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Database: UniProt
Entry: R1ETU8_BOTPV
LinkDB: R1ETU8_BOTPV
Original site: R1ETU8_BOTPV 
ID   R1ETU8_BOTPV            Unreviewed;       305 AA.
AC   R1ETU8;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   25-APR-2018, entry version 26.
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=UCRNP2_1991 {ECO:0000313|EMBL:EOD51243.1};
OS   Botryosphaeria parva (strain UCR-NP2) (Grapevine canker fungus)
OS   (Neofusicoccum parvum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
OC   Dothideomycetes; Dothideomycetes incertae sedis; Botryosphaeriales;
OC   Botryosphaeriaceae; Neofusicoccum.
OX   NCBI_TaxID=1287680 {ECO:0000313|EMBL:EOD51243.1, ECO:0000313|Proteomes:UP000013521};
RN   [1] {ECO:0000313|Proteomes:UP000013521}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UCR-NP2 {ECO:0000313|Proteomes:UP000013521};
RX   PubMed=23766404; DOI=10.1128/genomeA.00339-13;
RA   Blanco-Ulate B., Rolshausen P., Cantu D.;
RT   "Draft genome sequence of Neofusicoccum parvum isolate UCR-NP2, a
RT   fungal vascular pathogen associated with grapevine cankers.";
RL   Genome Announc. 1:E0033913-E0033913(2013).
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; KB915886; EOD51243.1; -; Genomic_DNA.
DR   RefSeq; XP_007581302.1; XM_007581240.1.
DR   EnsemblFungi; EOD51243; EOD51243; UCRNP2_1991.
DR   KEGG; npa:UCRNP2_1991; -.
DR   KO; K00852; -.
DR   OrthoDB; EOG092C3WGL; -.
DR   UniPathway; UPA00916; UER00889.
DR   Proteomes; UP000013521; 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; 2.
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:UP000013521};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03215};
KW   Kinase {ECO:0000256|HAMAP-Rule:MF_03215,
KW   ECO:0000256|RuleBase:RU003704, ECO:0000313|EMBL:EOD51243.1};
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:UP000013521};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_03215,
KW   ECO:0000256|RuleBase:RU003704}.
FT   DOMAIN        6    235       PfkB. {ECO:0000259|Pfam:PF00294}.
FT   DOMAIN      237    297       PfkB. {ECO:0000259|Pfam:PF00294}.
FT   NP_BIND     247    248       ATP. {ECO:0000256|HAMAP-Rule:MF_03215}.
FT   REGION       13     15       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_03215}.
FT   REGION       41     45       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_03215}.
FT   ACT_SITE    248    248       Proton acceptor. {ECO:0000256|HAMAP-Rule:
FT                                MF_03215}.
FT   METAL       242    242       Potassium. {ECO:0000256|HAMAP-Rule:
FT                                MF_03215}.
FT   METAL       244    244       Potassium; via carbonyl oxygen.
FT                                {ECO:0000256|HAMAP-Rule:MF_03215}.
FT   METAL       286    286       Potassium; via carbonyl oxygen.
FT                                {ECO:0000256|HAMAP-Rule:MF_03215}.
FT   METAL       289    289       Potassium; via carbonyl oxygen.
FT                                {ECO:0000256|HAMAP-Rule:MF_03215}.
FT   METAL       291    291       Potassium; via carbonyl oxygen.
FT                                {ECO:0000256|HAMAP-Rule:MF_03215}.
FT   BINDING     149    149       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_03215}.
FT   BINDING     193    193       ATP. {ECO:0000256|HAMAP-Rule:MF_03215}.
FT   BINDING     248    248       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_03215}.
FT   BINDING     280    280       ATP. {ECO:0000256|HAMAP-Rule:MF_03215}.
SQ   SEQUENCE   305 AA;  31439 MW;  3DAA632A0E9CF519 CRC64;
     MPLPIIAVLG SLNVDLVTRT PRVPSAGETL IAGGFSTGYG GKGANQAVAC ARLSRRASSP
     DAGTVEVRMV GAVGVDEFSG GFLDSLRRDG VDVRGVRTLG GGERTGVAVI VVEEASGENR
     ILVSPGANDR VEARPLLPEG TALAVFQLEV PLEVVLVNVR DAKARGVDVL INPAPAVPLP
     DELYEGLGHL VVNESEAALL AGKSAEEITP DSDLTAVAAD FIRRGVKNVI ITLGSAKVQV
     VDTTAAGDTF VGAYAVAVAR NRADPTKTAF DMDAAIAFAN RAAGQTVQRK GAQSAIPWVD
     EVPEA
//
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