ID A0A0B7N3L7_9FUNG Unreviewed; 320 AA.
AC A0A0B7N3L7;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=ribose-phosphate diphosphokinase {ECO:0000256|ARBA:ARBA00013247};
DE EC=2.7.6.1 {ECO:0000256|ARBA:ARBA00013247};
GN Name=PARPA_03645.1 scaffold 9253 {ECO:0000313|EMBL:CEP10028.1};
OS Parasitella parasitica.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Mucorineae; Mucoraceae; Parasitella.
OX NCBI_TaxID=35722 {ECO:0000313|EMBL:CEP10028.1, ECO:0000313|Proteomes:UP000054107};
RN [1] {ECO:0000313|EMBL:CEP10028.1, ECO:0000313|Proteomes:UP000054107}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 412.66 {ECO:0000313|EMBL:CEP10028.1,
RC ECO:0000313|Proteomes:UP000054107};
RA Ellenberger Sabrina;
RL Submitted (SEP-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; LN723087; CEP10028.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0B7N3L7; -.
DR STRING; 35722.A0A0B7N3L7; -.
DR OrthoDB; 276387at2759; -.
DR Proteomes; UP000054107; Unassembled WGS sequence.
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; 2.
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 Reference proteome {ECO:0000313|Proteomes:UP000054107};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 6..122
FT /note="Ribose-phosphate pyrophosphokinase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF13793"
SQ SEQUENCE 320 AA; 34877 MW; 216B9FBD2F0635CB CRC64;
MSDNAIKIFT GNSHPELAKL VAKRIGIDLA KAVVMKYSNQ ETSVTVGESV RDEDVFIIQS
GCGEINDNLM ELLILINACK TASARRITAV IPCFPYARQD KKDKSRAPIT AKLTANMLTV
AGANHVITMD LHASQIQGFF NIPVDNLYCE PSMIKYIRTK IPDWKNAIIV SPDAGGAKRA
TSIADRLELD FALIHKERKR ANEVSRMVLV GDVKGKIAIL VDDMADTCGT LGLAAKTLME
NGAVKVYAIV AHGILSGKAI KVINESVIEK LVVTNTIPHQ DKMDICPKLD VIDISPTLAE
AIRRTHNGES VSYLFSHAPE
//
