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Database: UniProt
Entry: A0A089YU73_9PSED
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ID   A0A089YU73_9PSED        Unreviewed;       305 AA.
AC   A0A089YU73;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   28-MAR-2018, entry version 22.
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   ORFNames=LT40_07575 {ECO:0000313|EMBL:AIS17270.1};
OS   Pseudomonas rhizosphaerae.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=216142 {ECO:0000313|EMBL:AIS17270.1, ECO:0000313|Proteomes:UP000029499};
RN   [1] {ECO:0000313|EMBL:AIS17270.1, ECO:0000313|Proteomes:UP000029499}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 16299 {ECO:0000313|EMBL:AIS17270.1};
RX   PubMed=25483321; DOI=10.1016/j.jbiotec.2014.11.031;
RA   Kwak Y., Jung B.K., Shin J.H.;
RT   "Complete genome sequence of Pseudomonas rhizosphaerae IH5T (=DSM
RT   16299T), a phosphate-solubilizing rhizobacterium for bacterial
RT   biofertilizer.";
RL   J. Biotechnol. 193:137-138(2015).
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: ATP + D-ribose = ADP + D-ribose 5-phosphate.
CC       {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   -!- ENZYME 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; CP009533; AIS17270.1; -; Genomic_DNA.
DR   RefSeq; WP_043188356.1; NZ_CP009533.1.
DR   EnsemblBacteria; AIS17270; AIS17270; LT40_07575.
DR   KEGG; prh:LT40_07575; -.
DR   KO; K00852; -.
DR   UniPathway; UPA00916; UER00889.
DR   Proteomes; UP000029499; 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; IPR002173; Carboh/pur_kinase_PfkB_CS.
DR   InterPro; IPR011877; D_ribokin.
DR   InterPro; IPR011611; PfkB_dom.
DR   InterPro; IPR002139; Ribo/fructo_kinase.
DR   InterPro; IPR029056; Ribokinase-like.
DR   InterPro; IPR017583; Tagatose/fructose_Pkinase.
DR   Pfam; PF00294; PfkB; 1.
DR   PIRSF; PIRSF000535; 1PFK/6PFK/LacC; 1.
DR   PRINTS; PR00990; RIBOKINASE.
DR   SUPFAM; SSF53613; SSF53613; 1.
DR   TIGRFAMs; TIGR02152; D_ribokin_bact; 1.
DR   PROSITE; PS00584; PFKB_KINASES_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_01987};
KW   Carbohydrate metabolism {ECO:0000256|HAMAP-Rule:MF_01987};
KW   Complete proteome {ECO:0000313|Proteomes:UP000029499};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01987};
KW   Kinase {ECO:0000256|HAMAP-Rule:MF_01987,
KW   ECO:0000256|RuleBase:RU003704, ECO:0000256|SAAS:SAAS00061343,
KW   ECO:0000313|EMBL:AIS17270.1};
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:UP000029499};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_01987,
KW   ECO:0000256|PIRNR:PIRNR000535, ECO:0000256|RuleBase:RU003704,
KW   ECO:0000256|SAAS:SAAS00061368}.
FT   DOMAIN        3    296       PfkB. {ECO:0000259|Pfam:PF00294}.
FT   NP_BIND     222    227       ATP. {ECO:0000256|HAMAP-Rule:MF_01987}.
FT   NP_BIND     253    254       ATP. {ECO:0000256|HAMAP-Rule:MF_01987}.
FT   REGION       12     14       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_01987}.
FT   REGION       40     44       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_01987}.
FT   ACT_SITE    254    254       Proton acceptor. {ECO:0000256|HAMAP-Rule:
FT                                MF_01987}.
FT   METAL       248    248       Potassium. {ECO:0000256|HAMAP-Rule:
FT                                MF_01987}.
FT   METAL       250    250       Potassium; via carbonyl oxygen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01987}.
FT   METAL       284    284       Potassium; via carbonyl oxygen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01987}.
FT   METAL       287    287       Potassium; via carbonyl oxygen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01987}.
FT   METAL       289    289       Potassium; via carbonyl oxygen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01987}.
FT   METAL       293    293       Potassium. {ECO:0000256|HAMAP-Rule:
FT                                MF_01987}.
FT   BINDING     141    141       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01987}.
FT   BINDING     186    186       ATP. {ECO:0000256|HAMAP-Rule:MF_01987}.
FT   BINDING     254    254       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01987}.
SQ   SEQUENCE   305 AA;  30961 MW;  328F9718FE7A0CE3 CRC64;
     MQANVLVIGS LNMDLVAQAE RLPRAGETLL GQSFATVPGG KGANQAVAAA RLGGQVAMIG
     CVGADAYGHA LRQALADEGI DCQGVRVAED VATGIAMIVV DANSQNAIVI VAGGNGQLEC
     ADIERFDGLL QAADVVVCQL EIPYAVVAFA LERAHQAGKT VILNPAPASG PLPQEWLAWV
     DYLIPNESEA QALTGLAVDS VDDAEQAAGL LHEAGAGKVI ITLGERGVLF AAGAQSRHYP
     GRKVQAVDTT AAGDTFVGGF AAALARGLDE SQAIAFGQAA AALSVTHAGA QPSIPTLAQV
     EQVLS
//
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