Skip Header

 
Contribute Send feedback

Reviewed, UniProtKB/Swiss-Prot Q1WVB1 (PYRC_LACS1)

Last modified September 2, 2008. Version 19. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Dihydroorotase
      Short name=DHOase
    EC=3.5.2.3
Gene names
Name: pyrC
Ordered Locus Names: LSL_0191
OrganismLactobacillus salivarius subsp. salivarius (strain UCC118) [Complete proteome] [HAMAP]
Taxonomic identifier362948 [NCBI]
Taxonomic lineageBacteriaFirmicutesLactobacillalesLactobacillaceaeLactobacillus

Protein attributes

Sequence length429 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

General annotation (Comments)

Catalytic activity

(S)-dihydroorotate + H(2)O = N-carbamoyl-L-aspartate.

Cofactor

Binds 2 zinc ions per subunit By similarity.

Pathway

Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from HCO(3)(-): step 3/6.

Subunit structure

Homodimer By similarity.

Sequence similarities

Belongs to the DHOase family. Type 2 subfamily.

Ontologies

Keywords

   Biological processPyrimidine biosynthesis
   LigandMetal-binding
Zinc
   Molecular functionHydrolase
   Technical termComplete proteome

Gene Ontology (GO)

   Biological processpyrimidine nucleotide biosynthetic process

Inferred from electronic annotation. Source: HAMAP

   Molecular functiondihydroorotase activity

Inferred from electronic annotation. Source: HAMAP

zinc ion binding

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 429429Dihydroorotase
PRO_1000024091

Sites

Metal binding611Zinc 1 By similarity
Metal binding631Zinc 1 By similarity
Metal binding1431Zinc 1; via carbamate group By similarity
Metal binding1431Zinc 2; via carbamate group By similarity
Metal binding1801Zinc 2 By similarity
Metal binding2331Zinc 2 By similarity
Metal binding3061Zinc 1 By similarity

Amino acid modifications

Modified residue1431N6-carboxylysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q1WVB1-1 [UniParc].

Last modified May 2, 2006. Version 1.
Checksum: 7A32DF5D16BE2303

FASTA42946,735
        10         20         30         40         50         60 
MATLIKNGNL YQAGRIYQAD VLIEDGKIKA IGKNLSDVVK ENLVEIDATN KLVAPGLVDV 

        70         80         90        100        110        120 
HVHYRDPGFT YKETIHTGSL AAAHGGYTTV CAMPNLDPVP DTPELVEKMC SRNQEDGVVK 

       130        140        150        160        170        180 
VKQYGSITHG LKSEELVDFV GMKKAGAFAF SNDGSGVQTA GTMYQAMKSA AALNMAIVAH 

       190        200        210        220        230        240 
VEDNSLLFGG VMNAGKRADE LGLPGILGIS ESSQIARDLL LAKETGVHYH VCHVSTKESV 

       250        260        270        280        290        300 
ELVRLAKQHK INVTCEVSPH HLLLADVDIP GNDPYYKMNP PLRGVEDRQA LIDSLLDGTI 

       310        320        330        340        350        360 
DMIATDHAPH SIDEKTGDMR EASFGITGSE TAFAMLYTKF VKTGIFTLEQ LLQWMSINPA 

       370        380        390        400        410        420 
EKFGMEDAGE LLPGKSADLA IFDLNKEYVI KEEDYLSKGI NTPFTGEKVY GQTVLTMVDG 


QKVYQREEK 

« Hide

Cross-references

Sequence databases

CP000233 Genomic DNA. Translation: ABD99006.1.
RefSeqYP_535089.1.

3D structure databases

ModBaseSearch...

Protein family/group databases

MEROPSM38.972.

Genome annotation databases

GeneID3978041.
GenomeReviewsGene locus LSL_0191 in contig CP000233_GR.
KEGGlsl:LSL_0191.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ1WVB1.

Enzyme and pathway databases

BioCycLSAL362948:LSL_0191-MON.

Family and domain databases

HAMAPMF_00220.
[Tree]
InterProIPR006680. Amidohydro_1.
IPR004722. DHOmult.
IPR002195. Dihydroorotase_CS.
[Graphical view]
PfamPF01979. Amidohydro_1. 1 hit.
[Graphical view]
ProDomPD000518. DHOase. 1 hit.
[Graphical view] [Entries sharing at least one domain]
TIGRFAMsTIGR00857. pyrC_multi. 1 hit.
PROSITEPS00482. DIHYDROOROTASE_1. False negative.
PS00483. DIHYDROOROTASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePYRC_LACS1
AccessionPrimary (citable) accession number: Q1WVB1
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: May 2, 2006
Last modified: September 2, 2008
This is version 19 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents