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Database: UniProt
Entry: A0A0J1FY02_9FIRM
LinkDB: A0A0J1FY02_9FIRM
Original site: A0A0J1FY02_9FIRM 
ID   A0A0J1FY02_9FIRM        Unreviewed;       303 AA.
AC   A0A0J1FY02;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   RecName: Full=ribokinase {ECO:0000256|ARBA:ARBA00012035};
DE            EC=2.7.1.15 {ECO:0000256|ARBA:ARBA00012035};
GN   ORFNames=RHS_6014 {ECO:0000313|EMBL:KLU68167.1};
OS   Robinsoniella sp. RHS.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC   Robinsoniella.
OX   NCBI_TaxID=1504536 {ECO:0000313|EMBL:KLU68167.1, ECO:0000313|Proteomes:UP000036477};
RN   [1] {ECO:0000313|EMBL:KLU68167.1, ECO:0000313|Proteomes:UP000036477}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RHS {ECO:0000313|EMBL:KLU68167.1};
RX   PubMed=25284151; DOI=10.1016/j.cell.2014.09.008;
RA   Seedorf H., Griffin N.W., Ridaura V.K., Reyes A., Cheng J., Rey F.E.,
RA   Smith M.I., Simon G.M., Scheffrahn R.H., Woebken D., Spormann A.M.,
RA   Van Treuren W., Ursell L.K., Pirrung M., Robbins-Pianka A., Cantarel B.L.,
RA   Lombard V., Henrissat B., Knight R., Gordon J.I.;
RT   "Bacteria from diverse habitats colonize and compete in the mouse gut.";
RL   Cell 159:253-266(2014).
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   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KLU68167.1}.
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DR   EMBL; JNGB01000223; KLU68167.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0J1FY02; -.
DR   PATRIC; fig|1504536.3.peg.3203; -.
DR   Proteomes; UP000036477; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004747; F:ribokinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006014; P:D-ribose metabolic process; IEA:InterPro.
DR   CDD; cd01174; ribokinase; 1.
DR   Gene3D; 3.40.1190.20; -; 1.
DR   InterPro; IPR011877; D_ribokin.
DR   InterPro; IPR011611; PfkB_dom.
DR   InterPro; IPR002139; Ribo/fructo_kinase.
DR   InterPro; IPR029056; Ribokinase-like.
DR   PANTHER; PTHR10584:SF166; RIBOKINASE; 1.
DR   PANTHER; PTHR10584; SUGAR KINASE; 1.
DR   Pfam; PF00294; PfkB; 1.
DR   PRINTS; PR00990; RIBOKINASE.
DR   SUPFAM; SSF53613; Ribokinase-like; 1.
PE   4: Predicted;
KW   Kinase {ECO:0000256|ARBA:ARBA00022777};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Potassium {ECO:0000256|ARBA:ARBA00022958};
KW   Reference proteome {ECO:0000313|Proteomes:UP000036477};
KW   Transferase {ECO:0000256|ARBA:ARBA00022777}.
FT   DOMAIN          2..280
FT                   /note="Carbohydrate kinase PfkB"
FT                   /evidence="ECO:0000259|Pfam:PF00294"
SQ   SEQUENCE   303 AA;  32463 MW;  D84AB5B0A28C3F70 CRC64;
     MVGGINIDIT LNLDELPHSG KAVSTSRSTT FPGGKGVNQA IGAARLGHPV SLIGKVGTDY
     DSALIYSAMK ENGVDIQGIG RDLSASTGKA YIHVQNDGES TISILTGANQ NVTAQDIINN
     ERLFENAGYC LLPTEIPDFT IETAAQTAKK YGARTILKPT LLDRIPDSIL KNIDIFIPNQ
     IEMISLCPGI RTLPEQADCF LSKGVSTVII TLGHRGCYVK SNGLERYYPA VGFVSVDNTG
     AADAFISALA SYLLYGYSLD EAIRIASYAA GFCTSRQGVV PALIDRSSLE TYIKKVEPDL
     IHR
//
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