ACL_RS06795

Uniprot: A9NE05
Description: ribokinase
EC number: 2.7.1.15
Annotation score: 3 out of 5
Miscellaneous [CC]:
Protein existence: Inferred from homology
Catalytic activity: CATALYTIC ACTIVITY: ATP + D-ribose = ADP + D-ribose 5-phosphate. {ECO:0000256|HAMAP-Rule:MF_01987}.
Cofactor: 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: 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}.
Function [CC]: 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}.
Pathway: PATHWAY: Carbohydrate metabolism; D-ribose degradation; D-ribose 5-phosphate from beta-D-ribopyranose: step 2/2. {ECO:0000256|HAMAP-Rule:MF_01987}.
Active site: ACT_SITE 252 252 Proton acceptor. {ECO:0000256|HAMAP-Rule:MF_01987}.
Binding site: BINDING 140 140 Substrate. {ECO:0000256|HAMAP-Rule:MF_01987}.; BINDING 184 184 ATP. {ECO:0000256|HAMAP-Rule:MF_01987}.; BINDING 252 252 Substrate. {ECO:0000256|HAMAP-Rule:MF_01987}.
Calcium binding:
DNA binding:
Metal binding: METAL 246 246 Potassium. {ECO:0000256|HAMAP-Rule:MF_01987}.; METAL 248 248 Potassium; via carbonyl oxygen. {ECO:0000256|HAMAP-Rule:MF_01987}.; METAL 282 282 Potassium; via carbonyl oxygen. {ECO:0000256|HAMAP-Rule:MF_01987}.; METAL 285 285 Potassium; via carbonyl oxygen. {ECO:0000256|HAMAP-Rule:MF_01987}.; METAL 287 287 Potassium; via carbonyl oxygen. {ECO:0000256|HAMAP-Rule:MF_01987}.
Nucleotide binding: NP_BIND 220 225 ATP. {ECO:0000256|HAMAP-Rule:MF_01987}.; NP_BIND 251 252 ATP. {ECO:0000256|HAMAP-Rule:MF_01987}.
Site:
Gene names (primary): rbsK
Gene names (synonym):
Mass: 33,536
Subunit structure [CC]: SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01987}.
Gene ontology (GO): cytoplasm [GO:0005737]; ATP binding [GO:0005524]; metal ion binding [GO:0046872]; ribokinase activity [GO:0004747]; D-ribose catabolic process [GO:0019303]
Gene ontology IDs: GO:0004747; GO:0005524; GO:0005737; GO:0019303; GO:0046872
Chain:
Signal peptide:
Domain [CC]:
Sequence similarities: SIMILARITY: Belongs to the carbohydrate kinase PfkB family. Ribokinase subfamily. {ECO:0000256|HAMAP-Rule:MF_01987}.
Protein families: Carbohydrate kinase PfkB family, Ribokinase subfamily
Coiled coil:
Domain [FT]: DOMAIN 5 290 PfkB. {ECO:0000259|Pfam:PF00294}.
Motif:
Region: REGION 14 16 Substrate binding. {ECO:0000256|HAMAP-Rule:MF_01987}.
EMBL: CP000896
ProteinModelPortal: A9NE05
MEROPS:
EnsemblBacteria KO: ABX81965
UniPathway: K00852
CDD:
Gene3D:
HAMAP: 3.40.1190.20
InterPro: MF_01987
PANTHER: IPR002173;IPR011877;IPR011611;IPR002139;IPR029056
PIRSF:
PRINTS:
PROSITE: PR00990
Pfam: PS00584
ProDom: PF00294
SMART:
SUPFAM:
TIGRFAMs: SSF53613

1436663-1437584(-)

>nucleotide sequence
TCATTTTGATTCCTCCATTAATTTTTCTATATCACTGTAGGTGCCCATTGCATCTTCGAC
ACCTTCTTTTAAGCAAGCATATGCGCCAGCTGCTGATGCAATCTTTAAGCATGTTGTTAT
AGGTTCATGCATTGCTAATCCATAAGCAAATGCTCCTATGTAAGCATCACCAGCACCAGT
TGTATCTACTGTTTTAATCTTATAGGCTTTGGATTCATATAACTCATCTTTAGACATGTA
GACAGAACCTTTAGAGCCCATTGTAACTATTAATCTTGTGATACCTTTTTTAAATAAATA
TGATGCTGCTTTTTTAACATCTTGTTCGTGTGTTGGGTATACACCTGATAAAATCTCACA
TTCTGTTTGATTTAAAATAATGTAATCCACATAAGGATAAATATCTTCCTCTAAATATCT
AGAAGGCGCAGGATTTAGAATCGTAATCATATTTAATGACTTCGCCTTCTTAAACGCACT
CTTTACAATTTCATACGGAATTTCATATTGAGATACCAATATATCACCTGGATTTCCTTG
AACTGCCTCTAGTACTTTATCTTGTTCTATTTTATGGTTTGCACCCTCATGTAATATAAT
TCGATTATCACGATTAGTTCGTGTAATAAAGGCCATTCCAGTATGGCTGTCTGCTAATGA
TACGTATCTAGTATCAACACCATTTTTTTCGATGGATATTAATGCTTCTTTGCCAAAAAT
ATCTTTACCAACAGCAGCAATCAAATAAGTTTTAGCGCCAAGTTTTGCTGCTGAGACAGC
CTGATTTGCTCCCTTATCCCCAATATTTTTGATAAATTCATGACCACTTTTAGTTTCCCC
TTCAAGTGGTATTTTGTCAACTGAAATTGACATATCAACATTAATACTACCTAATACATA
TACTTTATTTTTTTGGTTCAT

>protein sequence
MNQKNKVYVLGSINVDMSISVDKIPLEGETKSGHEFIKNIGDKGANQAVSAAKLGAKTYL
IAAVGKDIFGKEALISIEKNGVDTRYVSLADSHTGMAFITRTNRDNRIILHEGANHKIEQ
DKVLEAVQGNPGDILVSQYEIPYEIVKSAFKKAKSLNMITILNPAPSRYLEEDIYPYVDY
IILNQTECEILSGVYPTHEQDVKKAASYLFKKGITRLIVTMGSKGSVYMSKDELYESKAY
KIKTVDTTGAGDAYIGAFAYGLAMHEPITTCLKIASAAGAYACLKEGVEDAMGTYSDIEK
LMEESKW