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Ribokinase (RK) (EC 2.7.1.15)

 A0A1B4X1N5_9PSED        Unreviewed;       305 AA.
A0A1B4X1N5;
02-NOV-2016, integrated into UniProtKB/TrEMBL.
02-NOV-2016, sequence version 1.
25-APR-2018, entry version 8.
RecName: Full=Ribokinase {ECO:0000256|HAMAP-Rule:MF_01987};
Short=RK {ECO:0000256|HAMAP-Rule:MF_01987};
EC=2.7.1.15 {ECO:0000256|HAMAP-Rule:MF_01987};
Name=rbsK {ECO:0000256|HAMAP-Rule:MF_01987};
ORFNames=LAB08_3392 {ECO:0000313|EMBL:BAV28662.1};
Pseudomonas sp. LAB-08.
Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
Pseudomonadaceae; Pseudomonas.
NCBI_TaxID=143813 {ECO:0000313|EMBL:BAV28662.1, ECO:0000313|Proteomes:UP000218595};
[1] {ECO:0000313|EMBL:BAV28662.1, ECO:0000313|Proteomes:UP000218595}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Suzuki K., Fatma A., Inuzuka Y., Tashiro Y., Futamata H.;
"Draft genome sequence of Pseudomonassp. LAB-08 isolated from TCE
contaminated aquifer soil.";
Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
-!- FUNCTION: Catalyzes the phosphorylation of ribose at O-5 in a
reaction requiring ATP and magnesium. The resulting D-ribose-5-
phosphate can then be used either for sythesis of nucleotides,
histidine, and tryptophan, or as a component of the pentose
phosphate pathway. {ECO:0000256|HAMAP-Rule:MF_01987}.
-!- CATALYTIC ACTIVITY: ATP + D-ribose = ADP + D-ribose 5-phosphate.
{ECO:0000256|HAMAP-Rule:MF_01987}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000256|HAMAP-Rule:MF_01987};
Note=Requires a divalent cation, most likely magnesium in vivo, as
an electrophilic catalyst to aid phosphoryl group transfer. It is
the chelate of the metal and the nucleotide that is the actual
substrate. {ECO:0000256|HAMAP-Rule:MF_01987};
-!- ENZYME REGULATION: Activated by a monovalent cation that binds
near, but not in, the active site. The most likely occupant of the
site in vivo is potassium. Ion binding induces a conformational
change that may alter substrate affinity. {ECO:0000256|HAMAP-
Rule:MF_01987}.
-!- PATHWAY: Carbohydrate metabolism; D-ribose degradation; D-ribose
5-phosphate from beta-D-ribopyranose: step 2/2.
{ECO:0000256|HAMAP-Rule:MF_01987}.
-!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01987}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01987}.
-!- SIMILARITY: Belongs to the carbohydrate kinase PfkB family.
Ribokinase subfamily. {ECO:0000256|HAMAP-Rule:MF_01987}.
-!- CAUTION: Lacks conserved residue(s) required for the propagation
of feature annotation. {ECO:0000256|HAMAP-Rule:MF_01987}.
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EMBL; AP017423; BAV28662.1; -; Genomic_DNA.
UniPathway; UPA00916; UER00889.
Proteomes; UP000218595; Chromosome.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0004747; F:ribokinase activity; IEA:UniProtKB-UniRule.
GO; GO:0019303; P:D-ribose catabolic process; IEA:UniProtKB-UniRule.
CDD; cd01174; ribokinase; 1.
Gene3D; 3.40.1190.20; -; 1.
HAMAP; MF_01987; Ribokinase; 1.
InterPro; IPR002173; Carboh/pur_kinase_PfkB_CS.
InterPro; IPR011877; D_ribokin.
InterPro; IPR011611; PfkB_dom.
InterPro; IPR002139; Ribo/fructo_kinase.
InterPro; IPR029056; Ribokinase-like.
