NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-21, FUNCTION, COFACTOR, SUBSTRATE SPECIFICITY, ENZYME REGULATION, AND MUTAGENESIS OF HIS-52 AND HIS-96.
STRAIN=KU-7;
DOI=10.1128/AEM.69.3.1564-1572.2003; PubMed=12620844 [NCBI, ExPASy, EBI, Israel, Japan]
Muraki T., Taki M., Hasegawa Y., Iwaki H., Lau P.C.K.;
"Prokaryotic homologs of the eukaryotic 3-hydroxyanthranilate 3,4-dioxygenase and 2-amino-3-carboxymuconate-6-semialdehyde decarboxylase in the 2-nitrobenzoate degradation pathway of Pseudomonas fluorescens strain KU-7.";
Appl. Environ. Microbiol. 69:1564-1572(2003).

Comments

FUNCTION: Catalyzes the oxidative ring opening of 3-hydroxyanthranilate to 2-amino-3-carboxymuconate semialdehyde, which spontaneously cyclizes to quinolinate.
CATALYTIC ACTIVITY: 3-hydroxyanthranilate + O₂ = 2-amino-3-carboxymuconate semialdehyde.
COFACTOR: Binds 2 Fe(2+) ions per subunit (Probable).
ENZYME REGULATION: Inhibited by Zn(2+), Cu(2+) and Cd(2+).
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

AB088043; BAC65311.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

SMR

Q83V26; 2-175.

ModBase

Q83V26.

Enzyme and pathway databases

BioCyc

MetaCyc:MON-13359; -.

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).
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.

Other

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

Keywords

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

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 185`	`185`	`3-hydroxyanthranilate 3,4-dioxygenase.`	`PRO_0000245472`
`METAL`	`52 52`		`Iron 1; catalytic (Probable).`
`METAL`	`58 58`		`Iron 1; catalytic (By similarity).`
`METAL`	`96 96`		`Iron 1; catalytic (Probable).`
`METAL`	`126 126`		`Iron 2 (By similarity).`
`METAL`	`129 129`		`Iron 2 (By similarity).`
`METAL`	`163 163`		`Iron 2 (By similarity).`
`METAL`	`166 166`		`Iron 2 (By similarity).`
`BINDING`	`48 48`		`Dioxygen (By similarity).`
`BINDING`	`58 58`		`Substrate (By similarity).`
`BINDING`	`100 100`		`Substrate (By similarity).`
`BINDING`	`111 111`		`Substrate (By similarity).`
`MUTAGEN`	`52 52`		`H->A: Loss of activity.`
`MUTAGEN`	`96 96`		`H->A: Loss of activity.`

Sequence information

Length: 185 AA [This is the length of the unprocessed precursor]

Molecular weight: 21245 Da [This is the MW of the unprocessed precursor]

CRC64: AC932875CC9D3D7D [This is a checksum on the sequence]

        10         20         30         40         50         60 
MMFTFGKPLN FQRWLDDHSD LLRPPVGNQQ VWQDSDFIVT VVGGPNFRTD FHDDPMEEFF 

        70         80         90        100        110        120 
YQFKGNAYLN IMDRGQMDRV ELKEGDIFLL PPHLRHSPQR PEAGSRCLVI ERQRPKGMLD 

       130        140        150        160        170        180 
GFEWYCLSCN GLVYRVDVQL NSIVTDLPPL FDIFYGNVGL RKCPQCGQVH PGKAAIEAVA 


RGDQP

Q83V26 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
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	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