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Ribokinase (RK) (EC 2.7.1.15)

 A0A084G1H3_9PEZI        Unreviewed;       417 AA.
A0A084G1H3;
29-OCT-2014, integrated into UniProtKB/TrEMBL.
29-OCT-2014, sequence version 1.
27-SEP-2017, entry version 12.
RecName: Full=Ribokinase {ECO:0000256|HAMAP-Rule:MF_03215};
Short=RK {ECO:0000256|HAMAP-Rule:MF_03215};
EC=2.7.1.15 {ECO:0000256|HAMAP-Rule:MF_03215};
ORFNames=SAPIO_CDS7267 {ECO:0000313|EMBL:KEZ41185.1};
Scedosporium apiospermum.
Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
Sordariomycetes; Hypocreomycetidae; Microascales; Microascaceae;
Scedosporium.
NCBI_TaxID=563466 {ECO:0000313|EMBL:KEZ41185.1, ECO:0000313|Proteomes:UP000028545};
[1] {ECO:0000313|EMBL:KEZ41185.1, ECO:0000313|Proteomes:UP000028545}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=IHEM 14462 {ECO:0000313|EMBL:KEZ41185.1,
ECO:0000313|Proteomes:UP000028545};
Vandeputte P., Rechenmann M., Bouchara J.-P.;
Submitted (JUN-2014) 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_03215}.
-!- CATALYTIC ACTIVITY: ATP + D-ribose = ADP + D-ribose 5-phosphate.
{ECO:0000256|HAMAP-Rule:MF_03215}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000256|HAMAP-Rule:MF_03215};
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_03215};
-!- 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_03215}.
-!- PATHWAY: Carbohydrate metabolism; D-ribose degradation; D-ribose
5-phosphate from beta-D-ribopyranose: step 2/2.
{ECO:0000256|HAMAP-Rule:MF_03215}.
-!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_03215}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03215}.
Nucleus {ECO:0000256|HAMAP-Rule:MF_03215}.
-!- SIMILARITY: Belongs to the carbohydrate kinase PfkB family.
Ribokinase subfamily. {ECO:0000256|HAMAP-Rule:MF_03215}.
-!- CAUTION: Lacks conserved residue(s) required for the propagation
of feature annotation. {ECO:0000256|HAMAP-Rule:MF_03215}.
-!- CAUTION: The sequence shown here is derived from an
EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
preliminary data. {ECO:0000313|EMBL:KEZ41185.1}.
-----------------------------------------------------------------------
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EMBL; JOWA01000110; KEZ41185.1; -; Genomic_DNA.
RefSeq; XP_016640984.1; XM_016789157.1.
EnsemblFungi; KEZ41185; KEZ41185; SAPIO_CDS7267.
GeneID; 27726339; -.
UniPathway; UPA00916; UER00889.
Proteomes; UP000028545; Unassembled WGS sequence.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0005634; C:nucleus; 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.
PROSITE; PS00584; PFKB_KINASES_2; 1.
3: Inferred from homology;
ATP-binding {ECO:0000256|HAMAP-Rule:MF_03215};
Carbohydrate metabolism {ECO:0000256|HAMAP-Rule:MF_03215};
Complete proteome {ECO:0000313|Proteomes:UP000028545};
Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03215};
Kinase {ECO:0000256|HAMAP-Rule:MF_03215,
ECO:0000256|RuleBase:RU003704, ECO:0000313|EMBL:KEZ41185.1};
Magnesium {ECO:0000256|HAMAP-Rule:MF_03215};
Metal-binding {ECO:0000256|HAMAP-Rule:MF_03215};
Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_03215};
Nucleus {ECO:0000256|HAMAP-Rule:MF_03215};
Potassium {ECO:0000256|HAMAP-Rule:MF_03215};
Reference proteome {ECO:0000313|Proteomes:UP000028545};
Transferase {ECO:0000256|HAMAP-Rule:MF_03215,
ECO:0000256|RuleBase:RU003704, ECO:0000313|EMBL:KEZ41185.1}.
DOMAIN 17 330 PfkB. {ECO:0000259|Pfam:PF00294}.
NP_BIND 251 256 ATP. {ECO:0000256|HAMAP-Rule:MF_03215}.
NP_BIND 284 285 ATP. {ECO:0000256|HAMAP-Rule:MF_03215}.
REGION 25 27 Substrate binding. {ECO:0000256|HAMAP-
Rule:MF_03215}.
REGION 53 57 Substrate binding. {ECO:0000256|HAMAP-
Rule:MF_03215}.
ACT_SITE 285 285 Proton acceptor. {ECO:0000256|HAMAP-
Rule:MF_03215}.
METAL 279 279 Potassium. {ECO:0000256|HAMAP-
Rule:MF_03215}.
METAL 281 281 Potassium; via carbonyl oxygen.
{ECO:0000256|HAMAP-Rule:MF_03215}.
METAL 318 318 Potassium; via carbonyl oxygen.
{ECO:0000256|HAMAP-Rule:MF_03215}.
METAL 321 321 Potassium; via carbonyl oxygen.
{ECO:0000256|HAMAP-Rule:MF_03215}.
METAL 323 323 Potassium; via carbonyl oxygen.
{ECO:0000256|HAMAP-Rule:MF_03215}.
METAL 327 327 Potassium. {ECO:0000256|HAMAP-
Rule:MF_03215}.
BINDING 167 167 Substrate. {ECO:0000256|HAMAP-
Rule:MF_03215}.
BINDING 211 211 ATP. {ECO:0000256|HAMAP-Rule:MF_03215}.
BINDING 285 285 Substrate. {ECO:0000256|HAMAP-
Rule:MF_03215}.
SEQUENCE 417 AA; 44494 MW; A553CB3A60BF6FC8 CRC64;
MAAEASQAEN ATPPLPQITV IGSLNMDLTS YVSRVPRAGE TIMGDHFSTG TGGKGANQAV
ACSKLAHVSP GHAPLERGPL AKVKMVGAVG GDFFGQELIS ALESQSVDCS NVKRIEGEST
GVAMIMVESS GENRIIVTLN ANKKLAPADI GDTIPGDKPD LVILQLELDL KTVLHTISVA
KKQGVPILLN PSPVRKLPED VYQGLDHLIV NEMECRMLLG HANPARELTQ EDMRKAGFSF
VKKGVKNVVI TLGPRGAFYF NHQHEFGFVP AQFHGDVVDT TGAGDTFTGA YALGVVRNKE
NFNIAFALED GAHAAAWTVT ARGALSSIPH LERLTLPNLR FDHSRRDELL AAIRAAKGDS
IGISKEDAAM SVDKDSGDSP SNWALSEDDL DPVPEKRPSE NGDGDERPAK RHCEDGA


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