Q8PAD0 (3HAO_XANCP) 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:	XCC1555

Organism

Xanthomonas campestris pv. campestris (strain ATCC 33913 / NCPPB 528 / LMG 568) [Reference proteome] [HAMAP]

Taxonomic identifier

190485 [NCBI]

Taxonomic lineage

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

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.

Ontologies

Keywords
Biological process	Pyridine nucleotide biosynthesis
Ligand	Iron Metal-binding
Molecular function	Dioxygenase Oxidoreductase
Technical term	Complete proteome Reference 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_0000245482
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)
	Q8PAD0 [UniParc]. Last modified October 1, 2002. Version 1. Checksum: 3C2FDD218C8458D4	FASTA	176	20,128
	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

References

[1]

"Comparison of the genomes of two Xanthomonas pathogens with differing host specificities." da Silva A.C.R., Ferro J.A., Reinach F.C., Farah C.S., Furlan L.R., Quaggio R.B., Monteiro-Vitorello C.B., Van Sluys M.A., Almeida N.F. Jr., Alves L.M.C., do Amaral A.M., Bertolini M.C., Camargo L.E.A., Camarotte G., Cannavan F., Cardozo J., Chambergo F., Ciapina L.P. , Cicarelli R.M.B., Coutinho L.L., Cursino-Santos J.R., El-Dorry H., Faria J.B., Ferreira A.J.S., Ferreira R.C.C., Ferro M.I.T., Formighieri E.F., Franco M.C., Greggio C.C., Gruber A., Katsuyama A.M., Kishi L.T., Leite R.P., Lemos E.G.M., Lemos M.V.F., Locali E.C., Machado M.A., Madeira A.M.B.N., Martinez-Rossi N.M., Martins E.C., Meidanis J., Menck C.F.M., Miyaki C.Y., Moon D.H., Moreira L.M., Novo M.T.M., Okura V.K., Oliveira M.C., Oliveira V.R., Pereira H.A., Rossi A., Sena J.A.D., Silva C., de Souza R.F., Spinola L.A.F., Takita M.A., Tamura R.E., Teixeira E.C., Tezza R.I.D., Trindade dos Santos M., Truffi D., Tsai S.M., White F.F., Setubal J.C., Kitajima J.P. Nature 417:459-463(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 33913 / NCPPB 528 / LMG 568.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE008922 Genomic DNA. Translation: AAM40850.1.
RefSeq	NP_636926.1. NC_003902.1.
3D structure databases
ProteinModelPortal	Q8PAD0.
ModBase	Search...
Protein-protein interaction databases
STRING	190485.XCC1555.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAM40850; AAM40850; XCC1555.
GeneID	998201.
KEGG	xcc:XCC1555.
PATRIC	24073908. VBIXanCam115730_1668.
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_XANCP

Accession

Primary (citable) accession number: Q8PAD0

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 11, 2006
Last sequence update:	October 1, 2002
Last modified:	May 1, 2013
This is version 70 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program