ID   W6MHC1_9ASCO            Unreviewed;       325 AA.
AC   W6MHC1;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   RecName: Full=ribose-phosphate diphosphokinase {ECO:0000256|ARBA:ARBA00013247};
DE            EC=2.7.6.1 {ECO:0000256|ARBA:ARBA00013247};
GN   ORFNames=KUCA_T00001589001 {ECO:0000313|EMBL:CDK25619.1};
OS   Kuraishia capsulata CBS 1993.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetales incertae sedis; Kuraishia.
OX   NCBI_TaxID=1382522 {ECO:0000313|EMBL:CDK25619.1};
RN   [1] {ECO:0000313|EMBL:CDK25619.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=CBS 1993 {ECO:0000313|EMBL:CDK25619.1};
RA   Genoscope - CEA;
RL   Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:CDK25619.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=CBS 1993 {ECO:0000313|EMBL:CDK25619.1};
RA   Morales L., Noel B., Porcel B., Marcet-Houben M., Hullo M-F., Sacerdot C.,
RA   Tekaia F., Leh-Louis V., Despons L., Khanna V., Aury J-M., Barbe V.,
RA   Couloux A., Labadie K., Pelletier E., Souciet J-L., Boekhout T.,
RA   Gabaldon T., Wincker P., Dujon B.;
RT   "Complete DNA sequence of /Kuraishia capsulata/ illustrates novel genomic
RT   features among budding yeasts (/Saccharomycotina/).";
RL   Submitted (FEB-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + D-ribose 5-phosphate = 5-phospho-alpha-D-ribose 1-
CC         diphosphate + AMP + H(+); Xref=Rhea:RHEA:15609, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:58017, ChEBI:CHEBI:78346,
CC         ChEBI:CHEBI:456215; EC=2.7.6.1;
CC         Evidence={ECO:0000256|ARBA:ARBA00000179};
CC   -!- SIMILARITY: Belongs to the ribose-phosphate pyrophosphokinase family.
CC       {ECO:0000256|ARBA:ARBA00006478}.
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DR   EMBL; HG793126; CDK25619.1; -; Genomic_DNA.
DR   AlphaFoldDB; W6MHC1; -.
DR   STRING; 1382522.W6MHC1; -.
DR   HOGENOM; CLU_033546_4_0_1; -.
DR   OrthoDB; 276387at2759; -.
DR   GO; GO:0002189; C:ribose phosphate diphosphokinase complex; IEA:UniProt.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0004749; F:ribose phosphate diphosphokinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006015; P:5-phosphoribose 1-diphosphate biosynthetic process; IEA:UniProt.
DR   GO; GO:0031505; P:fungal-type cell wall organization; IEA:UniProt.
DR   GO; GO:0009165; P:nucleotide biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0009156; P:ribonucleoside monophosphate biosynthetic process; IEA:InterPro.
DR   CDD; cd06223; PRTases_typeI; 1.
DR   Gene3D; 3.40.50.2020; -; 2.
DR   InterPro; IPR000842; PRib_PP_synth_CS.
DR   InterPro; IPR029099; Pribosyltran_N.
DR   InterPro; IPR000836; PRibTrfase_dom.
DR   InterPro; IPR029057; PRTase-like.
DR   InterPro; IPR005946; Rib-P_diPkinase.
DR   NCBIfam; TIGR01251; ribP_PPkin; 1.
DR   PANTHER; PTHR10210:SF32; RIBOSE-PHOSPHATE DIPHOSPHOKINASE; 1.
DR   PANTHER; PTHR10210; RIBOSE-PHOSPHATE DIPHOSPHOKINASE FAMILY MEMBER; 1.
DR   Pfam; PF14572; Pribosyl_synth; 1.
DR   Pfam; PF13793; Pribosyltran_N; 1.
DR   SMART; SM01400; Pribosyltran_N; 1.
DR   SUPFAM; SSF53271; PRTase-like; 1.
DR   PROSITE; PS00114; PRPP_SYNTHASE; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleotide biosynthesis {ECO:0000256|ARBA:ARBA00022727};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          10..128
FT                   /note="Ribose-phosphate pyrophosphokinase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF13793"
SQ   SEQUENCE   325 AA;  35408 MW;  FA4A20770BF74C38 CRC64;
     MSVQKSPNQI KLLSGNSHLE LTGLIAGKLG IPISKVSAFQ YTNQETAVII GESVRDEDVY
     IVQTGTGVDN INDYVMELLI MIHACKAASA RRITVVMPCF PYARQDKKDK SRAPITAKLI
     ANLLTTAGCH HLVTMDLHAS QIQGFFKIPV DNLYAEPNVL KYIRESIDYR NAIIVSPDAG
     GAKRVAAIAD KLDTSFALIH KERARANEIS RMVLVGDVTD KTCILIDDMA DTCGTLCKAS
     DILLDNGANE VIAIVTHGIF SSDAIEKINK SSLKKIICTN SLPLSSKAEV CGRLETIDIS
     GTLAEAIRRQ HYGESVSYLF NNVPM
//