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Protein

Orotate phosphoribosyltransferase

Gene

pyrE

Organism
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the transfer of a ribosyl phosphate group from 5-phosphoribose 1-diphosphate to orotate, leading to the formation of orotidine monophosphate (OMP).UniRule annotation1 Publication

Catalytic activityi

Orotidine 5'-phosphate + diphosphate = orotate + 5-phospho-alpha-D-ribose 1-diphosphate.UniRule annotation

Cofactori

Mg2+1 Publication, Mn2+1 PublicationNote: Mg2+. Mn2+ can replace Mg2+ as the divalent metal. The role of the metal is to bind 5-phosphoribose 1-diphosphate and form a Mg-5-phosphoribose 1-diphosphate complex which then serves as substrate for OPRTase.1 Publication

Pathwayi: UMP biosynthesis via de novo pathway

This protein is involved in step 1 of the subpathway that synthesizes UMP from orotate.UniRule annotation
Proteins known to be involved in the 2 steps of the subpathway in this organism are:
  1. Orotate phosphoribosyltransferase (pyrE)
  2. Orotidine 5'-phosphate decarboxylase (pyrF)
This subpathway is part of the pathway UMP biosynthesis via de novo pathway, which is itself part of Pyrimidine metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes UMP from orotate, the pathway UMP biosynthesis via de novo pathway and in Pyrimidine metabolism.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei26 – 2615-phosphoribose 1-diphosphate1 Publication
Binding sitei99 – 9915-phosphoribose 1-diphosphate; shared with dimeric partner1 Publication
Binding sitei100 – 10015-phosphoribose 1-diphosphate1 Publication
Binding sitei103 – 10315-phosphoribose 1-diphosphate; shared with dimeric partner1 Publication
Binding sitei105 – 10515-phosphoribose 1-diphosphate; shared with dimeric partner1 Publication
Binding sitei128 – 1281Orotate1 Publication
Binding sitei156 – 1561Orotate1 Publication

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Keywords - Biological processi

Pyrimidine biosynthesis

Keywords - Ligandi

Magnesium

Enzyme and pathway databases

BioCyciSENT99287:GCTI-3758-MONOMER.
SABIO-RKP08870.
UniPathwayiUPA00070; UER00119.

Names & Taxonomyi

Protein namesi
Recommended name:
Orotate phosphoribosyltransferaseUniRule annotation (EC:2.4.2.10UniRule annotation)
Short name:
OPRTUniRule annotation
Short name:
OPRTaseUniRule annotation
Gene namesi
Name:pyrE1 Publication
Ordered Locus Names:STM3733
OrganismiSalmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Taxonomic identifieri99287 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSalmonella
Proteomesi
  • UP000001014 Componenti: Chromosome

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi19 – 191K → Q: No loss of activity. 1 Publication
Mutagenesisi26 – 261K → A or Q: Reduced activity. 1 Publication
Mutagenesisi73 – 731K → A or Q: Significant loss of activity. 1 Publication
Mutagenesisi100 – 1001K → A: Reduced activity. 1 Publication
Mutagenesisi103 – 1031K → A or Q: Drastically reduced activity. 1 Publication
Mutagenesisi124 – 1241D → N: Loss of activity. 1 Publication
Mutagenesisi125 – 1251D → N: Loss of activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved1 Publication
Chaini2 – 213212Orotate phosphoribosyltransferasePRO_0000110734Add
BLAST

Proteomic databases

PaxDbiP08870.
PRIDEiP08870.

Interactioni

Subunit structurei

Homodimer.3 Publications

Protein-protein interaction databases

STRINGi99287.STM3733.

