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UniProtKB/Swiss-Prot entry Q6FD29

[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name PYRC_ACIAD
Primary accession number Q6FD29
Secondary accession numbers None
Integrated into Swiss-Prot on January 15, 2008
Sequence was last modified on July 19, 2004 (Sequence version 1)
Annotations were last modified on    September 2, 2008 (Entry version 25)
Name and origin of the protein
Protein name Dihydroorotase
Synonyms DHOase
EC 3.5.2.3
Gene name
Name: pyrC
OrderedLocusNames: ACIAD1150
From
Acinetobacter sp. (strain ADP1) [TaxID: 62977] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; Moraxellaceae; Acinetobacter.
Protein existence 3: Inferred from homology;
References
[1]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1093/nar/gkh910; PubMed=15514110 [NCBI, ExPASy, EBI, Israel, Japan]
Barbe V., Vallenet D., Fonknechten N., Kreimeyer A., Oztas S., Labarre L., Cruveiller S., Robert C., Duprat S., Wincker P., Ornston L.N., Weissenbach J., Marliere P., Cohen G.N., Medigue C.;
"Unique features revealed by the genome sequence of Acinetobacter sp. ADP1, a versatile and naturally transformation competent bacterium.";
Nucleic Acids Res. 32:5766-5779(2004).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
CR543861; CAG68030.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq YP_045852.1; -.
3D structure databases
ModBase Q6FD29.
Enzyme and pathway databases
BioCyc ASP62977:ACIAD1150-MON; -.
Ontologies
GO
GO:0004151; Molecular function: dihydroorotase activity (inferred from electronic annotation from HAMAP).
GO:0008270; Molecular function: zinc ion binding (inferred from electronic annotation from HAMAP).
GO:0006221; Biological process: pyrimidine nucleotide biosynthetic process (inferred from electronic annotation from HAMAP).
QuickGo view.
Family and domain databases
HAMAP MF_00219; -; 1.
PBIL [Tree]
InterPro IPR006680; Amidohydro_1.
IPR004721; DHOdimr.
IPR002195; Dihydroorotase_CS.
Graphical view of domain structure.
Pfam PF01979; Amidohydro_1; 1.
Pfam graphical view of domain structure.
PIRSF PIRSF001237; DHOdimr; 1.
TIGRFAMs TIGR00856; pyrC_dimer; 1.
PROSITE PS00482; DIHYDROOROTASE_1; 1.
PS00483; DIHYDROOROTASE_2; 1.
BLOCKS Q6FD29.
Genome annotation databases
GeneID 2879564; -.
GenomeReviews CR543861_GR; ACIAD1150.
KEGG aci:ACIAD1150; -.
NMPDR fig|62977.3.peg.65; -.
Phylogenomic databases
HOGENOM Q6FD29; -.
Genome annotation databases
CMR Q6FD29; ACIAD1150.
Other
ProtoNet Q6FD29.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Complete proteome; Hydrolase; Metal-binding; Pyrimidine biosynthesis; Zinc.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   344  344     Dihydroorotase. PRO_1000024007
METAL   13    13        Zinc 1 (By similarity). 
METAL   15    15        Zinc 1 (By similarity). 
METAL   99    99        Zinc 1; via carbamate group (By similarity). 
METAL   99    99        Zinc 2; via carbamate group (By similarity). 
METAL   136   136        Zinc 2 (By similarity). 
METAL   174   174        Zinc 2 (By similarity). 
METAL   247   247        Zinc 1 (By similarity). 
MOD_RES   99    99        N6-carboxylysine (By similarity). 
Sequence information
Length: 344 AA [This is the length of the unprocessed precursor] Molecular weight: 38867 Da [This is the MW of the unprocessed precursor] CRC64: DE11304473479E6E [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MDTITLLQPD DWHAHLRDGL ALKRTVPDLA QQFARAICMP NLVPPVKTVD EAEAYRERIM 

        70         80         90        100        110        120 
AHVPEGVHFD PRMVLYFTDH TSPSEVKKIK DSAHVNAIKL YPAGATTNSD NGVSDIRKVY 

       130        140        150        160        170        180 
AVIEQLEEHQ VPLLLHGEVT HHHVDIFDRE KRFLDEVLSP LLKQFPKLKL VLEHITTSEA 

       190        200        210        220        230        240 
AHFVLEQDRN VAATITPQHL LFNRNDMLVG GIKPHFYCLP ILKRQTHQQT LIEVATSGNP 

       250        260        270        280        290        300 
KFFLGTDSAP HSKNAKENAC GCAGCYSAPT AIELYAQAFD QVNKIERLEG FASHFGADFY 

       310        320        330        340 
GLPRNTNTIT LVKEDQIIPE QLDYLDDEKI IPLYAGKTIQ WRKV
Q6FD29 in FASTA format

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