ID   A0A154P6D5_9HYME        Unreviewed;       309 AA.
AC   A0A154P6D5;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   28-MAR-2018, entry version 12.
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   ORFNames=WN55_09393 {ECO:0000313|EMBL:KZC07401.1};
OS   Dufourea novaeangliae.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
OC   Pterygota; Neoptera; Holometabola; Hymenoptera; Apocrita; Aculeata;
OC   Apoidea; 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
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}.
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DR   EMBL; KQ434826; KZC07401.1; -; Genomic_DNA.
DR   RefSeq; XP_015428929.1; XM_015573443.1.
DR   GeneID; 107185697; -.
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   Complete proteome {ECO:0000313|Proteomes:UP000076502};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03215};
KW   Kinase {ECO:0000256|HAMAP-Rule:MF_03215,
KW   ECO:0000256|RuleBase:RU003704, ECO:0000313|EMBL:KZC07401.1};
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:UP000076502};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_03215,
KW   ECO:0000256|RuleBase:RU003704}.
FT   DOMAIN        3    299       PfkB. {ECO:0000259|Pfam:PF00294}.
FT   NP_BIND     221    226       ATP. {ECO:0000256|HAMAP-Rule:MF_03215}.
FT   NP_BIND     254    255       ATP. {ECO:0000256|HAMAP-Rule:MF_03215}.
FT   REGION       12     14       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_03215}.
FT   REGION       40     44       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_03215}.
FT   ACT_SITE    255    255       Proton acceptor. {ECO:0000256|HAMAP-Rule:
FT                                MF_03215}.
FT   METAL       249    249       Potassium. {ECO:0000256|HAMAP-Rule:
FT                                MF_03215}.
FT   METAL       251    251       Potassium; via carbonyl oxygen.
FT                                {ECO:0000256|HAMAP-Rule:MF_03215}.
FT   METAL       287    287       Potassium; via carbonyl oxygen.
FT                                {ECO:0000256|HAMAP-Rule:MF_03215}.
FT   METAL       290    290       Potassium; via carbonyl oxygen.
FT                                {ECO:0000256|HAMAP-Rule:MF_03215}.
FT   METAL       292    292       Potassium; via carbonyl oxygen.
FT                                {ECO:0000256|HAMAP-Rule:MF_03215}.
FT   METAL       296    296       Potassium. {ECO:0000256|HAMAP-Rule:
FT                                MF_03215}.
FT   BINDING     141    141       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_03215}.
FT   BINDING     185    185       ATP. {ECO:0000256|HAMAP-Rule:MF_03215}.
FT   BINDING     242    242       ATP. {ECO:0000256|HAMAP-Rule:MF_03215}.
FT   BINDING     255    255       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                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
//