Skip Header

Contribute Send feedback
Read comments (?) or add your own

Q8NQ39 (PYRC_CORGL) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 63. 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:Cgl1611, cg1815
OrganismCorynebacterium glutamicum (Brevibacterium flavum)
Taxonomic identifier1718 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeCorynebacteriaceaeCorynebacterium

Protein attributes

Sequence length447 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
Reference 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 – 447447Dihydroorotase HAMAP MF_00220_B
PRO_0000147232

Sites

Metal binding731Zinc 1 By similarity
Metal binding751Zinc 1 By similarity
Metal binding1941Zinc 2 By similarity
Metal binding2471Zinc 2 By similarity
Metal binding3201Zinc 1 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8NQ39 [UniParc].

Last modified October 1, 2002. Version 1.
Checksum: 5AAD2377CF5F6572

FASTA44747,827
        10         20         30         40         50         60 
MVDSNTQYPE TGALAPAPAD SLLISNVLVY GEGEPTNVFV KDGVIAAIGG THEADRTIDG 

        70         80         90        100        110        120 
NGGVLLPGFV DMHVHLREPG REDTETIATG SAAAAKGGFT AVFTMANTTP VMDQPVIAES 

       130        140        150        160        170        180 
VWFKGQNIGL CDVHPVGSIT KGLEGKELTE FGMMARSEAK VRMFSDDGKC VDDPQVMRRA 

       190        200        210        220        230        240 
LEYAKGMDVL IAQHAEDHRL TEGASAHEGE NAARLGLRGW PRVAEESIVV RDAIMARDYG 

       250        260        270        280        290        300 
NRVHICHAST EGTVELLRWA KSQGIPITAE VTPHHLTLTD ERLETYDAVN KVNPPLRESR 

       310        320        330        340        350        360 
DAEALKKALL DGTIDVVATD HAPHGSEDKC CEFENAKPGM LGLETSLSII VDTFVATGLA 

       370        380        390        400        410        420 
DWRFVARVMS ERPAEITRLP GQGRPIAEGE PANLAIVDPG KTWTASGADF ASKAENTPFE 

       430        440 
GQEFSAKVTH TVLRGKVTCA DGVAQNA 

« Hide

References

[1]"Complete genomic sequence of Corynebacterium glutamicum ATCC 13032."
Nakagawa S.
Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025.
[2]"The complete Corynebacterium glutamicum ATCC 13032 genome sequence and its impact on the production of L-aspartate-derived amino acids and vitamins."
Kalinowski J., Bathe B., Bartels D., Bischoff N., Bott M., Burkovski A., Dusch N., Eggeling L., Eikmanns B.J., Gaigalat L., Goesmann A., Hartmann M., Huthmacher K., Kraemer R., Linke B., McHardy A.C., Meyer F., Moeckel B. expand/collapse author list , Pfefferle W., Puehler A., Rey D.A., Rueckert C., Rupp O., Sahm H., Wendisch V.F., Wiegraebe I., Tauch A.
J. Biotechnol. 104:5-25(2003) [PubMed: 12948626] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000036 Genomic DNA. Translation: BAB99004.1.
BX927152 Genomic DNA. Translation: CAF21620.1.
RefSeqNP_600825.1. NC_003450.3.
YP_225896.1. NC_006958.1.

3D structure databases

ProteinModelPortalQ8NQ39.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1019579.
3343550.
GenomeReviewsGene locus Cgl1611 in contig BA000036_GR.
Gene locus cg1815 in contig BX927147_GR.
KEGGcgb:cg1815.
cgl:NCgl1549.
PATRIC21495259. VBICorGlu203724_1573.

Phylogenomic databases

HOGENOMHBG724623.
OMACDVHPVG.
PhylomeDBQ8NQ39.
ProtClustDBPRK09357.

Enzyme and pathway databases

BioCycCGLU196627:CG1815-MONOMER.

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_CORGL
AccessionPrimary (citable) accession number: Q8NQ39
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 2003
Last sequence update: October 1, 2002
Last modified: January 25, 2012
This is version 63 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