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Reviewed, UniProtKB/Swiss-Prot P46953 (3HAO_RAT)

Last modified June 16, 2009. Version 66. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    3-hydroxyanthranilate 3,4-dioxygenase
    EC=1.13.11.6
Alternative name(s):
    3-hydroxyanthranilic acid dioxygenase
      Short name=HAD
    3-hydroxyanthranilate oxygenase
      Short name=3-HAO
Gene names
Name: Haao
OrganismRattus norvegicus (Rat)
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length286 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Catalyzes the oxidative ring opening of 3-hydroxyanthranilate to 2-amino-3-carboxymuconate semialdehyde, which spontaneously cyclizes to quinolinate By similarity.

Catalytic activity

3-hydroxyanthranilate + O2 = 2-amino-3-carboxymuconate semialdehyde.

Cofactor

Fe2+ ion By similarity.

Pathway

Cofactor biosynthesis; NAD(+) biosynthesis; pyridine-2,3-dicarboxylate from L-kynurenine: step 3/3.

Subunit structure

Monomer By similarity.

Subcellular location

Cytoplasm By similarity.

Sequence similarities

Belongs to the 3-HAO family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 2862863-hydroxyanthranilate 3,4-dioxygenase
PRO_0000064374

Sites

Metal binding471Iron; catalytic By similarity
Metal binding531Iron; catalytic By similarity
Metal binding911Iron; catalytic By similarity
Binding site431Dioxygen By similarity
Binding site531Substrate By similarity
Binding site951Substrate By similarity
Binding site1051Substrate By similarity

Amino acid modifications

Modified residue91Phosphoserine By similarity

Experimental info

Sequence conflict291R → Q in AAH85739. Ref.2
Sequence conflict441K → S AA sequence Ref.3
Sequence conflict1991S → F AA sequence Ref.3
Sequence conflict2041G → C AA sequence Ref.3
Sequence conflict2141H → Y AA sequence Ref.3
Sequence conflict2291W → P AA sequence Ref.3

Sequences

Sequence LengthMass (Da)Tools
P46953-1 [UniParc].

Last modified December 15, 1998. Version 2.
Checksum: B4F535AD8949DAB7

FASTA28632,582
        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 

« Hide

References

« Hide 'large scale' references
[1]"Increase in the level of mRNA for 3-hydroxyanthranilate 3,4-dioxygenase in brain of epilepsy-prone El mice."
Nakagawa Y., Asai H., Mori H., Kitoh J., Nakano K.
Biosci. Biotechnol. Biochem. 59:2191-2192(1995) [PubMed: 8541664] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: Sprague-Dawley.
Tissue: Liver.
[2]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Kidney.
[3]"Molecular cloning and functional expression of human 3-hydroxyanthranilic-acid dioxygenase."
Malherbe P., Kohler C., da Prada M., Lang G., Kiefer V., Schwarcz R., Lahm H., Cesura A.M.
J. Biol. Chem. 269:13792-13797(1994) [PubMed: 7514594] [Abstract]
Cited for: PARTIAL NUCLEOTIDE SEQUENCE [MRNA] OF 44-236, PARTIAL PROTEIN SEQUENCE.

Cross-references

Sequence databases

D44494 mRNA. Translation: BAA07937.1.
BC085739 mRNA. Translation: AAH85739.1.
D28339 mRNA. Translation: BAA21019.1.
IPIIPI00339188.
RefSeqNP_064461.1.
UniGeneRn.48675

3D structure databases

ModBaseSearch...

Proteomic databases

PRIDEP46953.

Genome annotation databases

EnsemblENSRNOG00000031263. Rattus norvegicus. [Contig view]
GeneID56823.
KEGGrno:56823.

Organism-specific databases

RGD71071. Haao.

Phylogenomic databases

HOVERGENP46953.

Enzyme and pathway databases

BRENDA1.13.11.6. 248.

Gene expression databases

ArrayExpressP46953.
GermOnlineENSRNOG00000031263. Rattus norvegicus.

Family and domain databases

InterProIPR010329. 3hydroanth_dOase.
IPR016700. 3hydroanth_dOase_met.
[Graphical view]
PfamPF06052. 3-HAO. 1 hit.
[Graphical view]
PIRSFPIRSF017681. 3hydroanth_dOase_animal. 1 hit.
TIGRFAMsTIGR03037. anthran_nbaC. 1 hit.
ProtoNetSearch...

Other Resources

NextBio611253.

Entry information

Entry name3HAO_RAT
AccessionPrimary (citable) accession number: P46953
Secondary accession number(s): P70474, Q5RKK0, Q64556
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: December 15, 1998
Last modified: June 16, 2009
This is version 66 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents