ID A0A1S3WMH4_ERIEU Unreviewed; 294 AA.
AC A0A1S3WMH4;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Ribokinase {ECO:0000256|ARBA:ARBA00016943, ECO:0000256|HAMAP-Rule:MF_03215};
DE Short=RK {ECO:0000256|HAMAP-Rule:MF_03215};
DE EC=2.7.1.15 {ECO:0000256|ARBA:ARBA00012035, ECO:0000256|HAMAP-Rule:MF_03215};
GN Name=RBKS {ECO:0000256|HAMAP-Rule:MF_03215,
GN ECO:0000313|RefSeq:XP_016047339.1};
OS Erinaceus europaeus (Western European hedgehog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Eulipotyphla; Erinaceidae; Erinaceinae;
OC Erinaceus.
OX NCBI_TaxID=9365 {ECO:0000313|Proteomes:UP000079721, ECO:0000313|RefSeq:XP_016047339.1};
RN [1] {ECO:0000313|RefSeq:XP_016047339.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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_03215}.
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_03215};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_03215};
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_03215};
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_03215}.
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_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. Ribokinase
CC subfamily. {ECO:0000256|HAMAP-Rule:MF_03215}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_03215}.
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DR RefSeq; XP_016047339.1; XM_016191853.1.
DR AlphaFoldDB; A0A1S3WMH4; -.
DR CTD; 64080; -.
DR OrthoDB; 1217765at2759; -.
DR UniPathway; UPA00916; UER00889.
DR Proteomes; UP000079721; Unplaced.
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 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_03215};
KW Carbohydrate metabolism {ECO:0000256|HAMAP-Rule:MF_03215};
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03215};
KW Kinase {ECO:0000256|HAMAP-Rule:MF_03215};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_03215};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_03215}; Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_03215};
KW Nucleus {ECO:0000256|HAMAP-Rule:MF_03215};
KW Potassium {ECO:0000256|ARBA:ARBA00022958, ECO:0000256|HAMAP-Rule:MF_03215};
KW Reference proteome {ECO:0000313|Proteomes:UP000079721};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_03215}.
FT DOMAIN 17..265
FT /note="Carbohydrate kinase PfkB"
FT /evidence="ECO:0000259|Pfam:PF00294"
FT ACT_SITE 263
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03215"
FT BINDING 25..27
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03215"
FT BINDING 53..57
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03215"
FT BINDING 154
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03215"
FT BINDING 199
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03215"
FT BINDING 235..240
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03215"
FT BINDING 256
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03215"
FT BINDING 259
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03215"
FT BINDING 263
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03215"
FT BINDING 275
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03215"
SQ SEQUENCE 294 AA; 30689 MW; 24DB5E537337AE59 CRC64;
MAASGEPCRP GRGEAAAVVV VGSCMTDLVS LAHRLPKTGE TIHGHKFFIG FGGKGANQCV
QAARLGAKTS LVCKVGKDSF GNNYIENLKQ NDISTEFAYQ TKDAATGTAS IIVNNEGQNI
IVIVAGANLL LNTEDLRGAV SVISRARVML CQLEISPATS LGALAMARSS GVKTLFNPAP
AIADLDPQFY TLSDVFCCNE SEAEILTGLT VGSPADAGKA ALMLMGRGCQ VVIVTLGAGG
CVMLSQTEPT PKHIPTETVK AVDTTPSRLV FSVYSCNSRG PAHVTVESLY NRKP
//
