Skip Header

Contribute Send feedback
Read comments (?) or add your own

Q2NQT8 (Q2NQT8_SODGM) Unreviewed, UniProtKB/TrEMBL

Last modified May 1, 2013. Version 66. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry infoCustomize order

Names and origin

Protein namesRecommended name:
Orotate phosphoribosyltransferase HAMAP-Rule MF_01208

Short name=OPRT HAMAP-Rule MF_01208
Short name=OPRTase HAMAP-Rule MF_01208
EC=2.4.2.10 HAMAP-Rule MF_01208
Gene names
Name:pyrE HAMAP-Rule MF_01208
Ordered Locus Names:SG2212 EMBL BAE75487.1
OrganismSodalis glossinidius (strain morsitans) [Complete proteome] [HAMAP] EMBL BAE75487.1
Taxonomic identifier343509 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSodalis

Protein attributes

Sequence length213 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the transfer of a ribosyl phosphate group from 5-phosphoribose 1-diphosphate to orotate, leading to the formation of orotidine monophosphate (OMP) By similarity. HAMAP-Rule MF_01208 SAAS SAAS004467

Catalytic activity

Orotidine 5'-phosphate + diphosphate = orotate + 5-phospho-alpha-D-ribose 1-diphosphate. HAMAP-Rule MF_01208 SAAS SAAS023031

Cofactor

Magnesium By similarity. HAMAP-Rule MF_01208

Pathway

Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from orotate: step 1/2. HAMAP-Rule MF_01208

Subunit structure

Homodimer By similarity. HAMAP-Rule MF_01208 SAAS SAAS004467

Sequence similarities

Belongs to the purine/pyrimidine phosphoribosyltransferase family. PyrE subfamily. HAMAP-Rule MF_01208

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Regions

Region34 – 352Orotate binding By similarity HAMAP-Rule MF_01208
Region72 – 7325-phosphoribose 1-diphosphate binding By similarity HAMAP-Rule MF_01208
Region124 – 13295-phosphoribose 1-diphosphate binding By similarity HAMAP-Rule MF_01208

Sites

Binding site2615-phosphoribose 1-diphosphate By similarity HAMAP-Rule MF_01208
Binding site9915-phosphoribose 1-diphosphate; shared with dimeric partner By similarity HAMAP-Rule MF_01208
Binding site10015-phosphoribose 1-diphosphate By similarity HAMAP-Rule MF_01208
Binding site10315-phosphoribose 1-diphosphate; shared with dimeric partner By similarity HAMAP-Rule MF_01208
Binding site10515-phosphoribose 1-diphosphate; shared with dimeric partner By similarity HAMAP-Rule MF_01208
Binding site1281Orotate By similarity HAMAP-Rule MF_01208
Binding site1561Orotate By similarity HAMAP-Rule MF_01208

Sequences

Sequence LengthMass (Da)Tools
Q2NQT8 [UniParc].

Last modified February 7, 2006. Version 1.
Checksum: EA0B1ABDCF29C807

FASTA21323,458
        10         20         30         40         50         60 
MKEYQSKFIE YALNKQVLKF GEFTLKSGRI SPYFFNAGLF NTGRDLAFLG RVYAAALMDS 

        70         80         90        100        110        120 
GVRFDVLFGP AYKGIPIATT TAVALAEQHQ RDVPYCFNRK EAKDHGEGGT LVGSPLQGKV 

       130        140        150        160        170        180 
MLVDDVITAG TAIRESMEII AAHQATLAGV MISLDRQEKG RSEISAIQEV ERDYHCQVLA 

       190        200        210 
IITLADLIAY LEEKGEMAGH LAAVRAYQQQ YGI 

« Hide

References

[1]"Massive genome erosion and functional adaptations provide insights into the symbiotic lifestyle of Sodalis glossinidius in the tsetse host."
Toh H., Weiss B.L., Perkin S.A.H., Yamashita A., Oshima K., Hattori M., Aksoy S.
Genome Res. 16:149-156(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: morsitans.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AP008232 Genomic DNA. Translation: BAE75487.1.
RefSeqYP_455892.1. NC_007712.1.

3D structure databases

ProteinModelPortalQ2NQT8.
SMRQ2NQT8. Positions 1-213.
ModBaseSearch...

Protein-protein interaction databases

STRING343509.SG2212.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAE75487; BAE75487; ENAG00098106.
GeneID3868757.
KEGGsgl:SG2212.
PATRIC23656307. VBISodGlo61428_5428.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0461.
KOK00762.
OMAMKAYQRQ.
ProtClustDBPRK00455.

Enzyme and pathway databases

BioCycSGLO343509:GJJC-2288-MONOMER.
UniPathwayUPA00070; UER00119.

Family and domain databases

HAMAPMF_01208. PyrE.
InterProIPR023031. OPRT.
IPR004467. Or_phspho_trans_dom.
IPR000836. PRibTrfase_dom.
[Graphical view]
PfamPF00156. Pribosyltran. 1 hit.
[Graphical view]
TIGRFAMsTIGR00336. pyrE. 1 hit.
ProtoNetSearch...

Entry information

Entry nameQ2NQT8_SODGM
AccessionPrimary (citable) accession number: Q2NQT8
Entry history
Integrated into UniProtKB/TrEMBL: February 7, 2006
Last sequence update: February 7, 2006
Last modified: May 1, 2013
This is version 66 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)