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Reviewed, UniProtKB/Swiss-Prot Q5WFJ0 (PYRC_BACSK)

Last modified September 2, 2008. Version 25. 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: ABC2335
OrganismBacillus clausii (strain KSM-K16) [Complete proteome] [HAMAP]
Taxonomic identifier66692 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacillalesBacillaceaeBacillus

Protein attributes

Sequence length427 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 – 427427Dihydroorotase
PRO_0000325587

Sites

Metal binding571Zinc 1 By similarity
Metal binding591Zinc 1 By similarity
Metal binding1391Zinc 1; via carbamate group By similarity
Metal binding1391Zinc 2; via carbamate group By similarity
Metal binding1761Zinc 2 By similarity
Metal binding2291Zinc 2 By similarity
Metal binding3021Zinc 1 By similarity

Amino acid modifications

Modified residue1391N6-carboxylysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5WFJ0-1 [UniParc].

Last modified November 23, 2004. Version 1.
Checksum: C207AABD1D32A4CC

FASTA42745,862
        10         20         30         40         50         60 
MAMKVTGGFI LDENGEQVAK DVYIKDGKIV EHVADGDIRQ QFDATGLLIS PGFVDVHVHL 

        70         80         90        100        110        120 
REPGGEKKET IETGTKAAAR GGFTTVAAMP NTRPVPDNAE QLDLLQARIS ETAVVRVLPY 

       130        140        150        160        170        180 
ASITTRQLGQ ELTDFKALKE AGAFAFTDDG VGIQEAGMML SAMKEAAALN MAVVAHCEDN 

       190        200        210        220        230        240 
SLINGGAVHE GHYAKAHGLN GIPSVCEAVH IARDVLLAEA AGAHYHVCHV STKESVRTIR 

       250        260        270        280        290        300 
DAKKAGIRVT AEVTPHHLLL CEDDIIGKDP NFKMNPPLRA KEDRDALVAG LLDGTIDFIA 

       310        320        330        340        350        360 
TDHAPHTAEE KSASLERAPF GIVGLETAFP LLYTHFVKPG TFTLKQLIDW LTVKPAQTFN 

       370        380        390        400        410        420 
LPYGTLQVGA AADLTLIDLK ANETIDPSMF LSKGKNTPFA GWDCAGIPQA TMVAGKTVYK 


KERITNE 

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References

[1]"The complete genome sequence of the alkaliphilic Bacillus clausii KSM-K16."
Takaki Y., Kageyama Y., Shimamura S., Suzuki H., Nishi S., Hatada Y., Kawai S., Ito S., Horikoshi K.
Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

AP006627 Genomic DNA. Translation: BAD64870.1.
RefSeqYP_175831.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID3202825.
GenomeReviewsGene locus ABC2335 in contig AP006627_GR.
KEGGbcl:ABC2335.
NMPDRfig|66692.3.peg.2023.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ5WFJ0.

Enzyme and pathway databases

BioCycBCLA66692:ABC2335-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. 1 hit.
PS00483. DIHYDROOROTASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePYRC_BACSK
AccessionPrimary (citable) accession number: Q5WFJ0
Entry history
Integrated into UniProtKB/Swiss-Prot: March 18, 2008
Last sequence update: November 23, 2004
Last modified: September 2, 2008
This is version 25 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