Structurei

Secondary structure

1
213
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi3 – 1412Combined sources
Beta strandi17 – 248Combined sources
Beta strandi30 – 356Combined sources
Helixi37 – 393Combined sources
Helixi43 – 6018Combined sources
Beta strandi65 – 684Combined sources
Turni71 – 733Combined sources
Helixi74 – 8916Combined sources
Beta strandi94 – 985Combined sources
Beta strandi104 – 1063Combined sources
Beta strandi109 – 1146Combined sources
Beta strandi118 – 1236Combined sources
Beta strandi128 – 1303Combined sources
Helixi132 – 14211Combined sources
Beta strandi146 – 15510Combined sources
Beta strandi161 – 1655Combined sources
Helixi166 – 1749Combined sources
Beta strandi177 – 1837Combined sources
Helixi184 – 19310Combined sources
Helixi195 – 1973Combined sources
Helixi198 – 21114Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1LH0X-ray2.00A/B1-213[»]
1OPRX-ray2.30A1-213[»]
1STOX-ray2.60A1-213[»]
ProteinModelPortaliP08870.
SMRiP08870. Positions 1-213.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP08870.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni34 – 352Orotate binding1 Publication
Regioni72 – 7325-phosphoribose 1-diphosphate binding1 Publication
Regioni124 – 13295-phosphoribose 1-diphosphate binding1 Publication

Sequence similaritiesi

Belongs to the purine/pyrimidine phosphoribosyltransferase family. PyrE subfamily.UniRule annotation

Phylogenomic databases

eggNOGiENOG4107QP2. Bacteria.
COG0461. LUCA.
HOGENOMiHOG000037974.
KOiK00762.
OMAiMKAYQRQ.
OrthoDBiEOG6091H8.
PhylomeDBiP08870.

Family and domain databases

Gene3Di3.40.50.2020. 1 hit.
HAMAPiMF_01208. PyrE.
InterProiIPR023031. OPRT.
IPR004467. Or_phspho_trans_dom.
IPR000836. PRibTrfase_dom.
IPR029057. PRTase-like.
[Graphical view]
PfamiPF00156. Pribosyltran. 1 hit.
[Graphical view]
SUPFAMiSSF53271. SSF53271. 1 hit.
TIGRFAMsiTIGR00336. pyrE. 1 hit.
PROSITEiPS00103. PUR_PYR_PR_TRANSFER. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P08870-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKPYQRQFIE FALNKQVLKF GEFTLKSGRK SPYFFNAGLF NTGRDLALLG
60 70 80 90 100
RFYAEALVDS GIEFDLLFGP AYKGIPIATT TAVALAEHHD KDLPYCFNRK
110 120 130 140 150
EAKDHGEGGS LVGSALQGRV MLVDDVITAG TAIRESMEII QAHGATLAGV
160 170 180 190 200
LISLDRQERG RGEISAIQEV ERDYGCKVIS IITLKDLIAY LEEKPDMAEH
210
LAAVRAYREE FGV
Length:213
Mass (Da):23,562
Last modified:January 23, 2007 - v3
Checksum:i963A8BE3DD9113B0
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z19547 Genomic DNA. Translation: CAA79607.1.
AE006468 Genomic DNA. Translation: AAL22592.1.
PIRiS32801.
RefSeqiNP_462633.1. NC_003197.1.
WP_000806167.1. NC_003197.1.

Genome annotation databases

EnsemblBacteriaiAAL22592; AAL22592; STM3733.
GeneIDi1255257.
KEGGistm:STM3733.
PATRICi32386305. VBISalEnt20916_3949.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z19547 Genomic DNA. Translation: CAA79607.1.
AE006468 Genomic DNA. Translation: AAL22592.1.
PIRiS32801.
RefSeqiNP_462633.1. NC_003197.1.
WP_000806167.1. NC_003197.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1LH0X-ray2.00A/B1-213[»]
1OPRX-ray2.30A1-213[»]
1STOX-ray2.60A1-213[»]
ProteinModelPortaliP08870.
SMRiP08870. Positions 1-213.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi99287.STM3733.

Proteomic databases

PaxDbiP08870.
PRIDEiP08870.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAL22592; AAL22592; STM3733.
GeneIDi1255257.
KEGGistm:STM3733.
PATRICi32386305. VBISalEnt20916_3949.

