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Q2LQ82 (PYRF_SYNAS) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 56. 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:SYNAS_02780
ORF Names:SYN_01281
OrganismSyntrophus aciditrophicus (strain SB) [Complete proteome] [HAMAP]
Taxonomic identifier56780 [NCBI]
Taxonomic lineageBacteriaProteobacteriaDeltaproteobacteriaSyntrophobacteralesSyntrophaceaeSyntrophus

Protein attributes

Sequence length251 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 – 251251Orotidine 5'-phosphate decarboxylase HAMAP-Rule MF_01200
PRO_0000241923

Regions

Region69 – 7810Substrate binding By similarity

Sites

Active site711Proton donor By similarity
Binding site191Substrate By similarity
Binding site421Substrate By similarity
Binding site1331Substrate By similarity
Binding site1941Substrate By similarity
Binding site2041Substrate By similarity
Binding site2241Substrate; via amide nitrogen By similarity
Binding site2251Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q2LQ82 [UniParc].

Last modified February 21, 2006. Version 1.
Checksum: 0BDAD356B62E33A7

FASTA25127,021
        10         20         30         40         50         60 
MTKTMSNKES LEKLIFALDM GGGLDDVMSW VRRLAGHVGV FKVGKEAFTR FGPQLVQSIQ 

        70         80         90        100        110        120 
ETGSRVFLDL KFHDIPNTVA RAAEGAVELG VAMFNVHALG GMSMMTETVE SVKKMAGRRE 

       130        140        150        160        170        180 
LPMPLILGVT VLTSLNDEDL QRLGFTCTTG ELVLRLARMA QDAGLSGVVA SAQDVEAIRA 

       190        200        210        220        230        240 
ACGKDFVIVT PGIRGLARVA GDDQKRVLTA EEAVRRGSDY LVIGRPIRTA EDPVAAADDF 

       250 
CREIARGLSA R 

« Hide

References

[1]"The genome of the syntrophic bacterium Syntrophus aciditrophicus: Life dependent on negative change in electrical potential."
Gunsalus R., Rohlin L., Kim U., Krupp R., Bhattacharyya A., Campbell J., Mclerney M., Moutakki H., Rio-Hernandez L.
Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: SB.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000252 Genomic DNA. Translation: ABC76157.1.
RefSeqYP_460325.1. NC_007759.1.

3D structure databases

ProteinModelPortalQ2LQ82.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING56780.SYN_01281.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABC76157; ABC76157; SYN_01281.
GeneID3884670.
KEGGsat:SYN_01281.
PATRIC23860957. VBISynAci70500_0306.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0284.
HOGENOMHOG000226070.
KOK01591.
OMARPITQSA.
OrthoDBEOG6N6815.

Enzyme and pathway databases

BioCycSACI56780:GHXT-282-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_SYNAS
AccessionPrimary (citable) accession number: Q2LQ82
Entry history
Integrated into UniProtKB/Swiss-Prot: June 27, 2006
Last sequence update: February 21, 2006
Last modified: May 14, 2014
This is version 56 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