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D0KT28 (D0KT28_SULS9) Unreviewed, UniProtKB/TrEMBL

Last modified June 11, 2014. Version 30. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Orotidine 5'-phosphate decarboxylase HAMAP-Rule MF_01200

EC=4.1.1.23 HAMAP-Rule MF_01200
Alternative name(s):
OMP decarboxylase HAMAP-Rule MF_01200
Gene names
Name:pyrF HAMAP-Rule MF_01200
Ordered Locus Names:Ssol_1680 EMBL ACX91897.1
OrganismSulfolobus solfataricus (strain 98/2) [Complete proteome] [HAMAP] EMBL ACX91897.1
Taxonomic identifier555311 [NCBI]
Taxonomic lineageArchaeaCrenarchaeotaThermoproteiSulfolobalesSulfolobaceaeSulfolobus

Protein attributes

Sequence length222 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

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. HAMAP-Rule MF_01200

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Regions

Region59 – 6810Substrate binding By similarity HAMAP-Rule MF_01200
Region164 – 17411Substrate binding By similarity HAMAP-Rule MF_01200
Region187 – 1882Sulfate 4 binding

Sites

Active site611Proton donor By similarity HAMAP-Rule MF_01200
Binding site111Substrate By similarity HAMAP-Rule MF_01200
Binding site301Substrate By similarity HAMAP-Rule MF_01200
Binding site991Sulfate 2 PDB 4DBE
Binding site1151Substrate By similarity HAMAP-Rule MF_01200
Binding site1211Sulfate 3
Binding site1481Sulfate 3
Binding site1691Sulfate 4
Binding site1871Substrate; via amide nitrogen By similarity HAMAP-Rule MF_01200
Binding site1881Substrate By similarity HAMAP-Rule MF_01200

Sequences

Sequence LengthMass (Da)Tools
D0KT28 [UniParc].

Last modified December 15, 2009. Version 1.
Checksum: 48F3E83DB0F043FF

FASTA22224,701
        10         20         30         40         50         60 
MLKSRVILAM DKPLSYQVLK EMENELYGIK VGLPLVLDLG VDKTRELLIG LDVEEIIVDF 

        70         80         90        100        110        120 
KLADIGYIMK SIVERLSFAN SFIAHSFIGV KGSLDELKRY LDANSKNLYL VAVMSHEGWS 

       130        140        150        160        170        180 
TLFADYIKNV IREISPKGIV VGGTKLDHIT QYRRDFEKMT IVSPGMGSQG GSYGDAVCAG 

       190        200        210        220 
ADYEIIGRSI YNAGNPLTAL RTINKIIEDK VMKCKGAIFR KK 

« Hide

References

« Hide 'large scale' references
[1]"Complete sequence of Sulfolobus solfataricus 98/2."
US DOE Joint Genome Institute
Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D., Goodwin L., Pitluck S., Munk A.C., Brettin T., Detter J.C., Han C., Tapia R., Larimer F., Land M., Hauser L., Kyrpides N., Ovchinnikova G., Mead D.
Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 98/2 EMBL ACX91897.1.
[2]"Crystal structure of orotidine 5'-monophosphate decarboxylase from Sulfolobus solfataricus complexed with inhibitor BMP."
Fedorov A.A., Fedorov E.V., Desai B., Gerlt J.A., Almo S.C.
Submitted (JAN-2012) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (1.79 ANGSTROMS) IN COMPLEX WITH SULFATE.
[3]"Crystal structure of orotidine 5'-monophosphate decarboxylase from Sulfolobus solfataricus."
Fedorov A.A., Fedorov E.V., Desai B., Gerlt J.A., Almo S.C.
Submitted (JAN-2012) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) IN COMPLEX WITH SULFATE.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001800 Genomic DNA. Translation: ACX91897.1.
RefSeqYP_005643498.1. NC_017274.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
4DBDX-ray1.70A1-222[»]
4DBEX-ray1.79A/B1-222[»]
ProteinModelPortalD0KT28.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACX91897; ACX91897; Ssol_1680.
GeneID12257711.
KEGGsol:Ssol_1680.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHOG000226069.
KOK01591.
OMATEMSHPG.

Enzyme and pathway databases

BioCycSSOL555311:GLLY-1711-MONOMER.
UniPathwayUPA00070; UER00120.

Family and domain databases

Gene3D3.20.20.70. 1 hit.
HAMAPMF_01200_A. OMPdecase_type1_A.
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.
ProtoNetSearch...

Entry information

Entry nameD0KT28_SULS9
AccessionPrimary (citable) accession number: D0KT28
Entry history
Integrated into UniProtKB/TrEMBL: December 15, 2009
Last sequence update: December 15, 2009
Last modified: June 11, 2014
This is version 30 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)