ACL_RS01010

Uniprot: A9NEQ2
Description: uracil phosphoribosyltransferase
EC number: 2.4.2.9
Annotation score: 3 out of 5
Miscellaneous [CC]:
Protein existence: Inferred from homology
Catalytic activity: CATALYTIC ACTIVITY: UMP + diphosphate = uracil + 5-phospho-alpha-D-ribose 1-diphosphate. {ECO:0000255|HAMAP-Rule:MF_01218}.
Cofactor: COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP-Rule:MF_01218}; ; Note=Binds 1 Mg(2+) ion per subunit. The magnesium is bound as Mg-PRPP. {ECO:0000255|HAMAP-Rule:MF_01218}
Enzyme regulation: ENZYME REGULATION: Allosterically activated by GTP. {ECO:0000255|HAMAP-Rule:MF_01218}.
Function [CC]: FUNCTION: Catalyzes the conversion of uracil and 5-phospho-alpha-D-ribose 1-diphosphate (PRPP) to UMP and diphosphate. {ECO:0000255|HAMAP-Rule:MF_01218}.
Pathway: PATHWAY: Pyrimidine metabolism; UMP biosynthesis via salvage pathway; UMP from uracil: step 1/1. {ECO:0000255|HAMAP-Rule:MF_01218}.
Active site:
Binding site: BINDING 78 78 5-phospho-alpha-D-ribose 1-diphosphate. {ECO:0000255|HAMAP-Rule:MF_01218}.; BINDING 103 103 5-phospho-alpha-D-ribose 1-diphosphate. {ECO:0000255|HAMAP-Rule:MF_01218}.; BINDING 193 193 Uracil; via amide nitrogen. {ECO:0000255|HAMAP-Rule:MF_01218}.; BINDING 199 199 5-phospho-alpha-D-ribose 1-diphosphate. {ECO:0000255|HAMAP-Rule:MF_01218}.
Calcium binding:
DNA binding:
Metal binding:
Nucleotide binding:
Site:
Gene names (primary): upp
Gene names (synonym):
Mass: 22,687
Subunit structure [CC]:
Gene ontology (GO): GTP binding [GO:0005525]; magnesium ion binding [GO:0000287]; uracil phosphoribosyltransferase activity [GO:0004845]; UMP salvage [GO:0044206]; uracil salvage [GO:0006223]
Gene ontology IDs: GO:0000287; GO:0004845; GO:0005525; GO:0006223; GO:0044206
Chain: CHAIN 1 208 Uracil phosphoribosyltransferase. /FTId=PRO_1000085619.
Signal peptide:
Domain [CC]:
Sequence similarities: SIMILARITY: Belongs to the UPRTase family. {ECO:0000255|HAMAP-Rule:MF_01218}.
Protein families: UPRTase family
Coiled coil:
Domain [FT]:
Motif:
Region: REGION 130 138 5-phospho-alpha-D-ribose 1-diphosphate binding. {ECO:0000255|HAMAP-Rule:MF_01218}.; REGION 198 200 Uracil binding. {ECO:0000255|HAMAP-Rule:MF_01218}.
EMBL: CP000896
ProteinModelPortal: A9NEQ2
MEROPS:
EnsemblBacteria KO: ABX80832
UniPathway: K00761
CDD:
Gene3D: cd06223
HAMAP: 3.40.50.2020
InterPro: MF_01218_B
PANTHER: IPR000836;IPR029057;IPR005765
PIRSF:
PRINTS:
PROSITE:
Pfam:
ProDom: PF14681
SMART:
SUPFAM:
TIGRFAMs: SSF53271

197287-197914(+)

>nucleotide sequence
ATGGGCAAACTTGTTGTATTAAATCACCCATTAATCGATCATAAAATGGCACTTATAAGA
GATAAAAACACCAGTACAAAAACATTTAGAGAAACTGTTGGAGAAATTGGTGCATTAATC
ACTTATGAAATCACAAAAGATCTAGAAACTGTTGAAATTGAAGTGGAAACTCCAATTCAA
AAAACAATTTGTAGACAATTAAAAAAACAACTTGTTATCGTTCCAATTTTAAGAGCAGGA
CTCGGTATGGTGAATGGTATTCATGATATGGTACCAAGTGCAAAAATAGGCCATATTGGT
TTATATAGAGATGAAAAATCTCTAGAACCAGTATCTTATTATGCAAAATTCCCAACAGAC
ATATTAGATGGTGTAGTGTTAGTTGTTGACCCAATGCTTGCAACGGGTGGATCAGCTACT
GCAGCAATCACTGAACTTAAAAATCGTGGAGCTAAAGATGTTAGATTTGTTGGTCTAGTA
GGGTGTCCTGAAGGTGTTAAACGTCTTCAAATGGATCATCCGGATGTACCAATATATTTA
GCAGCATTAGATGAGAAACTTAATGAGGTTGGCTACATTGTACCAGGACTTGGAGATGCA
GGAGACCGCCTCTTCGGTACTAAATAA

>protein sequence
MGKLVVLNHPLIDHKMALIRDKNTSTKTFRETVGEIGALITYEITKDLETVEIEVETPIQ
KTICRQLKKQLVIVPILRAGLGMVNGIHDMVPSAKIGHIGLYRDEKSLEPVSYYAKFPTD
ILDGVVLVVDPMLATGGSATAAITELKNRGAKDVRFVGLVGCPEGVKRLQMDHPDVPIYL
AALDEKLNEVGYIVPGLGDAGDRLFGTK