Skip Header

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

Q8F1Z0 (Q8F1Z0_LEPIN) Unreviewed, UniProtKB/TrEMBL

Last modified December 14, 2011. Version 67. 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
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 MF_01208
Short name=OPRT HAMAP MF_01208
Short name=OPRTase HAMAP MF_01208
EC=2.4.2.10 HAMAP MF_01208
Gene names
Name:pyrE HAMAP MF_01208 EMBL AAN50186.1
Ordered Locus Names:LA_2988 EMBL AAN50186.1
OrganismLeptospira interrogans serogroup Icterohaemorrhagiae serovar Lai (strain 56601)
Taxonomic identifier189518 [NCBI]
Taxonomic lineageBacteria › Spirochaetes › Spirochaetales › Leptospiraceae › Leptospira

Protein attributes

Sequence length194 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 MF_01208 SAAS SAAS004467

Catalytic activity

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

Cofactor

Magnesium By similarity. HAMAP MF_01208

Pathway

Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from orotate: step 1/2. HAMAP MF_01208 SAAS SAAS023031

Subunit structure

Homodimer By similarity. HAMAP MF_01208 SAAS SAAS004467

Sequence similarities

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Regions

Region132 – 14095-phosphoribose 1-diphosphate binding By similarity HAMAP MF_01208

Sites

Binding site10615-phosphoribose 1-diphosphate; shared with dimeric partner By similarity HAMAP MF_01208
Binding site10715-phosphoribose 1-diphosphate By similarity HAMAP MF_01208
Binding site11015-phosphoribose 1-diphosphate; shared with dimeric partner By similarity HAMAP MF_01208
Binding site11215-phosphoribose 1-diphosphate; shared with dimeric partner By similarity HAMAP MF_01208
Binding site1361Orotate By similarity HAMAP MF_01208

Sequences

Sequence LengthMass (Da)Tools
Q8F1Z0 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: 409C300EF020D408

FASTA19421,845
        10         20         30         40         50         60 
MLKKELSMKQ ELLELIRTHV YRYSEQPFTL ASGRKSRHYF NCKEITLVPD RLELLCKFIV 

        70         80         90        100        110        120 
EQHLGESGIL LPHAFGGLTM GADPICYGIS LEFRKQNKNV YPLIVRKLSK DHGTKKLVEG 

       130        140        150        160        170        180 
STHLVKQCVV IDDVITTGGS TIQAIRSLRD CGIEVVQGVC ILDRQEGGKD AILAEGVEMF 

       190 
PIFKKSDFGN LEHE

« Hide

References

[1]"Unique physiological and pathogenic features of Leptospira interrogans revealed by whole-genome sequencing."
Ren S.-X., Fu G., Jiang X.-G., Zeng R., Miao Y.-G., Xu H., Zhang Y.-X., Xiong H., Lu G., Lu L.-F., Jiang H.-Q., Jia J., Tu Y.-F., Jiang J.-X., Gu W.-Y., Zhang Y.-Q., Cai Z., Sheng H.-H. expand/collapse author list , Yin H.-F., Zhang Y., Zhu G.-F., Wan M., Huang H.-L., Qian Z., Wang S.-Y., Ma W., Yao Z.-J., Shen Y., Qiang B.-Q., Xia Q.-C., Guo X.-K., Danchin A., Saint Girons I., Somerville R.L., Wen Y.-M., Shi M.-H., Chen Z., Xu J.-G., Zhao G.-P.
Nature 422:888-893(2003) [PubMed: 12712204] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 56601.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE010300 Genomic DNA. Translation: AAN50186.1.
RefSeqNP_713168.1. NC_004342.2.

3D structure databases

HSSPHSSP built from PDB template 1LH0 based on UniProtKB P08870.
ProteinModelPortalQ8F1Z0.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1152330.
GenomeReviewsGene locus LA2988 in contig AE010300_GR.
KEGGlil:LA_2988.
NMPDRfig|189518.1.peg.2987.
PATRIC22386806. VBILepInt91350_2967.

Phylogenomic databases

HOGENOMHBG404341.
OMAAMVTGKA.
PhylomeDBQ8F1Z0.
ProtClustDBCLSK574681.

Family and domain databases

HAMAPMF_01208. PyrE.
[Tree]
InterProIPR004467. Or_phspho_trans_clade-1.
IPR023031. Orotate_PribosylTferase.
IPR000836. PRibTrfase.
[Graphical view]
KOK00762.
PfamPF00156. Pribosyltran. 1 hit.
[Graphical view]
TIGRFAMsTIGR00336. PyrE. 1 hit.
ProtoNetSearch...

Entry information

Entry nameQ8F1Z0_LEPIN
AccessionPrimary (citable) accession number: Q8F1Z0
Entry history
Integrated into UniProtKB/TrEMBL: March 1, 2003
Last sequence update: March 1, 2003
Last modified: December 14, 2011
This is version 67 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info