Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

A6Q2C1 (PYRF_NITSB) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 46. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Orotidine 5'-phosphate decarboxylase

EC=4.1.1.23
Alternative name(s):
OMP decarboxylase
Short name=OMPDCase
Short name=OMPdecase
Gene names
Name:pyrF
Ordered Locus Names:NIS_0516
OrganismNitratiruptor sp. (strain SB155-2) [Complete proteome] [HAMAP]
Taxonomic identifier387092 [NCBI]
Taxonomic lineageBacteriaProteobacteriaEpsilonproteobacteriaNitratiruptor

Protein attributes

Sequence length227 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the decarboxylation of orotidine 5'-monophosphate (OMP) to uridine 5'-monophosphate (UMP) By similarity. HAMAP-Rule MF_01200

Catalytic activity

Orotidine 5'-phosphate = UMP + CO2. HAMAP-Rule MF_01200

Pathway

Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from orotate: step 2/2. HAMAP-Rule MF_01200

Subunit structure

Homodimer By similarity. HAMAP-Rule MF_01200

Sequence similarities

Belongs to the OMP decarboxylase family. Type 1 subfamily.

Ontologies

Keywords
   Biological processPyrimidine biosynthesis
   Molecular functionDecarboxylase
Lyase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_process'de novo' UMP biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

'de novo' pyrimidine nucleobase biosynthetic process

Inferred from electronic annotation. Source: InterPro

   Molecular_functionorotidine-5'-phosphate decarboxylase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 227227Orotidine 5'-phosphate decarboxylase HAMAP-Rule MF_01200
PRO_1000065923

Regions

Region59 – 6810Substrate binding By similarity

Sites

Active site611Proton donor By similarity
Binding site81Substrate By similarity
Binding site301Substrate By similarity
Binding site1181Substrate By similarity
Binding site1781Substrate By similarity
Binding site1871Substrate By similarity
Binding site2071Substrate; via amide nitrogen By similarity
Binding site2081Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
A6Q2C1 [UniParc].

Last modified August 21, 2007. Version 1.
Checksum: 12DA729F1FD13C58

FASTA22725,503
        10         20         30         40         50         60 
MQLCVALDLP SIEENLSLAK SLKNYDIWLK VGLRSYIRDG KEFLKQIKQI NPNFHIFLDL 

        70         80         90        100        110        120 
KLYDIPNTMA DAAEEIAKLG VEMFNIHASA GKEAMQSVMQ RVQKFQNPPL VLAVTVLTSF 

       130        140        150        160        170        180 
NEEQFRSIYN DSIENKAKQF AKEAYEAGLD GVVCSVYESD LIKNITSDTF ITLTPGIRPF 

       190        200        210        220 
GESAGDQKRV ADINLAKEKK VDFIVVGRPI YQANNPAEVV EKILTNL 

« Hide

References

[1]"Deep-sea vent epsilon-proteobacterial genomes provide insights into emergence of pathogens."
Nakagawa S., Takaki Y., Shimamura S., Reysenbach A.-L., Takai K., Horikoshi K.
Proc. Natl. Acad. Sci. U.S.A. 104:12146-12150(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: SB155-2.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AP009178 Genomic DNA. Translation: BAF69630.1.
RefSeqYP_001355987.1. NC_009662.1.

3D structure databases

ProteinModelPortalA6Q2C1.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING387092.NIS_0516.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAF69630; BAF69630; NIS_0516.
GeneID5360934.
KEGGnis:NIS_0516.
PATRIC22683066. VBINitSp82229_0547.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0284.
HOGENOMHOG000226071.
KOK01591.
OMARPITQSA.
OrthoDBEOG6N6815.

Enzyme and pathway databases

BioCycNSP387092:GHA5-544-MONOMER.
UniPathwayUPA00070; UER00120.

Family and domain databases

Gene3D3.20.20.70. 1 hit.
HAMAPMF_01200_B. OMPdecase_type1_B.
InterProIPR013785. Aldolase_TIM.
IPR014732. OMPdecase.
IPR018089. OMPdecase_AS.
IPR001754. OMPdeCOase_dom.
IPR011060. RibuloseP-bd_barrel.
[Graphical view]
PfamPF00215. OMPdecase. 1 hit.
[Graphical view]
SMARTSM00934. OMPdecase. 1 hit.
[Graphical view]
SUPFAMSSF51366. SSF51366. 1 hit.
TIGRFAMsTIGR01740. pyrF. 1 hit.
PROSITEPS00156. OMPDECASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePYRF_NITSB
AccessionPrimary (citable) accession number: A6Q2C1
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: August 21, 2007
Last modified: May 14, 2014
This is version 46 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways