Q5H043 (3HAO_XANOR) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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:	nbaC
Ordered Locus Names:	XOO2424

Organism

Xanthomonas oryzae pv. oryzae (strain KACC10331 / KXO85) [Complete proteome] [HAMAP]

Taxonomic identifier

291331 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Xanthomonadales › Xanthomonadaceae › Xanthomonas › Xanthomonas oryzae › Xanthomonas oryzae pv. oryzae

Protein attributes

Sequence length	176 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

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_00825
Catalytic activity	3-hydroxyanthranilate + O2 = 2-amino-3-carboxymuconate semialdehyde. HAMAP-Rule MF_00825
Cofactor	Binds 2 Fe2+ ions per subunit By similarity.
Pathway	Cofactor biosynthesis; NAD(+) biosynthesis; quinolinate from L-kynurenine: step 3/3. HAMAP-Rule MF_00825
Subunit structure	Homodimer By similarity.
Sequence similarities	Belongs to the 3-HAO family.
Sequence caution	The sequence AAW75678.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Pyridine nucleotide biosynthesis
Ligand	Iron Metal-binding
Molecular function	Dioxygenase Oxidoreductase
Technical term	Complete proteome
Gene Ontology (GO)
Biological_process	anthranilate metabolic process Inferred from electronic annotation. Source: HAMAP de novo NAD biosynthetic process from tryptophan Inferred from electronic annotation. Source: HAMAP quinolinate biosynthetic process Inferred from electronic annotation. Source: HAMAP tryptophan catabolic process Inferred from electronic annotation. Source: HAMAP
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 – 176	176	3-hydroxyanthranilate 3,4-dioxygenase HAMAP-Rule MF_00825		PRO_0000245484
Sites
	Metal binding	48	1	Iron 1; catalytic By similarity
	Metal binding	54	1	Iron 1; catalytic By similarity
	Metal binding	92	1	Iron 1; catalytic By similarity
	Metal binding	121	1	Iron 2 By similarity
	Metal binding	124	1	Iron 2 By similarity
	Metal binding	158	1	Iron 2 By similarity
	Metal binding	161	1	Iron 2 By similarity
	Binding site	44	1	Dioxygen By similarity
	Binding site	54	1	Substrate By similarity
	Binding site	96	1	Substrate By similarity
	Binding site	106	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q5H043 [UniParc]. Last modified July 11, 2006. Version 2. Checksum: 4274767A24F2B088	FASTA	176	20,196
	10 20 30 40 50 60 MLIPPINLHA WIEEHRHLLK PPVGNKCIQQ DGFIIMIVGG PNARTDYHYD EGPEWFFQLE 70 80 90 100 110 120 GEMVLKVQDD GVARDIPIRA GEIFLLPPRV PHSPQRAAGS IGIVIERVRL PHEQDGLQWY 130 140 150 160 170 CPQCNHKLYE AMFPLKNIET DFPPVFDHFY RSLALRTCSQ CGHLHPAPER YAAVED

References

[1]

"The genome sequence of Xanthomonas oryzae pathovar oryzae KACC10331, the bacterial blight pathogen of rice." Lee B.-M., Park Y.-J., Park D.-S., Kang H.-W., Kim J.-G., Song E.-S., Park I.-C., Yoon U.-H., Hahn J.-H., Koo B.-S., Lee G.-B., Kim H., Park H.-S., Yoon K.-O., Kim J.-H., Jung C.-H., Koh N.-H., Seo J.-S., Go S.-J. Nucleic Acids Res. 33:577-586(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: KACC10331 / KXO85.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE013598 Genomic DNA. Translation: AAW75678.1. Different initiation.
RefSeq	YP_201063.1. NC_006834.1.
3D structure databases
ProteinModelPortal	Q5H043.
ModBase	Search...
Protein-protein interaction databases
STRING	291331.XOO2424.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAW75678; AAW75678; XOO2424.
GeneID	3261805.
KEGG	xoo:XOO2424.
PATRIC	24104129. VBIXanOry111333_2696.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	NOG77058.
HOGENOM	HOG000218448.
KO	K00452.
OMA	HSPQRPE.
ProtClustDB	PRK13264.
Enzyme and pathway databases
UniPathway	UPA00253; UER00330.
Family and domain databases
Gene3D	2.60.120.10. 1 hit.
HAMAP	MF_00825. 3_HAO.
InterPro	IPR010329. 3hydroanth_dOase. IPR026014. 3hydroanth_dOase_bac. IPR014710. RmlC-like_jellyroll. IPR011051. RmlC_Cupin. [Graphical view]
PANTHER	PTHR15497. PTHR15497. 1 hit.
Pfam	PF06052. 3-HAO. 1 hit. [Graphical view]
SUPFAM	SSF51182. RmlC_like_cupin. 1 hit.
TIGRFAMs	TIGR03037. anthran_nbaC. 1 hit.
ProtoNet	Search...

Entry information

Entry name

3HAO_XANOR

Accession

Primary (citable) accession number: Q5H043

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 11, 2006
Last sequence update:	July 11, 2006
Last modified:	May 1, 2013
This is version 63 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program