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

Last modified April 16, 2014. Version 104. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
3-hydroxyanthranilate 3,4-dioxygenase

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

Protein attributes

Sequence length286 AA.
Sequence statusComplete.
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. HAMAP-Rule MF_03019

Catalytic activity

3-hydroxyanthranilate + O2 = 2-amino-3-carboxymuconate semialdehyde. HAMAP-Rule MF_03019

Cofactor

Fe2+ ion By similarity. HAMAP-Rule MF_03019

Pathway

Cofactor biosynthesis; NAD(+) biosynthesis; quinolinate from L-kynurenine: step 3/3. HAMAP-Rule MF_03019

Subunit structure

Monomer By similarity. HAMAP-Rule MF_03019

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_03019.

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 HAMAP-Rule MF_03019
PRO_0000064374

Regions

Region1 – 160160Domain A (catalytic) By similarity
Region161 – 17717Linker By similarity
Region178 – 286109Domain B By similarity

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

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 [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: PARTIAL NUCLEOTIDE SEQUENCE [MRNA] OF 44-236, PARTIAL PROTEIN SEQUENCE.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D44494 mRNA. Translation: BAA07937.1.
BC085739 mRNA. Translation: AAH85739.1.
D28339 mRNA. Translation: BAA21019.1.
RefSeqNP_064461.1. NM_020076.2.
UniGeneRn.48675.

3D structure databases

ProteinModelPortalP46953.
SMRP46953. Positions 2-286.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

MINTMINT-4569623.

PTM databases

PhosphoSiteP46953.

Proteomic databases

PaxDbP46953.
PRIDEP46953.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000045996; ENSRNOP00000043835; ENSRNOG00000031263.
GeneID56823.
KEGGrno:56823.
UCSCRGD:71071. rat.

Organism-specific databases

CTD23498.
RGD71071. Haao.

Phylogenomic databases

eggNOGNOG77058.
GeneTreeENSGT00390000013008.
HOGENOMHOG000218448.
HOVERGENHBG000018.
KOK00452.
OrthoDBEOG7FFMS4.
PhylomeDBP46953.
TreeFamTF300246.

Enzyme and pathway databases

UniPathwayUPA00253; UER00330.

Gene expression databases

GenevestigatorP46953.

Family and domain databases

Gene3D2.60.120.10. 2 hits.
HAMAPMF_00825. 3_HAO.
InterProIPR010329. 3hydroanth_dOase.
IPR016700. 3hydroanth_dOase_met.
IPR014710. RmlC-like_jellyroll.
IPR011051. RmlC_Cupin.
[Graphical view]
PfamPF06052. 3-HAO. 1 hit.
[Graphical view]
PIRSFPIRSF017681. 3hydroanth_dOase_animal. 1 hit.
SUPFAMSSF51182. SSF51182. 2 hits.
TIGRFAMsTIGR03037. anthran_nbaC. 1 hit.
ProtoNetSearch...

Other

NextBio611253.
PROP46953.

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: April 16, 2014
This is version 104 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways