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Protein

Orotidine 5'-phosphate decarboxylase

Gene

pyrF

Organism
Sulfolobus solfataricus (strain 98/2)
Status
Unreviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the decarboxylation of orotidine 5'-monophosphate (OMP) to uridine 5'-monophosphate (UMP).UniRule annotation

Catalytic activityi

Orotidine 5'-phosphate = UMP + CO2.UniRule annotation

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei11 – 111SubstrateUniRule annotation
Binding sitei30 – 301SubstrateUniRule annotation
Active sitei61 – 611Proton donorUniRule annotation
Binding sitei115 – 1151SubstrateUniRule annotation
Binding sitei187 – 1871Substrate; via amide nitrogenUniRule annotation
Binding sitei188 – 1881SubstrateUniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

DecarboxylaseUniRule annotation, Lyase

Keywords - Biological processi

Pyrimidine biosynthesisUniRule annotation

Enzyme and pathway databases

BioCyciSSOL555311:GLLY-1711-MONOMER.
UniPathwayiUPA00070; UER00120.

Names & Taxonomyi

Protein namesi
Recommended name:
Orotidine 5'-phosphate decarboxylaseUniRule annotation (EC:4.1.1.23UniRule annotation)
Alternative name(s):
OMP decarboxylaseUniRule annotation
Gene namesi
Name:pyrFUniRule annotation
Ordered Locus Names:Ssol_1680Imported
OrganismiSulfolobus solfataricus (strain 98/2)Imported
Taxonomic identifieri555311 [NCBI]
Taxonomic lineageiArchaeaCrenarchaeotaThermoproteiSulfolobalesSulfolobaceaeSulfolobus
ProteomesiUP000001493 Componenti: Chromosome

PTM / Processingi

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi178 ↔ 214Combined sources

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4DBDX-ray1.70A1-222[»]
4DBEX-ray1.79A/B1-222[»]
ProteinModelPortaliD0KT28.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni59 – 6810Substrate bindingUniRule annotation
Regioni164 – 17411Substrate bindingUniRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the OMP decarboxylase family. Type 1 subfamily.UniRule annotation

Phylogenomic databases

HOGENOMiHOG000226069.
KOiK01591.
OMAiVIMVTEM.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
HAMAPiMF_01200_A. OMPdecase_type1_A.
InterProiIPR013785. Aldolase_TIM.
IPR014732. OMPdecase.
IPR001754. OMPdeCOase_dom.
IPR011060. RibuloseP-bd_barrel.
[Graphical view]
PfamiPF00215. OMPdecase. 1 hit.
[Graphical view]
SMARTiSM00934. OMPdecase. 1 hit.
[Graphical view]
SUPFAMiSSF51366. SSF51366. 1 hit.

Sequencei

Sequence statusi: Complete.

D0KT28-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLKSRVILAM DKPLSYQVLK EMENELYGIK VGLPLVLDLG VDKTRELLIG
60 70 80 90 100
LDVEEIIVDF KLADIGYIMK SIVERLSFAN SFIAHSFIGV KGSLDELKRY
110 120 130 140 150
LDANSKNLYL VAVMSHEGWS TLFADYIKNV IREISPKGIV VGGTKLDHIT
160 170 180 190 200
QYRRDFEKMT IVSPGMGSQG GSYGDAVCAG ADYEIIGRSI YNAGNPLTAL
210 220
RTINKIIEDK VMKCKGAIFR KK
Length:222
Mass (Da):24,701
Last modified:December 15, 2009 - v1
Checksum:i48F3E83DB0F043FF
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001800 Genomic DNA. Translation: ACX91897.1.
RefSeqiWP_009991148.1. NZ_ACUK01000205.1.
YP_005643498.1. NC_017274.1.

Genome annotation databases

EnsemblBacteriaiACX91897; ACX91897; Ssol_1680.
GeneIDi12257711.
KEGGisol:Ssol_1680.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001800 Genomic DNA. Translation: ACX91897.1.
RefSeqiWP_009991148.1. NZ_ACUK01000205.1.
YP_005643498.1. NC_017274.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4DBDX-ray1.70A1-222[»]
4DBEX-ray1.79A/B1-222[»]
ProteinModelPortaliD0KT28.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiACX91897; ACX91897; Ssol_1680.
GeneIDi12257711.
KEGGisol:Ssol_1680.

Phylogenomic databases

HOGENOMiHOG000226069.
KOiK01591.
OMAiVIMVTEM.

Enzyme and pathway databases

UniPathwayiUPA00070; UER00120.
BioCyciSSOL555311:GLLY-1711-MONOMER.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
HAMAPiMF_01200_A. OMPdecase_type1_A.
InterProiIPR013785. Aldolase_TIM.
IPR014732. OMPdecase.
IPR001754. OMPdeCOase_dom.
IPR011060. RibuloseP-bd_barrel.
[Graphical view]
PfamiPF00215. OMPdecase. 1 hit.
[Graphical view]
SMARTiSM00934. OMPdecase. 1 hit.
[Graphical view]
SUPFAMiSSF51366. SSF51366. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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: 98/2Imported.
  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), DISULFIDE BONDS.
  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).

Entry informationi

Entry nameiD0KT28_SULS9
AccessioniPrimary (citable) accession number: D0KT28
Entry historyi
Integrated into UniProtKB/TrEMBL: December 15, 2009
Last sequence update: December 15, 2009
Last modified: May 27, 2015
This is version 40 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structureCombined sources, Complete proteomeImported

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.