Phylogenomic databases

eggNOGiENOG4107QP2. Bacteria.
COG0461. LUCA.
HOGENOMiHOG000037974.
KOiK00762.
OMAiMKAYQRQ.
OrthoDBiEOG6091H8.
PhylomeDBiP08870.

Enzyme and pathway databases

UniPathwayiUPA00070; UER00119.
BioCyciSENT99287:GCTI-3758-MONOMER.
SABIO-RKP08870.

Miscellaneous databases

EvolutionaryTraceiP08870.

Family and domain databases

Gene3Di3.40.50.2020. 1 hit.
HAMAPiMF_01208. PyrE.
InterProiIPR023031. OPRT.
IPR004467. Or_phspho_trans_dom.
IPR000836. PRibTrfase_dom.
IPR029057. PRTase-like.
[Graphical view]
PfamiPF00156. Pribosyltran. 1 hit.
[Graphical view]
SUPFAMiSSF53271. SSF53271. 1 hit.
TIGRFAMsiTIGR00336. pyrE. 1 hit.
PROSITEiPS00103. PUR_PYR_PR_TRANSFER. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Primary structure and crystallization of orotate phosphoribosyltransferase from Salmonella typhimurium."
    Scapin G., Sacchettini J.C., Dessen A., Bhatia M., Grubmeyer C.
    J. Mol. Biol. 230:1304-1308(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: LT2 / SGSC1412 / ATCC 700720.
  3. "Cloning and characterization of the pyrE gene and of PyrE::Mud1 (Ap lac) fusions from Salmonella typhimurium."
    Neuhard J., Stauning E., Kelln R.A.
    Eur. J. Biochem. 146:597-603(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-60.
  4. "Kinetic mechanism of orotate phosphoribosyltransferase from Salmonella typhimurium."
    Bhatia M.B., Vinitsky A., Grubmeyer C.
    Biochemistry 29:10480-10487(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-17, FUNCTION, KINETIC MECHANISM.
  5. "The role of divalent magnesium in activating the reaction catalyzed by orotate phosphoribosyltransferase."
    Bhatia M.B., Grubmeyer C.
    Arch. Biochem. Biophys. 303:321-325(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: COFACTOR.
  6. "Active site lysines in orotate phosphoribosyltransferase."
    Grubmeyer C., Segura E., Dorfman R.H.
    J. Biol. Chem. 268:20299-20304(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 20-29 AND 100-108.
  7. "Locations and functional roles of conserved lysine residues in Salmonella typhimurium orotate phosphoribosyltransferase."
    Ozturk D.H., Dorfman R.H., Scapin G., Sacchettini J.C., Grubmeyer C.
    Biochemistry 34:10755-10763(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS, PARTIAL PROTEIN SEQUENCE.
  8. "Structure and function of Salmonella typhimurium orotate phosphoribosyltransferase: protein complementation reveals shared active sites."
    Ozturk D.H., Dorfman R.H., Scapin G., Sacchettini J.C., Grubmeyer C.
    Biochemistry 34:10764-10770(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT, BINDING SITES.
  9. "Crystal structure of orotate phosphoribosyltransferase."
    Scapin G., Grubmeyer C., Sacchettini J.C.
    Biochemistry 33:1287-1294(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) IN COMPLEX WITH OMP.
  10. "The crystal structure of the orotate phosphoribosyltransferase complexed with orotate and alpha-D-5-phosphoribosyl-1-pyrophosphate."
    Scapin G., Ozturk D.H., Grubmeyer C., Sacchettini J.C.
    Biochemistry 34:10744-10754(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) IN COMPLEX WITH OROTATE AND PRPP.

Entry informationi

Entry nameiPYRE_SALTY
AccessioniPrimary (citable) accession number: P08870
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1988
Last sequence update: January 23, 2007
Last modified: January 20, 2016
This is version 135 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.