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Database: UniProt
Entry: Q2UAI8_ASPOR
LinkDB: Q2UAI8_ASPOR
Original site: Q2UAI8_ASPOR 
ID   Q2UAI8_ASPOR            Unreviewed;       381 AA.
AC   Q2UAI8;
DT   24-JAN-2006, integrated into UniProtKB/TrEMBL.
DT   24-JAN-2006, sequence version 1.
DT   27-SEP-2017, entry version 66.
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=AO090102000368 {ECO:0000313|EMBL:BAE61427.1};
OS   Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=510516 {ECO:0000313|EMBL:BAE61427.1, ECO:0000313|Proteomes:UP000006564};
RN   [1] {ECO:0000313|EMBL:BAE61427.1, ECO:0000313|Proteomes:UP000006564}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 42149 / RIB 40 {ECO:0000313|Proteomes:UP000006564};
RX   PubMed=16372010; DOI=10.1038/nature04300;
RA   Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G.,
RA   Kusumoto K., Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K.,
RA   Horiuchi H., Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W.,
RA   Galagan J.E., Nierman W.C., Yu J., Archer D.B., Bennett J.W.,
RA   Bhatnagar D., Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H.,
RA   Hosoyama A., Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R.,
RA   Kato M., Kato Y., Kin T., Kokubun A., Maeda H., Maeyama N.,
RA   Maruyama J., Nagasaki H., Nakajima T., Oda K., Okada K., Paulsen I.,
RA   Sakamoto K., Sawano T., Takahashi M., Takase K., Terabayashi Y.,
RA   Wortman J., Yamada O., Yamagata Y., Anazawa H., Hata Y., Koide Y.,
RA   Komori T., Koyama Y., Minetoki T., Suharnan S., Tanaka A., Isono K.,
RA   Kuhara S., Ogasawara N., Kikuchi H.;
RT   "Genome sequencing and analysis of Aspergillus oryzae.";
RL   Nature 438:1157-1161(2005).
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; AP007162; BAE61427.1; -; Genomic_DNA.
DR   RefSeq; XP_001822560.1; XM_001822508.2.
DR   ProteinModelPortal; Q2UAI8; -.
DR   STRING; 5062.CADAORAP00009499; -.
DR   EnsemblFungi; BAE61427; BAE61427; AO090102000368.
DR   GeneID; 5994605; -.
DR   KEGG; aor:AOR_1_638134; -.
DR   HOGENOM; HOG000235950; -.
DR   KO; K00852; -.
DR   OMA; NADHVIS; -.
DR   OrthoDB; EOG092C3WGL; -.
DR   UniPathway; UPA00916; UER00889.
DR   Proteomes; UP000006564; Chromosome 4.
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   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:UP000006564};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03215};
KW   Kinase {ECO:0000256|HAMAP-Rule:MF_03215,
KW   ECO:0000256|RuleBase:RU003704};
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:UP000006564};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_03215,
KW   ECO:0000256|RuleBase:RU003704}.
FT   DOMAIN        5    377       PfkB. {ECO:0000259|Pfam:PF00294}.
FT   NP_BIND     266    271       ATP. {ECO:0000256|HAMAP-Rule:MF_03215}.
FT   NP_BIND     310    311       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    311    311       Proton acceptor. {ECO:0000256|HAMAP-Rule:
FT                                MF_03215}.
FT   METAL       305    305       Potassium. {ECO:0000256|HAMAP-Rule:
FT                                MF_03215}.
FT   METAL       307    307       Potassium; via carbonyl oxygen.
FT                                {ECO:0000256|HAMAP-Rule:MF_03215}.
FT   METAL       365    365       Potassium; via carbonyl oxygen.
FT                                {ECO:0000256|HAMAP-Rule:MF_03215}.
FT   METAL       368    368       Potassium; via carbonyl oxygen.
FT                                {ECO:0000256|HAMAP-Rule:MF_03215}.
FT   METAL       370    370       Potassium; via carbonyl oxygen.
FT                                {ECO:0000256|HAMAP-Rule:MF_03215}.
FT   METAL       374    374       Potassium. {ECO:0000256|HAMAP-Rule:
FT                                MF_03215}.
FT   BINDING     161    161       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_03215}.
FT   BINDING     221    221       ATP. {ECO:0000256|HAMAP-Rule:MF_03215}.
FT   BINDING     311    311       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_03215}.
SQ   SEQUENCE   381 AA;  40075 MW;  57106136ED55AEB7 CRC64;
     MAPTIRVVGS LNADMVSVTP RFPEAGETIT SSSYFISAGG KGANQAVACG RLSRARSASS
     TSSGKGSVKV EMVGAVGGLD GHFDALLKPT LEKSGVDTSR VKIVEDAYTG VAVIIVDSSA
     GGENRILFSP GANYQGMQPE PSVLGMAMAA PVPDVIVMQG EIPVDSVIGI LREIRAWKTK
     NRAEGKRGIE AGPDVMFNPA PAPPGGLPED VYAAVDHFIM NETEAELMTP PAEQLLKVVP
     DAEGLSGNDK VARYFHQLGV TYVLITLGSK GVWYSATDAG TSGPADGVNR FTNQIPAAKV
     SRVLDTTAAG DTFVGAYAVG VARWREQRRA DGKAGQDLTS EEKPVRYQKV MDDAMGLATQ
     ASARCVERQG AMDSIPWEDE I
//
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