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Database: UniProt
Entry: A0A137Q1W3_9AGAR
LinkDB: A0A137Q1W3_9AGAR
Original site: A0A137Q1W3_9AGAR 
ID   A0A137Q1W3_9AGAR        Unreviewed;       320 AA.
AC   A0A137Q1W3;
DT   11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT   11-MAY-2016, sequence version 1.
DT   27-SEP-2017, entry version 7.
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=AN958_05879 {ECO:0000313|EMBL:KXN81190.1};
OS   Leucoagaricus sp. SymC.cos.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina;
OC   Agaricomycetes; Agaricomycetidae; Agaricales; Agaricaceae;
OC   Leucoagaricus.
OX   NCBI_TaxID=1714833 {ECO:0000313|EMBL:KXN81190.1, ECO:0000313|Proteomes:UP000070249};
RN   [1] {ECO:0000313|EMBL:KXN81190.1, ECO:0000313|Proteomes:UP000070249}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SymC.cos {ECO:0000313|EMBL:KXN81190.1,
RC   ECO:0000313|Proteomes:UP000070249};
RA   Hu H.;
RT   "Leucoagaricus sp. SymC.cos WGS genome.";
RL   Submitted (JAN-2016) 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; KQ963472; KXN81190.1; -; Genomic_DNA.
DR   UniPathway; UPA00916; UER00889.
DR   Proteomes; UP000070249; 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; 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.
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:UP000070249};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03215};
KW   Kinase {ECO:0000256|HAMAP-Rule:MF_03215, ECO:0000313|EMBL:KXN81190.1};
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:UP000070249};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_03215}.
FT   DOMAIN        5    307       PfkB. {ECO:0000259|Pfam:PF00294}.
FT   NP_BIND     223    228       ATP. {ECO:0000256|HAMAP-Rule:MF_03215}.
FT   NP_BIND     257    258       ATP. {ECO:0000256|HAMAP-Rule:MF_03215}.
FT   REGION       11     13       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_03215}.
FT   REGION       39     43       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_03215}.
FT   ACT_SITE    258    258       Proton acceptor. {ECO:0000256|HAMAP-Rule:
FT                                MF_03215}.
FT   METAL       252    252       Potassium. {ECO:0000256|HAMAP-Rule:
FT                                MF_03215}.
FT   METAL       254    254       Potassium; via carbonyl oxygen.
FT                                {ECO:0000256|HAMAP-Rule:MF_03215}.
FT   METAL       295    295       Potassium; via carbonyl oxygen.
FT                                {ECO:0000256|HAMAP-Rule:MF_03215}.
FT   METAL       298    298       Potassium; via carbonyl oxygen.
FT                                {ECO:0000256|HAMAP-Rule:MF_03215}.
FT   METAL       300    300       Potassium; via carbonyl oxygen.
FT                                {ECO:0000256|HAMAP-Rule:MF_03215}.
FT   METAL       304    304       Potassium. {ECO:0000256|HAMAP-Rule:
FT                                MF_03215}.
FT   BINDING     137    137       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_03215}.
FT   BINDING     182    182       ATP. {ECO:0000256|HAMAP-Rule:MF_03215}.
FT   BINDING     258    258       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_03215}.
SQ   SEQUENCE   320 AA;  34492 MW;  9D084B3F09D8BFC8 CRC64;
     MVHCLVRGSI NLDEYYYVPH ISQPGETISS HGFQQRMGGK GFNQAVAVAL ATGGGSQGKV
     SFYGTVGDDE AGKMLLYGFG EGVKLVKTKA TGRAIIQVGD DGENSIVLFP GANHSELIED
     QEKPWPMGTT HLLLQNEISL KSTLRAIESG TELITILNPS PMFTDEEIVQ FPWNKIDWLI
     VNHLEARSLL KALTKAIPPE GAKEMLDKLS KESVLNSIRI ICTLGANGVL ASVPGLPIVF
     VPVAPLQGPV VDTTGAGDTF TGYFVAELMS LGREVEQEAD IVRLLRVATR AAAMCVERAG
     TVDSVPTVDE VERRFGISRE
//
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