Reviewed, UniProtKB/Swiss-Prot Q83V26 (3HAO_PSEFL)

Names and origin

Protein names

Recommended 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:

nbaC

Organism

Pseudomonas fluorescens

Taxonomic identifier

294 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Pseudomonadaceae › Pseudomonas

Protein attributes

Sequence length	185 AA.
Sequence status	Complete.
Protein existence	Evidence 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. Ref.1
Catalytic activity	3-hydroxyanthranilate + O2 = 2-amino-3-carboxymuconate semialdehyde. HAMAP MF_00825
Cofactor	Binds 2 Fe2+ ions per subunit Probable. Ref.1
Enzyme regulation	Inhibited by Zn2+, Cu2+ and Cd2+. Ref.1
Subunit structure	Homodimer By similarity. HAMAP MF_00825
Sequence similarities	Belongs to the 3-HAO family.

Ontologies

Keywords
Ligand	Iron Metal-binding
Molecular function	Dioxygenase Oxidoreductase
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	3-hydroxyanthranilate 3,4-dioxygenase activity Inferred from electronic annotation. Source: HAMAP ferrous iron binding Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 185	185	3-hydroxyanthranilate 3,4-dioxygenase HAMAP MF_00825		PRO_0000245472
Sites
	Metal binding	52	1	Iron 1; catalytic Probable
	Metal binding	58	1	Iron 1; catalytic By similarity
	Metal binding	96	1	Iron 1; catalytic Probable
	Metal binding	126	1	Iron 2 By similarity
	Metal binding	129	1	Iron 2 By similarity
	Metal binding	163	1	Iron 2 By similarity
	Metal binding	166	1	Iron 2 By similarity
	Binding site	48	1	Dioxygen By similarity
	Binding site	58	1	Substrate By similarity
	Binding site	100	1	Substrate By similarity
	Binding site	111	1	Substrate By similarity
Experimental info
	Mutagenesis	52	1	H → A: Loss of activity. Ref.1
	Mutagenesis	96	1	H → A: Loss of activity. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q83V26-1 [UniParc]. Last modified June 1, 2003. Version 1. Checksum: AC932875CC9D3D7D	FASTA	185	21,245
	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

References

[1]

"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." Muraki T., Taki M., Hasegawa Y., Iwaki H., Lau P.C.K. Appl. Environ. Microbiol. 69:1564-1572(2003) [PubMed: 12620844] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-21, FUNCTION, COFACTOR, SUBSTRATE SPECIFICITY, ENZYME REGULATION, MUTAGENESIS OF HIS-52 AND HIS-96. Strain: KU-7.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AB088043 Genomic DNA. Translation: BAC65311.1.
3D structure databases
SMR	Q83V26. Positions 2-175.
ModBase	Search...
Enzyme and pathway databases
BioCyc	MetaCyc:MONOMER-13359.
BRENDA	1.13.11.6. 329.
Family and domain databases
HAMAP	MF_00825. 3_HAO. [Tree]
InterPro	IPR010329. 3hydroanth_dOase. IPR011051. Cupin_RmlC_type. [Graphical view]
Pfam	PF06052. 3-HAO. 1 hit. [Graphical view]
TIGRFAMs	TIGR03037. anthran_nbaC. 1 hit.
ProtoNet	Search...

Entry information

Entry name

3HAO_PSEFL

Accession

Primary (citable) accession number: Q83V26

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 11, 2006
Last sequence update:	June 1, 2003
Last modified:	February 9, 2010
This is version 34 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)