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: Binds 2 Fe(2+) ions per subunit (By similarity).
SUBUNIT: Homodimer (By similarity).
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

CP000050; AAY49728.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

YP_243748.1; -.

3D structure databases

ModBase

Q4UT95.

Enzyme and pathway databases

BioCyc

XCAM314565:XC_2679-MON; -.

Ontologies

GO:0000334;	Molecular function: 3-hydroxyanthranilate 3,4-dioxygenase activity (inferred from electronic annotation from HAMAP).
GO:0008198;	Molecular function: ferrous iron binding (inferred from electronic annotation from HAMAP).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

HAMAP

MF_00825; -; 1.
PBIL [Tree]

InterPro

IPR010329; 3hydroanth_dOase.
Graphical view of domain structure.

Pfam

PF06052; 3-HAO; 1.
Pfam graphical view of domain structure.

TIGRFAMs

TIGR03037; anthran_nbaC; 1.

Genome annotation databases

GeneID

3381213; -.

GenomeReviews

CP000050_GR; XC_2679.

KEGG

xcb:XC_2679; -.

Phylogenomic databases

HOGENOM

Q4UT95; -.

Genome annotation databases

CMR

Q4UT95; XC_2679.

Other

UniRef

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

Keywords

Complete proteome; Dioxygenase; Iron; Metal-binding; Oxidoreductase.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 176`	`176`	`3-hydroxyanthranilate 3,4-dioxygenase.`	`PRO_0000245481`
`METAL`	`48 48`		`Iron 1; catalytic (By similarity).`
`METAL`	`54 54`		`Iron 1; catalytic (By similarity).`
`METAL`	`92 92`		`Iron 1; catalytic (By similarity).`
`METAL`	`121 121`		`Iron 2 (By similarity).`
`METAL`	`124 124`		`Iron 2 (By similarity).`
`METAL`	`158 158`		`Iron 2 (By similarity).`
`METAL`	`161 161`		`Iron 2 (By similarity).`
`BINDING`	`44 44`		`Dioxygen (By similarity).`
`BINDING`	`54 54`		`Substrate (By similarity).`
`BINDING`	`96 96`		`Substrate (By similarity).`
`BINDING`	`106 106`		`Substrate (By similarity).`

Sequence information

Length: 176 AA [This is the length of the unprocessed precursor]

Molecular weight: 20128 Da [This is the MW of the unprocessed precursor]

CRC64: 3C2FDD218C8458D4 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MLVPPINLHA WVEQHRHLLK PPVGNKCIQQ DGFIIMIVGG PNARTDYHYD EGPEWFFQLE 

        70         80         90        100        110        120 
GEMVLKVQDD GTARDIPIRA GEIFLLPPKV PHSPQRAAGS IGLVIERERL PHEQDGLQWY 

       130        140        150        160        170 
CPQCNHKLYE AMFPLENIET DFPPVFDHFY RSLALRTCTQ CGHVHPAPER YAAVEA

Q4UT95 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