acceptor. {ECO:0000256|HAMAP-
Rule:MF_01987}.
METAL 247 247 Potassium. {ECO:0000256|HAMAP-
Rule:MF_01987}.
METAL 249 249 Potassium; via carbonyl oxygen.
{ECO:0000256|HAMAP-Rule:MF_01987}.
METAL 284 284 Potassium; via carbonyl oxygen.
{ECO:0000256|HAMAP-Rule:MF_01987}.
METAL 287 287 Potassium; via carbonyl oxygen.
{ECO:0000256|HAMAP-Rule:MF_01987}.
METAL 289 289 Potassium; via carbonyl oxygen.
{ECO:0000256|HAMAP-Rule:MF_01987}.
METAL 293 293 Potassium. {ECO:0000256|HAMAP-
Rule:MF_01987}.
BINDING 140 140 Substrate. {ECO:0000256|HAMAP-
Rule:MF_01987}.
BINDING 185 185 ATP. {ECO:0000256|HAMAP-Rule:MF_01987}.
BINDING 253 253 Substrate. {ECO:0000256|HAMAP-
Rule:MF_01987}.
SEQUENCE 302 AA; 31873 MW; FD781B9E90FB8CB8 CRC64;
MKKIVVLGSI NVDTILNIPR LPLPGETMAM GDQSTAGGGK GANQAIAAVR AGAETTFIAK
VGQDHSADFM LDTFKKDGLK MKYITVDSEA GTGKAYILLD EDGQNSILIY GGANQTITVD
DVENARDTIE NADCLIAQFE TPLDATLAAF QIAKQNDVVT ILNPAPAKTD IPQKLLSLTD
IIVPNETEAE AITGVKAVDK KSIINSAVKL NKLGVKCVII TVGSRGSLYY TDGKESFVDA
YKVSTVDTTA AGDTFIGYLA AKLDSNLANT VEAMKFASKA SSMAVQVKGA QNSIPYVDDV
KI


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