ID A0A1M7MIZ7_9ACTN Unreviewed; 287 AA.
AC A0A1M7MIZ7;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=Ribokinase {ECO:0000256|ARBA:ARBA00012035, ECO:0000256|HAMAP-Rule:MF_01987};
DE Short=RK {ECO:0000256|HAMAP-Rule:MF_01987};
DE EC=2.7.1.15 {ECO:0000256|ARBA:ARBA00012035, ECO:0000256|HAMAP-Rule:MF_01987};
GN Name=rbsK {ECO:0000256|HAMAP-Rule:MF_01987};
GN ORFNames=SAMN05443668_102145 {ECO:0000313|EMBL:SHM90922.1};
OS Cryptosporangium aurantiacum.
OC Bacteria; Actinomycetota; Actinomycetes; Cryptosporangiales;
OC Cryptosporangiaceae; Cryptosporangium.
OX NCBI_TaxID=134849 {ECO:0000313|EMBL:SHM90922.1, ECO:0000313|Proteomes:UP000184440};
RN [1] {ECO:0000313|EMBL:SHM90922.1, ECO:0000313|Proteomes:UP000184440}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 46144 {ECO:0000313|EMBL:SHM90922.1,
RC ECO:0000313|Proteomes:UP000184440};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the phosphorylation of ribose at O-5 in a reaction
CC requiring ATP and magnesium. The resulting D-ribose-5-phosphate can
CC then be used either for sythesis of nucleotides, histidine, and
CC tryptophan, or as a component of the pentose phosphate pathway.
CC {ECO:0000256|HAMAP-Rule:MF_01987}.
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 ECO:0000256|HAMAP-Rule:MF_01987};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01987};
CC Note=Requires a divalent cation, most likely magnesium in vivo, as an
CC electrophilic catalyst to aid phosphoryl group transfer. It is the
CC chelate of the metal and the nucleotide that is the actual substrate.
CC {ECO:0000256|HAMAP-Rule:MF_01987};
CC -!- ACTIVITY REGULATION: Activated by a monovalent cation that binds near,
CC but not in, the active site. The most likely occupant of the site in
CC vivo is potassium. Ion binding induces a conformational change that may
CC alter substrate affinity. {ECO:0000256|HAMAP-Rule:MF_01987}.
CC -!- PATHWAY: Carbohydrate metabolism; D-ribose degradation; D-ribose 5-
CC phosphate from beta-D-ribopyranose: step 2/2. {ECO:0000256|HAMAP-
CC Rule:MF_01987}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01987}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01987}.
CC -!- SIMILARITY: Belongs to the carbohydrate kinase PfkB family. Ribokinase
CC subfamily. {ECO:0000256|HAMAP-Rule:MF_01987}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_01987}.
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DR EMBL; FRCS01000002; SHM90922.1; -; Genomic_DNA.
DR RefSeq; WP_073253345.1; NZ_FRCS01000002.1.
DR AlphaFoldDB; A0A1M7MIZ7; -.
DR STRING; 134849.SAMN05443668_102145; -.
DR OrthoDB; 9775849at2; -.
DR UniPathway; UPA00916; UER00889.
DR Proteomes; UP000184440; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; 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 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 3: Inferred from homology;
KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_01987};
KW Carbohydrate metabolism {ECO:0000256|HAMAP-Rule:MF_01987};
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01987};
KW Kinase {ECO:0000256|HAMAP-Rule:MF_01987, ECO:0000313|EMBL:SHM90922.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_01987};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_01987}; Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01987};
KW Potassium {ECO:0000256|ARBA:ARBA00022958, ECO:0000256|HAMAP-Rule:MF_01987};
KW Reference proteome {ECO:0000313|Proteomes:UP000184440};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_01987}.
FT DOMAIN 5..282
FT /note="Carbohydrate kinase PfkB"
FT /evidence="ECO:0000259|Pfam:PF00294"
FT REGION 26..46
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 240
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01987"
FT BINDING 13..15
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01987"
FT BINDING 41..45
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01987"
FT BINDING 135
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01987"
FT BINDING 176
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01987"
FT BINDING 208..213
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01987"
FT BINDING 234
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01987"
FT BINDING 236
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01987"
FT BINDING 239..240
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01987"
FT BINDING 240
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01987"
FT BINDING 270
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01987"
FT BINDING 273
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01987"
FT BINDING 275
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01987"
FT BINDING 279
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01987"
SQ SEQUENCE 287 AA; 28954 MW; B3AE1DE9A0F68FEC CRC64;
MSSFEIVVVG SLNVDVTVDV PQAPEAGQTL LGGDARRSGG GKGGNQAVAA ARLGRSTAMV
GAVGASDGEF LLSLLRGENI DISGVRQVEA PTGQAFVFVD TEGDSTIVVS PGANDHVEVD
RELVAAARCV LLQQEVPAAV VEEAASVANG IVVLNPAPAR PVAPSLLANV DVLVPNRGEL
LGLAGGVDRG DLVQLAQNLG TRGPVVVTLG AQGCLVVEAE RSTRVPAEQV KAVDATAAGD
SFCAAIADAL LDGADIVEAA RWATRVAAVT VTRQGAMASL PTKDELA
//