Pfam; PF00294; PfkB; 1.
PRINTS; PR00990; RIBOKINASE.
SUPFAM; SSF53613; SSF53613; 1.
TIGRFAMs; TIGR02152; D_ribokin_bact; 1.
PROSITE; PS00584; PFKB_KINASES_2; 1.
3: Inferred from homology;
ATP-binding {ECO:0000256|HAMAP-Rule:MF_01987};
Carbohydrate metabolism {ECO:0000256|HAMAP-Rule:MF_01987};
Complete proteome {ECO:0000313|Proteomes:UP000218595};
Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01987};
Kinase {ECO:0000256|HAMAP-Rule:MF_01987,
ECO:0000256|RuleBase:RU003704, ECO:0000256|SAAS:SAAS00061343,
ECO:0000313|EMBL:BAV28662.1};
Magnesium {ECO:0000256|HAMAP-Rule:MF_01987};
Metal-binding {ECO:0000256|HAMAP-Rule:MF_01987};
Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01987};
Potassium {ECO:0000256|HAMAP-Rule:MF_01987};
Reference proteome {ECO:0000313|Proteomes:UP000218595};
Transferase {ECO:0000256|HAMAP-Rule:MF_01987,
ECO:0000256|RuleBase:RU003704, ECO:0000256|SAAS:SAAS00061343,
ECO:0000313|EMBL:BAV28662.1}.
DOMAIN 3 295 PfkB. {ECO:0000259|Pfam:PF00294}.
NP_BIND 221 226 ATP. {ECO:0000256|HAMAP-Rule:MF_01987}.
NP_BIND 252 253 ATP. {ECO:0000256|HAMAP-Rule:MF_01987}.
REGION 12 14 Substrate binding. {ECO:0000256|HAMAP-
Rule:MF_01987}.
REGION 40 44 Substrate binding. {ECO:0000256|HAMAP-
Rule:MF_01987}.
ACT_SITE 253 253 Proton acceptor. {ECO:0000256|HAMAP-
Rule:MF_01987}.
METAL 247 247 Potassium. {ECO:0000256|HAMAP-
Rule:MF_01987}.
METAL 249 249 Potassium; via carbonyl oxygen.
{ECO:0000256|HAMAP-Rule:MF_01987}.
METAL 283 283 Potassium; via carbonyl oxygen.
{ECO:0000256|HAMAP-Rule:MF_01987}.
METAL 286 286 Potassium; via carbonyl oxygen.
{ECO:0000256|HAMAP-Rule:MF_01987}.
METAL 288 288 Potassium; via carbonyl oxygen.
{ECO:0000256|HAMAP-Rule:MF_01987}.
METAL 292 292 Potassium. {ECO:0000256|HAMAP-
Rule:MF_01987}.
BINDING 140 140 Substrate. {ECO:0000256|HAMAP-
Rule:MF_01987}.
BINDING 185 185 ATP. {ECO:0000256|HAMAP-Rule:MF_01987}.
BINDING 253 253 Substrate. {ECO:0000256|HAMAP-
Rule:MF_01987}.
SEQUENCE 305 AA; 31011 MW; A6F6B01202B12A10 CRC64;
MPAKVVVIGS LNMDLVTRAP RLPQGGETLI GHSFTKVCGG KGANQAVAAA RLGAQVSMVG
CVGRDAYGEE LRAALLAEQV DCQAVSTVDD SSGVALIVVD DNSQNAIVIV AGANGALTPA
VVGCFDSVLQ AADVIICQLE VPDATVGHAL KRSRELGKIV ILNPAPASRP LPANWYENID
YLIPNESEAS TLSGLPVDSR QTAQAAASRL IELGAGKVII TLGAQGSLLA DGQRIEHFPA
PTVKAVDTTA AGDTFVGGFA AALAGGKGEA EAIRFGQVAA ALSVTRAGAQ PSIPTLSEVQ
AFKTP


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