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Q6A916 (Q6A916_PROAC) Unreviewed, UniProtKB/TrEMBL

Last modified January 25, 2012. Version 57. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein names
EC=3.5.2.3 EMBL AAT82750.1
Gene names
Ordered Locus Names:PPA0998
OrganismPropionibacterium acnes (strain KPA171202 / DSM 16379) [Complete proteome] [HAMAP] EMBL AAT82750.1
Taxonomic identifier267747 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesPropionibacterineaePropionibacteriaceaePropionibacterium

Protein attributes

Sequence length445 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

(S)-dihydroorotate + H2O = N-carbamoyl-L-aspartate. SAAS SAAS002195

Cofactor

Binds 2 zinc ions per subunit By similarity. SAAS SAAS002195

Pathway

Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 3/3. SAAS SAAS002195

Subunit structure

Homodimer By similarity. SAAS SAAS002195

Sequences

Sequence LengthMass (Da)Tools
Q6A916 [UniParc].

Last modified September 13, 2004. Version 1.
Checksum: EEE2688B8EFCF3B5

FASTA44547,629
        10         20         30         40         50         60 
MSRRVLLTGL TMLVGATPVS SQLLIRDERI EAISRGRSNA LDGADAEVVD LGGALVTPGM 

        70         80         90        100        110        120 
VDLHVHLREP GQEHKETIAS GTAAAARGGW TTICAMPNTV PDPHSPELMA DLNRRVEESA 

       130        140        150        160        170        180 
VVRVLPIAPI TVGLTGNDLV DVEALTRAGA VAFSNDGKGV QLAGVMYDAM RSAAAVDRPI 

       190        200        210        220        230        240 
AAHAEDESLV RGGVINDGRR ARELGLPPMT RLTETVQVAR DVMIAEETGA HYHLCHASTR 

       250        260        270        280        290        300 
QSIRTLRRGR EDGANVTGEA APHHLLLADD DIPDDDGFYK MNPPLRTRDD LNAMVEGLCD 

       310        320        330        340        350        360 
GTLTCIATDN APHAAEEKAC SFRDAAFGVI TNEHTFALLY TNFVLDRRFR LDQLVDWLTI 

       370        380        390        400        410        420 
GPAETFGIPE AGRLRVGGPA DLAAFDLRTE MTIIPGDGAG MGRNTPFAGR SVRGDCVLTM 

       430        440 
VGGQTVYRRG QPIGKTDDHE MGDPQ 

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References

[1]"The complete genome sequence of Propionibacterium acnes, a commensal of human skin."
Brueggemann H., Henne A., Hoster F., Liesegang H., Wiezer A., Strittmatter A., Hujer S., Duerre P., Gottschalk G.
Science 305:671-673(2004) [PubMed: 15286373] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: KPA171202 / DSM 16379.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE017283 Genomic DNA. Translation: AAT82750.1.
RefSeqYP_055708.1. NC_006085.1.

3D structure databases

ProteinModelPortalQ6A916.
ModBaseSearch...

Protein family/group databases

MEROPSM38.972.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID2931026.
GenomeReviewsGene locus PPA0998 in contig AE017283_GR.
KEGGpac:PPA0998.
NMPDRfig|267747.1.peg.985.
PATRIC23036721. VBIProAcn64440_1033.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG724623.
OMAILGFNEH.
PhylomeDBQ6A916.
ProtClustDBCLSK2763657.

Enzyme and pathway databases

BioCycPACN267747:PPA0998-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 nameQ6A916_PROAC
AccessionPrimary (citable) accession number: Q6A916
Entry history
Integrated into UniProtKB/TrEMBL: September 13, 2004
Last sequence update: September 13, 2004
Last modified: January 25, 2012
This is version 57 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)