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Database: UniProt
Entry: C4R2M4_KOMPG
LinkDB: C4R2M4_KOMPG
Original site: C4R2M4_KOMPG 
ID   C4R2M4_KOMPG            Unreviewed;       421 AA.
AC   C4R2M4;
DT   07-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   07-JUL-2009, sequence version 1.
DT   27-MAR-2024, entry version 83.
DE   RecName: Full=ribose-phosphate diphosphokinase {ECO:0000256|ARBA:ARBA00013247};
DE            EC=2.7.6.1 {ECO:0000256|ARBA:ARBA00013247};
GN   OrderedLocusNames=PAS_chr2-2_0174 {ECO:0000313|EMBL:CAY69748.1};
OS   Komagataella phaffii (strain GS115 / ATCC 20864) (Yeast) (Pichia pastoris).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Phaffomycetaceae; Komagataella.
OX   NCBI_TaxID=644223 {ECO:0000313|EMBL:CAY69748.1, ECO:0000313|Proteomes:UP000000314};
RN   [1] {ECO:0000313|EMBL:CAY69748.1, ECO:0000313|Proteomes:UP000000314}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GS115 / ATCC 20864 {ECO:0000313|Proteomes:UP000000314};
RX   PubMed=19465926; DOI=10.1038/nbt.1544;
RA   De Schutter K., Lin Y.C., Tiels P., Van Hecke A., Glinka S.,
RA   Weber-Lehmann J., Rouze P., Van de Peer Y., Callewaert N.;
RT   "Genome sequence of the recombinant protein production host Pichia
RT   pastoris.";
RL   Nat. Biotechnol. 27:561-566(2009).
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; FN392320; CAY69748.1; -; Genomic_DNA.
DR   RefSeq; XP_002492028.1; XM_002491983.1.
DR   AlphaFoldDB; C4R2M4; -.
DR   SMR; C4R2M4; -.
DR   STRING; 644223.C4R2M4; -.
DR   EnsemblFungi; CAY69748; CAY69748; PAS_chr2-2_0174.
DR   GeneID; 8198750; -.
DR   KEGG; ppa:PAS_chr2-2_0174; -.
DR   eggNOG; KOG1448; Eukaryota.
DR   HOGENOM; CLU_033546_0_1_1; -.
DR   InParanoid; C4R2M4; -.
DR   OMA; MMLVGDI; -.
DR   OrthoDB; 276387at2759; -.
DR   Proteomes; UP000000314; Chromosome 2.
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; -; 3.
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; RIBOSE-PHOSPHATE DIPHOSPHOKINASE FAMILY MEMBER; 1.
DR   PANTHER; PTHR10210:SF36; RIBOSE-PHOSPHATE PYROPHOSPHOKINASE 5; 1.
DR   Pfam; PF14572; Pribosyl_synth; 1.
DR   Pfam; PF13793; Pribosyltran_N; 1.
DR   SMART; SM01400; Pribosyltran_N; 1.
DR   SUPFAM; SSF53271; PRTase-like; 2.
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   Reference proteome {ECO:0000313|Proteomes:UP000000314};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          5..97
FT                   /note="Ribose-phosphate pyrophosphokinase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF13793"
FT   REGION          103..173
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        110..173
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   421 AA;  45591 MW;  232DA34A14AE08F8 CRC64;
     MRDLIVLSGS SNPQLTARIC KQLGVPKGEV ISTKFANGET SVTVVDSVRE KDVYIVQSGC
     GHTNDNFFEL LIMISACKTA SAKRVTAVLP LFPYSRQPDL PYNKNGYSVN GKREFDSSPG
     TPIPNSTASE STDYLTSSVV KDTSNDMRKS TLINQPVPTP TASSSSSLLN NNNTDDSPTY
     KEWIAQSGTL VANLLTTAGA DHIITMDLHD PQFQGFFDIP VDNLYSKPLL QHYIANNIPD
     FQNAVVVSPD SGGAKRAIAV ADQLGMSFAL IHKERRYRKL INPTTLDQSL LISSTITPSN
     SNKVIATTML VGDVAGKVCV LIDDLVDTSY TITRAASLLK DQGATYVYAL VTHGVFSGDA
     INRINDSAID KIITTTSTPQ DGHAKQLGTK LEVLDVSRIL AEAIRRINNG ESVSMLFEHG
     W
//
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