ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!
Search for

UniProtKB/Swiss-Prot entry P46953

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

Note: most headings are clickable, even if they don't appear as links. They link to the user manual or other documents.
Entry information
Entry name 3HAO_RAT
Primary accession number P46953
Secondary accession numbers P70474 Q5RKK0 Q64556
Integrated into Swiss-Prot on November 1, 1995
Sequence was last modified on December 15, 1998 (Sequence version 2)
Annotations were last modified on    September 2, 2008 (Entry version 58)
Name and origin of the protein
Protein name 3-hydroxyanthranilate 3,4-dioxygenase
Synonyms EC 1.13.11.6
3-hydroxyanthranilic acid dioxygenase
3-hydroxyanthranilate oxygenase
3-HAO
Gene name
Name: Haao
From
Rattus norvegicus (Rat) [TaxID: 10116] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; Muroidea; Muridae; Murinae; Rattus.
Protein existence 1: Evidence at protein level;
References
[1]
 NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=Sprague-Dawley;
TISSUE=Liver;
PubMed=8541664 [NCBI, ExPASy, EBI, Israel, Japan]
Nakagawa Y., Asai H., Mori H., Kitoh J., Nakano K.;
"Increase in the level of mRNA for 3-hydroxyanthranilate 3,4-dioxygenase in brain of epilepsy-prone El mice.";
Biosci. Biotechnol. Biochem. 59:2191-2192(1995).
[2]
 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Kidney;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[3]
 PARTIAL NUCLEOTIDE SEQUENCE [MRNA] OF 44-236, AND PARTIAL PROTEIN SEQUENCE.
PubMed=7514594 [NCBI, ExPASy, EBI, Israel, Japan]
Malherbe P., Kohler C., da Prada M., Lang G., Kiefer V., Schwarcz R., Lahm H., Cesura A.M.;
"Molecular cloning and functional expression of human 3-hydroxyanthranilic-acid dioxygenase.";
J. Biol. Chem. 269:13792-13797(1994).
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
D44494; BAA07937.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC085739; AAH85739.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
D28339; BAA21019.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_064461.1; -.
UniGene Rn.48675
3D structure databases
ModBase P46953.
Organism-specific databases
RGD 71071; Haao.
Gene expression databases
ArrayExpress P46953; -.
GermOnline ENSRNOG00000031263; Rattus norvegicus.
Family and domain databases
InterPro IPR010329; 3hydroanth_dOase.
IPR016700; 3hydroanth_dOase_met.
Graphical view of domain structure.
Pfam PF06052; 3-HAO; 1.
Pfam graphical view of domain structure.
PIRSF PIRSF017681; 3hydroanth_dOase_animal; 1.
TIGRFAMs TIGR03037; anthran_nbaC; 1.
BLOCKS P46953.
Genome annotation databases
Ensembl ENSRNOG00000031263; Rattus norvegicus. [Contig view]
GeneID 56823; -.
KEGG rno:56823; -.
Phylogenomic databases
HOVERGEN P46953; -.
Other
ProtoNet P46953.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Cytoplasm; Dioxygenase; Direct protein sequencing; Iron; Metal-binding; Oxidoreductase.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   286  286     3-hydroxyanthranilate 3,4-dioxygenase. PRO_0000064374
METAL   47    47        Iron; catalytic (By similarity). 
METAL   53    53        Iron; catalytic (By similarity). 
METAL   91    91        Iron; catalytic (By similarity). 
BINDING   43    43        Dioxygen (By similarity). 
BINDING   53    53        Substrate (By similarity). 
BINDING   95    95        Substrate (By similarity). 
BINDING   105   105        Substrate (By similarity). 
CONFLICT   29    29        R -> Q (in Ref. 2; AAH85739). 
CONFLICT   44    44        K -> S (in Ref. 3; AA sequence). 
CONFLICT   199   199        S -> F (in Ref. 3; AA sequence). 
CONFLICT   204   204        G -> C (in Ref. 3; AA sequence). 
CONFLICT   214   214        H -> Y (in Ref. 3; AA sequence). 
CONFLICT   229   229        W -> P (in Ref. 3; AA sequence). 
Sequence information
Length: 286 AA [This is the length of the unprocessed precursor] Molecular weight: 32582 Da [This is the MW of the unprocessed precursor] CRC64: B4F535AD8949DAB7 [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MERCVRVKSW VEENRASFQP PVCNKLMHRE QLKIMFVGGP NTRKDYHIEE GEEVFYQLEG 

        70         80         90        100        110        120 
DMVLRVLEQG EHRDVVIRQG EIFLLPARVP HSPQRFANTM GLVIERRRME TELDGLRYYV 

       130        140        150        160        170        180 
GDTEDVLFEK WFHCKDLGTQ LAPIIQEFFH SEQYRTGKPN PDQLLKEPPF PLSTRSVMEP 

       190        200        210        220        230        240 
MSLKAWLESH SRELQAGTSL SLFGDSYETQ VIAHGQGSSK GPRQDVDVWL WQLEGSSKVT 

       250        260        270        280 
MGGQCVALAP DDSLLVPAGF SYMWERAQGS VALSVTQDPA CKKPLG
P46953 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

BLAST logo BLAST submission on ExPASy/SIB
or at NCBI (USA) 		Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
PROSITE logo ScanProsite, MotifScan SWISS-MODEL Submit a homology modeling request to SWISS-MODEL
NPSA logo NPSA Sequence analysis tools

ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Hosted by kr flag YPRC Korea Mirror sites: Australia Brazil Canada China Switzerland
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!