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Q1QMP2 (PYRF_NITHX) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 58. 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:Nham_1688
OrganismNitrobacter hamburgensis (strain X14 / DSM 10229) [Complete proteome] [HAMAP]
Taxonomic identifier323097 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBradyrhizobiaceaeNitrobacter

Protein attributes

Sequence length240 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 – 240240Orotidine 5'-phosphate decarboxylase HAMAP-Rule MF_01200
PRO_1000065922

Regions

Region68 – 7710Substrate binding By similarity

Sites

Active site701Proton donor By similarity
Binding site191Substrate By similarity
Binding site411Substrate By similarity
Binding site1231Substrate By similarity
Binding site1841Substrate By similarity
Binding site1931Substrate By similarity
Binding site2131Substrate; via amide nitrogen By similarity
Binding site2141Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q1QMP2 [UniParc].

Last modified May 16, 2006. Version 1.
Checksum: 8DFF86AAB7E1EC3B

FASTA24026,164
        10         20         30         40         50         60 
MTDSHYLDRA REKLIVALDF WEVEDARKLV RKLGDEVSFY KVGLGLQLVG GNEFAKELIV 

        70         80         90        100        110        120 
EGKRVFLDYK YYDIEETVQR AVAQAAELKI TFLTVHGVAS IMKAAVAGRG NSDMKILGVT 

       130        140        150        160        170        180 
VLTSMDAEDI KEMGFDGKVE DLVIARAKKA LEVGVDGVVA SALEAAELRK QTSNKLMIVS 

       190        200        210        220        230        240 
PGIRPSGGAR HDQKRVATPF EAIRAGADYL VLGRPIYAAD DPKAAAQAII QEMADALRPD 

« Hide

References

[1]"Complete sequence of chromosome of Nitrobacter hamburgensis X14."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M. expand/collapse author list , Hauser L., Kyrpides N., Ivanova N., Ward B., Arp D., Klotz M., Stein L., O'Mullan G., Starkenburg S., Sayavedra L., Poret-Peterson A.T., Gentry M.E., Bruce D., Richardson P.
Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: X14 / DSM 10229.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000319 Genomic DNA. Translation: ABE62505.1.
RefSeqYP_576965.1. NC_007964.1.

3D structure databases

ProteinModelPortalQ1QMP2.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING323097.Nham_1688.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABE62505; ABE62505; Nham_1688.
GeneID4029392.
KEGGnha:Nham_1688.
PATRIC22691033. VBINitHam61822_2539.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0284.
HOGENOMHOG000226070.
KOK01591.
OMAHAKEPRE.
OrthoDBEOG6N6815.

Enzyme and pathway databases

BioCycNHAM323097:GHP7-1715-MONOMER.
UniPathwayUPA00070; UER00120.

Family and domain databases

Gene3D3.20.20.70. 1 hit.
HAMAPMF_01200_B. OMPdecase_type1_B.
InterProIPR013785. Aldolase_TIM.
IPR014732. OMPdecase.
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.
ProtoNetSearch...

Entry information

Entry namePYRF_NITHX
AccessionPrimary (citable) accession number: Q1QMP2
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: May 16, 2006
Last modified: May 14, 2014
This is version 58 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