[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

FUNCTION: Catalyzes the synthesis of the excitotoxin quinolinic acid (QUIN) from 3-hydroxyanthranilic acid. The direct product of the reaction spontaneously rearranges to QUIN.
CATALYTIC ACTIVITY: 3-hydroxyanthranilate + O₂ = 2-amino-3-carboxymuconate semialdehyde.
COFACTOR: Fe(2+) ion.
SUBUNIT: Monomer.
SUBCELLULAR LOCATION: Cytoplasm.
SIMILARITY: Belongs to the 3-HAO family.

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.

Ontologies

GO:0005737;	Cellular component: cytoplasm (inferred from electronic annotation from InterPro).
GO:0000334;	Molecular function: 3-hydroxyanthranilate 3,4-dioxygenase activity (inferred from electronic annotation from InterPro).
GO:0005506;	Molecular function: iron ion binding (inferred from electronic annotation from InterPro).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

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.

ProtoNet

P46953.

Genome annotation databases

Ensembl

ENSRNOG00000031263; Rattus norvegicus. [Contig view]

GeneID

56823; -.

KEGG

rno:56823; -.

Phylogenomic databases

HOVERGEN

P46953; -.

Other

NextBio

611253; -.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Cytoplasm; Dioxygenase; Direct protein sequencing; Iron; Metal-binding; Oxidoreductase; Phosphoprotein.

Features

Feature table viewer

`Key`	`From 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).`
`MOD_RES`	`9 9`		`Phosphoserine (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 submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools