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Database: UniProt
Entry: A0A0D6NST2_9PROT
LinkDB: A0A0D6NST2_9PROT
Original site: A0A0D6NST2_9PROT 
ID   A0A0D6NST2_9PROT        Unreviewed;       332 AA.
AC   A0A0D6NST2;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   28-MAR-2018, entry version 17.
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=Abol_029_023 {ECO:0000313|EMBL:GAN69227.1};
OS   Acetobacter orleanensis JCM 7639.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC   Acetobacteraceae; Acetobacter.
OX   NCBI_TaxID=1231342 {ECO:0000313|EMBL:GAN69227.1, ECO:0000313|Proteomes:UP000032676};
RN   [1] {ECO:0000313|EMBL:GAN69227.1, ECO:0000313|Proteomes:UP000032676}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 7639T {ECO:0000313|EMBL:GAN69227.1,
RC   ECO:0000313|Proteomes:UP000032676};
RA   Azuma Y., Higashiura N., Hirakawa H., Matsushita K.;
RT   "Whole genome sequence of Acetobacter orleanensis JCM 7639T.";
RL   Submitted (NOV-2012) 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_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}.
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:GAN69227.1}.
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DR   EMBL; BAMY01000026; GAN69227.1; -; Genomic_DNA.
DR   EnsemblBacteria; GAN69227; GAN69227; Abol_029_023.
DR   UniPathway; UPA00916; UER00889.
DR   Proteomes; UP000032676; Unassembled WGS sequence.
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   Pfam; PF00294; PfkB; 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:UP000032676};
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:GAN69227.1};
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:UP000032676};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_01987,
KW   ECO:0000256|RuleBase:RU003704, ECO:0000256|SAAS:SAAS00061368}.
FT   DOMAIN       21    317       PfkB. {ECO:0000259|Pfam:PF00294}.
FT   NP_BIND     244    249       ATP. {ECO:0000256|HAMAP-Rule:MF_01987}.
FT   NP_BIND     275    276       ATP. {ECO:0000256|HAMAP-Rule:MF_01987}.
FT   REGION       29     31       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_01987}.
FT   REGION       57     61       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_01987}.
FT   ACT_SITE    276    276       Proton acceptor. {ECO:0000256|HAMAP-Rule:
FT                                MF_01987}.
FT   METAL       270    270       Potassium. {ECO:0000256|HAMAP-Rule:
FT                                MF_01987}.
FT   METAL       272    272       Potassium; via carbonyl oxygen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01987}.
FT   METAL       306    306       Potassium; via carbonyl oxygen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01987}.
FT   METAL       309    309       Potassium; via carbonyl oxygen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01987}.
FT   METAL       311    311       Potassium; via carbonyl oxygen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01987}.
FT   BINDING     162    162       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01987}.
FT   BINDING     208    208       ATP. {ECO:0000256|HAMAP-Rule:MF_01987}.
FT   BINDING     276    276       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01987}.
SQ   SEQUENCE   332 AA;  34396 MW;  CEE9D65FB8072D5C CRC64;
     MLKYVPLTLT GRHAMPNPKP LILSFGSINI DVTARAARLP RPGETVHGES YAVMLGGKGS
     NQAAAAGRLA EGSGIQVALA GRIGQDSFGA QARRELERFG VDLSPLREDA ANPTGVALIG
     IDGSGENCIT VVGGANMAVD ETDVEAAAQW LERTSVLLLQ LEVPQKAVLA AARKARAAGA
     IVVLDPAPAP EQGLLDELWQ EIDILTPNES ETFQLTGIRP ESADDAAKAA NLLLAKGVKA
     VLVKMGSRGV FWHDGTQSGL CAPFSVQPVD TVAAGDCFNA GLAFALAQGQ PLSKAVRIAS
     ACGALATTRH GAADAAPDWK TVETLMAAQP ER
//
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