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B0CF78 (PYRC_ACAM1) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 30. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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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:AM1_5644
OrganismAcaryochloris marina (strain MBIC 11017) [Complete proteome] [HAMAP]
Taxonomic identifier329726 [NCBI]
Taxonomic lineageBacteria › Cyanobacteria › Chroococcales › Acaryochloris

Protein attributes

Sequence length345 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

(S)-dihydroorotate + H2O = N-carbamoyl-L-aspartate. HAMAP MF_00219

Cofactor

Binds 2 zinc ions per subunit By similarity. HAMAP MF_00219

Pathway

Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 3/3. HAMAP MF_00219

Subunit structure

Homodimer By similarity. HAMAP MF_00219

Sequence similarities

Belongs to the DHOase family. Type 1 subfamily.

Ontologies

Keywords
   Biological processPyrimidine biosynthesis
   LigandMetal-binding
Zinc
   Molecular functionHydrolase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processpyrimidine base biosynthetic process

Inferred from electronic annotation. Source: InterPro

pyrimidine 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 – 345345Dihydroorotase HAMAP MF_00219
PRO_1000078095

Sites

Metal binding131Zinc 1 By similarity
Metal binding151Zinc 1 By similarity
Metal binding991Zinc 1; via carbamate group By similarity
Metal binding991Zinc 2; via carbamate group By similarity
Metal binding1361Zinc 2 By similarity
Metal binding1741Zinc 2 By similarity
Metal binding2471Zinc 1 By similarity

Amino acid modifications

Modified residue991N6-carboxylysine By similarity

Sequences

Sequence LengthMass (Da)Tools
B0CF78 [UniParc].

Last modified February 26, 2008. Version 1.
Checksum: F512F4502DA91F41

FASTA34538,498
        10         20         30         40         50         60 
MQKLTLTRPD DWHLHLRDGD ALKAVLPHSA RQFARAIVMP NLKPPVRTVA DAADYRNRIL 

        70         80         90        100        110        120 
AALPVGQTFE PLMTLYLTDN TSPEEISAAK ASKFVKAVKY YPAGATTNSD FGVTDIRKCD 

       130        140        150        160        170        180 
RIFAAMEQED IPLLLHGEVT DTNIDVFDRE KVFIETHLIP LVSRFPKLRV VLEHITTSEA 

       190        200        210        220        230        240 
VTFVLNTNEN IGATITPQHL LFSRNAIFKG GIRPHYYCLP ILKREKHRQA LLQAATSGNP 

       250        260        270        280        290        300 
KFFLGTDSAP HARNSKEQSC GCAGCYSALH AMELYAEAFE SANALDKLEA FASFYGPDFY 

       310        320        330        340 
QLPRNTKTIT LAKQTWQIPD EVPFPGTGLV PLRAGEEITW KIMDG

« Hide

References

[1]"Niche adaptation and genome expansion in the chlorophyll d-producing cyanobacterium Acaryochloris marina."
Swingley W.D., Chen M., Cheung P.C., Conrad A.L., Dejesa L.C., Hao J., Honchak B.M., Karbach L.E., Kurdoglu A., Lahiri S., Mastrian S.D., Miyashita H., Page L., Ramakrishna P., Satoh S., Sattley W.M., Shimada Y., Taylor H.L. expand/collapse author list , Tomo T., Tsuchiya T., Wang Z.T., Raymond J., Mimuro M., Blankenship R.E., Touchman J.W.
Proc. Natl. Acad. Sci. U.S.A. 105:2005-2010(2008) [PubMed: 18252824] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: MBIC 11017.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000828 Genomic DNA. Translation: ABW30594.1.
RefSeqYP_001519913.1. NC_009925.1.

3D structure databases

ProteinModelPortalB0CF78.
SMRB0CF78. Positions 2-342.
ModBaseSearch...

Protein-protein interaction databases

STRINGB0CF78.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5684434.
GenomeReviewsGene locus AM1_5644 in contig CP000828_GR.
KEGGamr:AM1_5644.
PATRIC20625270. VBIAcaMar40141_5240.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG628648.
OMACLPVAKR.
PhylomeDBB0CF78.
ProtClustDBPRK05451.

Enzyme and pathway databases

BioCycAMAR329726:AM1_5644-MONOMER.

Family and domain databases

HAMAPMF_00219. PyrC_type1.
[Tree]
InterProIPR006680. Amidohydro_1.
IPR004721. DHOdimr.
IPR002195. Dihydroorotase_CS.
[Graphical view]
KOK01465.
PfamPF01979. Amidohydro_1. 1 hit.
[Graphical view]
PIRSFPIRSF001237. DHOdimr. 1 hit.
TIGRFAMsTIGR00856. PyrC_dimer. 1 hit.
PROSITEPS00482. DIHYDROOROTASE_1. 1 hit.
PS00483. DIHYDROOROTASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePYRC_ACAM1
AccessionPrimary (citable) accession number: B0CF78
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: February 26, 2008
Last modified: January 25, 2012
This is version 30 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

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