ID   A0A154P6D5_DUFNO        Unreviewed;       309 AA.
AC   A0A154P6D5;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   02-JUN-2021, entry version 20.
DE   RecName: Full=Ribokinase {ECO:0000256|ARBA:ARBA00016943, ECO:0000256|HAMAP-Rule:MF_03215};
DE            Short=RK {ECO:0000256|HAMAP-Rule:MF_03215};
DE            EC=2.7.1.15 {ECO:0000256|ARBA:ARBA00012035, ECO:0000256|HAMAP-Rule:MF_03215};
GN   ORFNames=WN55_09393 {ECO:0000313|EMBL:KZC07401.1};
OS   Dufourea novaeangliae (Sweat bee).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Apoidea;
OC   Halictidae; Rophitinae; Dufourea.
OX   NCBI_TaxID=178035 {ECO:0000313|EMBL:KZC07401.1, ECO:0000313|Proteomes:UP000076502};
RN   [1] {ECO:0000313|EMBL:KZC07401.1, ECO:0000313|Proteomes:UP000076502}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=0120121106 {ECO:0000313|EMBL:KZC07401.1};
RC   TISSUE=Whole body {ECO:0000313|EMBL:KZC07401.1};
RA   Pan H., Kapheim K.;
RT   "The genome of Dufourea novaeangliae.";
RL   Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the phosphorylation of ribose at O-5 in a reaction
CC       requiring ATP and magnesium. The resulting D-ribose-5-phosphate can
CC       then be used either for sythesis of nucleotides, histidine, and
CC       tryptophan, or as a component of the pentose phosphate pathway.
CC       {ECO:0000256|HAMAP-Rule:MF_03215}.
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|ARBA:ARBA00000691,
CC         ECO:0000256|HAMAP-Rule:MF_03215};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_03215};
CC       Note=Requires a divalent cation, most likely magnesium in vivo, as an
CC       electrophilic catalyst to aid phosphoryl group transfer. It is the
CC       chelate of the metal and the nucleotide that is the actual substrate.
CC       {ECO:0000256|HAMAP-Rule:MF_03215};
CC   -!- ACTIVITY REGULATION: Activated by a monovalent cation that binds near,
CC       but not in, the active site. The most likely occupant of the site in
CC       vivo is potassium. Ion binding induces a conformational change that may
CC       alter substrate affinity. {ECO:0000256|HAMAP-Rule:MF_03215}.
CC   -!- PATHWAY: Carbohydrate metabolism; D-ribose degradation; D-ribose 5-
CC       phosphate from beta-D-ribopyranose: step 2/2. {ECO:0000256|HAMAP-
CC       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       {ECO:0000256|ARBA:ARBA00010688, ECO:0000256|RuleBase:RU003704}.
CC   -!- SIMILARITY: Belongs to the carbohydrate kinase PfkB family. Ribokinase
CC       subfamily. {ECO:0000256|HAMAP-Rule:MF_03215}.
CC   -!- SIMILARITY: Belongs to the carbohydrate kinase pfkB family.
CC       {ECO:0000256|ARBA:ARBA00005380}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_03215}.
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DR   EMBL; KQ434826; KZC07401.1; -; Genomic_DNA.
DR   RefSeq; XP_015428929.1; XM_015573443.1.
DR   GeneID; 107185697; -.
DR   OrthoDB; 918144at2759; -.
DR   UniPathway; UPA00916; UER00889.
DR   Proteomes; UP000076502; 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   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_03215};
KW   Carbohydrate metabolism {ECO:0000256|HAMAP-Rule:MF_03215};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03215};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|HAMAP-Rule:MF_03215};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_03215};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW   Rule:MF_03215}; Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_03215};
KW   Nucleus {ECO:0000256|HAMAP-Rule:MF_03215};
KW   Potassium {ECO:0000256|ARBA:ARBA00022958, ECO:0000256|HAMAP-Rule:MF_03215};
KW   Reference proteome {ECO:0000313|Proteomes:UP000076502};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_03215}.
FT   DOMAIN          3..299
FT                   /note="PfkB"
FT                   /evidence="ECO:0000259|Pfam:PF00294"
FT   NP_BIND         221..226
FT                   /note="ATP"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03215"
FT   NP_BIND         254..255
FT                   /note="ATP"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03215"
FT   REGION          12..14
FT                   /note="Substrate binding"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03215"
FT   REGION          40..44
FT                   /note="Substrate binding"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03215"
FT   ACT_SITE        255
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03215"
FT   METAL           249
FT                   /note="Potassium"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03215"
FT   METAL           251
FT                   /note="Potassium; via carbonyl oxygen"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03215"
FT   METAL           287
FT                   /note="Potassium; via carbonyl oxygen"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03215"
FT   METAL           290
FT                   /note="Potassium; via carbonyl oxygen"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03215"
FT   METAL           292
FT                   /note="Potassium; via carbonyl oxygen"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03215"
FT   METAL           296
FT                   /note="Potassium"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03215"
FT   BINDING         141
FT                   /note="Substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03215"
FT   BINDING         185
FT                   /note="ATP"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03215"
FT   BINDING         242
FT                   /note="ATP"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03215"
FT   BINDING         255
FT                   /note="Substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03215"
SQ   SEQUENCE   309 AA;  33002 MW;  7E346693EF1605E2 CRC64;
     MSPKIVVVGS CMIDFTSYSP RLPKSGETLV GSNFEIKYGG KGANQCVAAA KLGASTAIVA
     SLGSDVYAQE YLKIFKKENV NVAHVQIQEN QHSGIAHITV ADNGENHIVI VSGSNESLSL
     KHVDAAAEVV RDAAVLLCQF ETPLETTRHA LKLHKDHGLS IVNGAPAMEH VDYDLLSLCD
     IFCVNETEAE IMTGVQPLGL SNMQEAIDKL LDNGCNTVIL TLGKMGAAYA SRKNRTATLV
     PTRRVKPVDT TGAGDAFLGA IAYFKAYHPG LSMDECIRRA CVVATESVLK LGTHASFPTR
     SSLSPDLFV
//