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Database: UniProt
Entry: A0A142ES28_9BACT
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ID   A0A142ES28_9BACT        Unreviewed;       305 AA.
AC   A0A142ES28;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   28-FEB-2018, entry version 11.
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=AO498_15875 {ECO:0000313|EMBL:AMQ57933.1};
OS   Algoriphagus sp. M8-2.
OC   Bacteria; Bacteroidetes; Cytophagia; Cytophagales; Cyclobacteriaceae;
OC   Algoriphagus.
OX   NCBI_TaxID=1727163 {ECO:0000313|EMBL:AMQ57933.1, ECO:0000313|Proteomes:UP000073816};
RN   [1] {ECO:0000313|Proteomes:UP000073816}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M8-2 {ECO:0000313|Proteomes:UP000073816};
RA   Shintani M.;
RT   "Complete sequence of Algoriphagus sp. M8-2.";
RL   Submitted (SEP-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_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; CP012836; AMQ57933.1; -; Genomic_DNA.
DR   RefSeq; WP_067550590.1; NZ_CP012836.1.
DR   EnsemblBacteria; AMQ57933; AMQ57933; AO498_15875.
DR   KEGG; alm:AO498_15875; -.
DR   PATRIC; fig|1727163.4.peg.3333; -.
DR   KO; K00852; -.
DR   UniPathway; UPA00916; UER00889.
DR   Proteomes; UP000073816; 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; 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;
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_01987};
KW   Carbohydrate metabolism {ECO:0000256|HAMAP-Rule:MF_01987};
KW   Complete proteome {ECO:0000313|Proteomes:UP000073816};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01987};
KW   Kinase {ECO:0000256|HAMAP-Rule:MF_01987,
KW   ECO:0000256|SAAS:SAAS00061343, ECO:0000313|EMBL:AMQ57933.1};
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:UP000073816};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_01987,
KW   ECO:0000256|SAAS:SAAS00061368, ECO:0000313|EMBL:AMQ57933.1}.
FT   DOMAIN        1    293       PfkB. {ECO:0000259|Pfam:PF00294}.
FT   NP_BIND     220    225       ATP. {ECO:0000256|HAMAP-Rule:MF_01987}.
FT   NP_BIND     251    252       ATP. {ECO:0000256|HAMAP-Rule:MF_01987}.
FT   REGION       11     13       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_01987}.
FT   REGION       39     43       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_01987}.
FT   ACT_SITE    252    252       Proton acceptor. {ECO:0000256|HAMAP-Rule:
FT                                MF_01987}.
FT   METAL       246    246       Potassium. {ECO:0000256|HAMAP-Rule:
FT                                MF_01987}.
FT   METAL       248    248       Potassium; via carbonyl oxygen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01987}.
FT   METAL       282    282       Potassium; via carbonyl oxygen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01987}.
FT   METAL       285    285       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       291    291       Potassium. {ECO:0000256|HAMAP-Rule:
FT                                MF_01987}.
FT   BINDING     140    140       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01987}.
FT   BINDING     184    184       ATP. {ECO:0000256|HAMAP-Rule:MF_01987}.
FT   BINDING     252    252       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01987}.
SQ   SEQUENCE   305 AA;  32576 MW;  B3409A5C823746D7 CRC64;
     MAKILVVGSS NTDLVVKTER FPQPGETVVG RDFFLFQGGK GANQAVAAAR MGGKVAFISR
     VGTDLFGSQT KEALEREGIS TAWMSMDASS PTGVAMITVN EQGENHIVVV PGANANLLPE
     ALDEAQDVLL DSEVWLCQLE IPVETAAYLA EKAQSFLKKL ILNPAPATDL PESIYQHLFL
     ITPNETEASL LSDLPCEQEA DYPKVAQWFL DKGVQQVVIT LGEKGAFFKN AELELRIPAP
     SVAAIDTTAA GDVFNGTLAV ALAEGQSWEK ALQTTIQAAS LSVTRMGAQA SAPYRSELFP
     TPPLI
//
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