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UniProtKB/Swiss-Prot entry Q8K9A4

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

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Entry information
Entry name RIBD1_BUCAP
Primary accession number Q8K9A4
Secondary accession numbers None
Integrated into Swiss-Prot on November 15, 2002
Sequence was last modified on October 1, 2002 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 43)
Name and origin of the protein
Protein name Diaminohydroxyphosphoribosylamino-pyrimidine deaminase
Synonyms DRAP deaminase
EC 3.5.4.26
Riboflavin-specific deaminase
Gene name
Name: ribD1
OrderedLocusNames: BUsg_445
From
Buchnera aphidicola subsp. Schizaphis graminum [TaxID: 98794] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; Enterobacteriaceae; Buchnera.
Protein existence 3: Inferred from homology;
References
[1]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1126/science.1071278; PubMed=12089438 [NCBI, ExPASy, EBI, Israel, Japan]
Tamas I., Klasson L., Canbaeck B., Naeslund A.K., Eriksson A.-S., Wernegreen J.J., Sandstroem J.P., Moran N.A., Andersson S.G.E.;
"50 million years of genomic stasis in endosymbiotic bacteria.";
Science 296:2376-2379(2002).
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
AE013218; AAM67988.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_660777.1; -.
3D structure databases
HSSP Q12178; 1UAQ. [HSSP ENTRY / PDB]
ModBase Q8K9A4.
Enzyme and pathway databases
BioCyc BAPH198804:BUSG445-MON; -.
Ontologies
GO
GO:0008703; Molecular function: 5-amino-6-(5-phosphoribosylamino)uracil reductase activity (inferred from electronic annotation from InterPro).
GO:0008835; Molecular function: diaminohydroxyphosphoribosylaminopyrimidine deaminase activity (inferred from electronic annotation from InterPro).
GO:0008270; Molecular function: zinc ion binding (inferred from electronic annotation from InterPro).
GO:0009231; Biological process: riboflavin biosynthetic process (inferred from electronic annotation from InterPro).
QuickGo view.
Family and domain databases
InterPro IPR016192; APOBEC/CMP_deaminase_Zn-bd.
IPR002125; CMP_dCMP_Zn_bd.
IPR004794; Eubact_ribD.
Graphical view of domain structure.
PANTHER PTHR11079:SF10; Eubact_ribD; 1.
Pfam PF00383; dCMP_cyt_deam_1; 1.
Pfam graphical view of domain structure.
TIGRFAMs TIGR00326; eubact_ribD; 1.
PROSITE PS00903; CYT_DCMP_DEAMINASES; 1.
ProtoNet Q8K9A4.
Genome annotation databases
GeneID 1005719; -.
GenomeReviews AE013218_GR; BUsg_445.
KEGG bas:BUsg445; -.
Phylogenomic databases
HOGENOM Q8K9A4; -.
Genome annotation databases
CMR Q8K9A4; BUsg_445.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Complete proteome; Hydrolase; Metal-binding; Riboflavin biosynthesis; Zinc.
Features
SEVIEWER logo Feature table viewer
KeyFrom  To Length Description FTId
CHAIN   1   147  147     Diaminohydroxyphosphoribosylamino-pyrimidine deaminase. PRO_0000171726
ACT_SITE   52    52        Proton donor (By similarity). 
METAL   50    50        Zinc; catalytic (By similarity). 
METAL   75    75        Zinc; catalytic (By similarity). 
METAL   84    84        Zinc; catalytic (By similarity). 
Sequence information
Length: 147 AA [This is the length of the unprocessed precursor] Molecular weight: 16233 Da [This is the MW of the unprocessed precursor] CRC64: EBCCF068610EECF0 [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MKDRFYMTRA IKLSKLGEFT TSPNPNVGCV IVQNKKIVGE GWHKKYGENH AEINALNMAG 

        70         80         90        100        110        120 
EKAKGSTAYI TLEPCNHFGK TPPCCDAIIQ SGIKNVIISS LDPNPKVSGK GVLYLRKKGI 

       130        140 
SVKIGLMSKE SQKYNKGFFK RMRTGLP
Q8K9A4 in FASTA format

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