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Database: UniProt
Entry: A0A0P7XQ54_9TELE
LinkDB: A0A0P7XQ54_9TELE
Original site: A0A0P7XQ54_9TELE 
ID   A0A0P7XQ54_9TELE        Unreviewed;       269 AA.
AC   A0A0P7XQ54;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   28-MAR-2018, entry version 10.
DE   RecName: Full=Ribokinase {ECO:0000256|HAMAP-Rule:MF_03215};
DE            Short=RK {ECO:0000256|HAMAP-Rule:MF_03215};
DE            EC=2.7.1.15 {ECO:0000256|HAMAP-Rule:MF_03215};
GN   Name=RBKS {ECO:0000256|HAMAP-Rule:MF_03215};
GN   ORFNames=Z043_103088 {ECO:0000313|EMBL:KPP77490.1};
OS   Scleropages formosus (Asian bonytongue).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Osteoglossocephala;
OC   Osteoglossomorpha; Osteoglossiformes; Osteoglossidae; Scleropages.
OX   NCBI_TaxID=113540 {ECO:0000313|EMBL:KPP77490.1, ECO:0000313|Proteomes:UP000034805};
RN   [1] {ECO:0000313|EMBL:KPP77490.1, ECO:0000313|Proteomes:UP000034805}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Aro1 {ECO:0000313|EMBL:KPP77490.1};
RA   Tan M.H., Gan H.M., Croft L.J., Austin C.M.;
RT   "The genome of the Asian arowana (Scleropages formosus).";
RL   Submitted (AUG-2015) to the EMBL/GenBank/DDBJ databases.
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_03215}.
CC   -!- CATALYTIC ACTIVITY: ATP + D-ribose = ADP + D-ribose 5-phosphate.
CC       {ECO:0000256|HAMAP-Rule:MF_03215}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_03215};
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_03215};
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_03215}.
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_03215}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_03215}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03215}.
CC       Nucleus {ECO:0000256|HAMAP-Rule:MF_03215}.
CC   -!- SIMILARITY: Belongs to the carbohydrate kinase PfkB family.
CC       Ribokinase subfamily. {ECO:0000256|HAMAP-Rule:MF_03215}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|HAMAP-Rule:MF_03215}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:KPP77490.1}.
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DR   EMBL; JARO02000760; KPP77490.1; -; Genomic_DNA.
DR   UniPathway; UPA00916; UER00889.
DR   Proteomes; UP000034805; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; 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   Pfam; PF00294; PfkB; 1.
DR   PRINTS; PR00990; RIBOKINASE.
DR   SUPFAM; SSF53613; SSF53613; 1.
DR   PROSITE; PS00584; PFKB_KINASES_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_03215};
KW   Carbohydrate metabolism {ECO:0000256|HAMAP-Rule:MF_03215};
KW   Complete proteome {ECO:0000313|Proteomes:UP000034805};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03215};
KW   Kinase {ECO:0000256|HAMAP-Rule:MF_03215,
KW   ECO:0000256|RuleBase:RU003704, ECO:0000313|EMBL:KPP77490.1};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_03215};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_03215};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_03215};
KW   Nucleus {ECO:0000256|HAMAP-Rule:MF_03215};
KW   Potassium {ECO:0000256|HAMAP-Rule:MF_03215};
KW   Reference proteome {ECO:0000313|Proteomes:UP000034805};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_03215,
KW   ECO:0000256|RuleBase:RU003704}.
FT   DOMAIN       10    260       PfkB. {ECO:0000259|Pfam:PF00294}.
FT   NP_BIND     182    187       ATP. {ECO:0000256|HAMAP-Rule:MF_03215}.
FT   NP_BIND     215    216       ATP. {ECO:0000256|HAMAP-Rule:MF_03215}.
FT   REGION       25     29       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_03215}.
FT   ACT_SITE    216    216       Proton acceptor. {ECO:0000256|HAMAP-Rule:
FT                                MF_03215}.
FT   METAL       210    210       Potassium. {ECO:0000256|HAMAP-Rule:
FT                                MF_03215}.
FT   METAL       212    212       Potassium; via carbonyl oxygen.
FT                                {ECO:0000256|HAMAP-Rule:MF_03215}.
FT   METAL       248    248       Potassium; via carbonyl oxygen.
FT                                {ECO:0000256|HAMAP-Rule:MF_03215}.
FT   METAL       251    251       Potassium; via carbonyl oxygen.
FT                                {ECO:0000256|HAMAP-Rule:MF_03215}.
FT   METAL       253    253       Potassium; via carbonyl oxygen.
FT                                {ECO:0000256|HAMAP-Rule:MF_03215}.
FT   METAL       257    257       Potassium. {ECO:0000256|HAMAP-Rule:
FT                                MF_03215}.
FT   BINDING     101    101       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_03215}.
FT   BINDING     146    146       ATP. {ECO:0000256|HAMAP-Rule:MF_03215}.
FT   BINDING     203    203       ATP. {ECO:0000256|HAMAP-Rule:MF_03215}.
FT   BINDING     216    216       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_03215}.
FT   BINDING     242    242       ATP. {ECO:0000256|HAMAP-Rule:MF_03215}.
SQ   SEQUENCE   269 AA;  28788 MW;  A190B75D5CB056C9 CRC64;
     MGQAPRLPKA GETIHGHRFF IGFGGKGANQ CVQAARLGAQ TAMRVGLQRK YALPCGLRAE
     FVSQTDRAAT GAASIIVNDA EELWGAEPLL GRAKVLVCQL EIRPDTSLQS LRMARERRVR
     TIFNPAPAVA DLHPDFFRVS DIFCCNETEA EILTGSTVTG PEDAGKVGAE LLRRGCCSVI
     VTLGPQGCVV LSAEDSSPLH IPTATVTALD TTGAGDSFIG ALAFYMARYP TISLEEMARR
     ANQVAAVSVQ AVGTQTSYPW RKDLPPELF
//
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