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Reviewed, UniProtKB/Swiss-Prot A4J556 (PYRC_DESRM)

Last modified September 2, 2008. Version 12. 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

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Names and origin

Protein namesRecommended name:
    Dihydroorotase
      Short name=DHOase
    EC=3.5.2.3
Gene names
Name: pyrC
Ordered Locus Names: Dred_1682
OrganismDesulfotomaculum reducens (strain MI-1) [Complete proteome] [HAMAP]
Taxonomic identifier349161 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Clostridia › Clostridiales › Peptococcaceae › Desulfotomaculum

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Protein attributes

Sequence length427 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

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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.

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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...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 427427Dihydroorotase
PRO_1000071754

Sites

Metal binding591Zinc 1 By similarity
Metal binding611Zinc 1 By similarity
Metal binding1401Zinc 1; via carbamate group By similarity
Metal binding1401Zinc 2; via carbamate group By similarity
Metal binding1771Zinc 2 By similarity
Metal binding2301Zinc 2 By similarity
Metal binding3031Zinc 1 By similarity

Amino acid modifications

Modified residue1401N6-carboxylysine By similarity

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Sequences

Sequence LengthMass (Da)Tools
A4J556-1 [UniParc].

Last modified May 1, 2007. Version 1.
Checksum: D9A87C2646FBB20C

FASTA42745,864
        10         20         30         40         50         60 
MRYLIKGGIV VDPVADTLTC TDILVEEGMI KEIGQLSDSE AEVIAAEGNY VCPGFMDMHV 

        70         80         90        100        110        120 
HLREPGYEYK EDIVSGTRAA AMGGFTSVAC MPNTNPVADN AAIISHVLAK ARNAAARVFP 

       130        140        150        160        170        180 
IGALTKGSLG KELTEMADLK GAGAVALSDD GMPVMNADIM LRVMQYASML EMTVISHCED 

       190        200        210        220        230        240 
NKLSEGGQMH EGAVSAMLGL KGIPSLAEEI MVARDILLSE YTGCRLHLAH ISTEGSVRLV 

       250        260        270        280        290        300 
RQAKERGVPV TAEATPHHFT LTEEAVQGYS TNAKVNPPLR RQTDVEAIKE GLRDGTIDVI 

       310        320        330        340        350        360 
ATDHAPHAYH EKDVEFQYAP NGMIGLETAV GLIFTQLVQP GILTVPQAVA KLTCNPHRVL 

       370        380        390        400        410        420 
GLSGGRLLPG TPANITIIDP KLSEVVDPTK LLSKSKNTPF GRWKLTGLPV LTMKDGLLVM 


RDRQLLE

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References

[1]"Complete sequence of Desulfotomaculum reducens MI-1."
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., Sims D., Brettin T., Bruce D., Han C., Tapia R., Schmutz J., Larimer F. expand/collapse author list , Land M., Hauser L., Kyrpides N., Kim E., Tebo B.M., Richardson P.
Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

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Cross-references

Sequence databases

CP000612 Genomic DNA. Translation: ABO50209.1.
RefSeqYP_001113034.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID4957126.
GenomeReviewsGene locus Dred_1682 in contig CP000612_GR.
KEGGdrm:Dred_1682.

Organism-specific databases

CMRSearch...

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. 1 hit.
PS00483. DIHYDROOROTASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry namePYRC_DESRM
AccessionPrimary (citable) accession number: A4J556
Entry history
Integrated into UniProtKB/Swiss-Prot: February 26, 2008
Last sequence update: May 1, 2007
Last modified: September 2, 2008
This is version 12 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)

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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