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B7GFA5 (PYRC_ANOFW) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 23. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Dihydroorotase

Short name=DHOase
EC=3.5.2.3
Gene names
Name:pyrC
Ordered Locus Names:Aflv_1805
OrganismAnoxybacillus flavithermus (strain DSM 21510 / WK1) [Complete proteome] [HAMAP]
Taxonomic identifier491915 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacillalesBacillaceaeAnoxybacillus

Protein attributes

Sequence length428 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

(S)-dihydroorotate + H2O = N-carbamoyl-L-aspartate. HAMAP MF_00220_B

Cofactor

Binds 2 zinc ions per subunit By similarity. HAMAP MF_00220_B

Pathway

Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 3/3. HAMAP MF_00220_B

Subunit structure

Homodimer By similarity. HAMAP MF_00220_B

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: UniProtKB-KW

   Molecular functiondihydroorotase activity

Inferred from electronic annotation. Source: EC

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 428428Dihydroorotase HAMAP MF_00220_B
PRO_1000193087

Sites

Metal binding601Zinc 1 By similarity
Metal binding621Zinc 1 By similarity
Metal binding1421Zinc 1; via carbamate group By similarity
Metal binding1421Zinc 2; via carbamate group By similarity
Metal binding1791Zinc 2 By similarity
Metal binding2321Zinc 2 By similarity
Metal binding3051Zinc 1 By similarity

Amino acid modifications

Modified residue1421N6-carboxylysine By similarity

Sequences

Sequence LengthMass (Da)Tools
B7GFA5 [UniParc].

Last modified February 10, 2009. Version 1.
Checksum: 3AC41A200F42B912

FASTA42846,807
        10         20         30         40         50         60 
MATIFKRVRL LNEQGELIQT DIKVAGGRIV QIAHDLHAEA DDEVIDVDGQ FVAPGFVDVH 

        70         80         90        100        110        120 
VHLREPGGEH KETIATGTLA AAKGGFTTIA AMPNTKPVPD TKQHMEWLVN RIRETAHVRV 

       130        140        150        160        170        180 
LPYASITVRQ AGKQLVDFVA LKEAGAFAFT DDGVGVQSAR IMYEAMQQAA ALDMPIVAHC 

       190        200        210        220        230        240 
EDETLTYKGC VHDGSFAKRY GLSGIPSVCE SVHIARDVLL AEATGCHYHV CHISTKQSVR 

       250        260        270        280        290        300 
IVREAKQAGI RVTAEVTPHH LLLCDEDIPT LDANFKMNPP LRTKEDQQAL IEGLLDGTID 

       310        320        330        340        350        360 
FIATDHAPHT KEEKSEGMVL APFGIVGLET AFPLLYTHFV EKGICTLKQL VDWLSKKPAE 

       370        380        390        400        410        420 
TFRIDGGELK VGAKADFVVI DLHTEQAIDP NTFVSKGKNT PFAGWTCKGW PTMTIVAGKI 


VWQKGRGE 

« Hide

References

[1]"Encapsulated in silica: genome, proteome and physiology of the thermophilic bacterium Anoxybacillus flavithermus WK1."
Saw J.H., Mountain B.W., Feng L., Omelchenko M.V., Hou S., Saito J.A., Stott M.B., Li D., Zhao G., Wu J., Galperin M.Y., Koonin E.V., Makarova K.S., Wolf Y.I., Rigden D.J., Dunfield P.F., Wang L., Alam M.
Genome Biol. 9:R161.1-R161.16(2008) [PubMed: 19014707] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 21510 / WK1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000922 Genomic DNA. Translation: ACJ34166.1.
RefSeqYP_002316151.1. NC_011567.1.

3D structure databases

ProteinModelPortalB7GFA5.
ModBaseSearch...

Protein-protein interaction databases

STRINGB7GFA5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID7038058.
GenomeReviewsGene locus Aflv_1805 in contig CP000922_GR.
KEGGafl:Aflv_1805.
PATRIC20955495. VBIAnoFla45531_1856.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG724623.
ProtClustDBPRK09357.

Family and domain databases

HAMAPMF_00220_B. PyrC_type2_B.
[Tree]
InterProIPR006680. Amidohydro_1.
IPR004722. DHOase.
IPR002195. Dihydroorotase_CS.
IPR011059. Metal-dep_hydrolase_composite.
[Graphical view]
KOK01465.
PfamPF01979. Amidohydro_1. 1 hit.
[Graphical view]
SUPFAMSSF51338. Metalo_hydrolase. 1 hit.
TIGRFAMsTIGR00857. PyrC_multi. 1 hit.
PROSITEPS00482. DIHYDROOROTASE_1. 1 hit.
PS00483. DIHYDROOROTASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePYRC_ANOFW
AccessionPrimary (citable) accession number: B7GFA5
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: February 10, 2009
Last modified: January 25, 2012
This is version 23 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families