(data stored in SCRATCH zone)

SWISSPROT: B2TEM2_PARPJ

ID   B2TEM2_PARPJ            Unreviewed;       310 AA.
AC   B2TEM2;
DT   01-JUL-2008, integrated into UniProtKB/TrEMBL.
DT   01-JUL-2008, sequence version 1.
DT   08-MAY-2019, entry version 66.
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   OrderedLocusNames=Bphyt_4160 {ECO:0000313|EMBL:ACD18543.1};
OS   Paraburkholderia phytofirmans (strain DSM 17436 / LMG 22146 / PsJN)
OS   (Burkholderia phytofirmans).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Paraburkholderia.
OX   NCBI_TaxID=398527 {ECO:0000313|EMBL:ACD18543.1, ECO:0000313|Proteomes:UP000001739};
RN   [1] {ECO:0000313|EMBL:ACD18543.1, ECO:0000313|Proteomes:UP000001739}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17436 / LMG 22146 / PsJN
RC   {ECO:0000313|Proteomes:UP000001739};
RX   PubMed=21551308; DOI=10.1128/JB.05055-11;
RA   Weilharter A., Mitter B., Shin M.V., Chain P.S., Nowak J.,
RA   Sessitsch A.;
RT   "Complete genome sequence of the plant growth-promoting endophyte
RT   Burkholderia phytofirmans strain PsJN.";
RL   J. Bacteriol. 193:3383-3384(2011).
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; CP001053; ACD18543.1; -; Genomic_DNA.
DR   RefSeq; WP_012426059.1; NC_010676.1.
DR   STRING; 398527.Bphyt_4160; -.
DR   EnsemblBacteria; ACD18543; ACD18543; Bphyt_4160.
DR   KEGG; bpy:Bphyt_4160; -.
DR   eggNOG; ENOG4108RVA; Bacteria.
DR   eggNOG; COG0524; LUCA.
DR   HOGENOM; HOG000235950; -.
DR   KO; K00852; -.
DR   OMA; DIVLIQQ; -.
DR   OrthoDB; 1030724at2; -.
DR   UniPathway; UPA00916; UER00889.
DR   Proteomes; UP000001739; Chromosome 2.
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.
DR   TIGRFAMs; TIGR02152; D_ribokin_bact; 1.
PE   3: Inferred from homology;
DR   PRODOM; B2TEM2.
DR   SWISS-2DPAGE; B2TEM2.
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_01987};
KW   Carbohydrate metabolism {ECO:0000256|HAMAP-Rule:MF_01987};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001739};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01987};
KW   Kinase {ECO:0000256|HAMAP-Rule:MF_01987,
KW   ECO:0000256|SAAS:SAAS00446051, ECO:0000313|EMBL:ACD18543.1};
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   Transferase {ECO:0000256|HAMAP-Rule:MF_01987,
KW   ECO:0000256|SAAS:SAAS00061368}.
FT   DOMAIN        9    302       PfkB. {ECO:0000259|Pfam:PF00294}.
FT   NP_BIND     227    232       ATP. {ECO:0000256|HAMAP-Rule:MF_01987}.
FT   NP_BIND     259    260       ATP. {ECO:0000256|HAMAP-Rule:MF_01987}.
FT   REGION       17     19       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_01987}.
FT   REGION       45     49       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_01987}.
FT   ACT_SITE    260    260       Proton acceptor. {ECO:0000256|HAMAP-Rule:
FT                                MF_01987}.
FT   METAL       254    254       Potassium. {ECO:0000256|HAMAP-Rule:
FT                                MF_01987}.
FT   METAL       256    256       Potassium; via carbonyl oxygen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01987}.
FT   METAL       290    290       Potassium; via carbonyl oxygen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01987}.
FT   METAL       293    293       Potassium; via carbonyl oxygen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01987}.
FT   METAL       295    295       Potassium; via carbonyl oxygen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01987}.
FT   METAL       299    299       Potassium. {ECO:0000256|HAMAP-Rule:
FT                                MF_01987}.
FT   BINDING     146    146       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01987}.
FT   BINDING     191    191       ATP. {ECO:0000256|HAMAP-Rule:MF_01987}.
FT   BINDING     260    260       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01987}.
SQ   SEQUENCE   310 AA;  31584 MW;  C474D5318AA538D4 CRC64;
     MSKETKQGRV LVVGSINTDL VARAPHLPRP GETIGGHEFS QVAGGKGGNQ AVAAARIGAQ
     VAMVGCVGKD ANGAQRVKDL EAEGIDCSGI EVHPGQPTGV AMVTVSDDGQ NTIVVVAGSN
     GELTPESVAR HEAAIKACDV VVCQLETPWD SVHATLALAR RLGKITVLNP APATGPLPAE
     WLPLVDYLVP NEVEAAILAG LPVESQSGAR RAATELQQGG ARNVIVTLGA QGAYLLVEGG
     EGMHFPAPQV QAVDTTAAGD TFIGVFAAQL ASRQPLESAI SLAQRAASIS VTRAGAQPSI
     PTRAEVDSAA
//

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