Reviewed, UniProtKB/Swiss-Prot Q8PM31 (3HAO_XANAC)

Names and originHide

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

Ordered Locus Names:

XAC1603

Organism

Xanthomonas axonopodis pv. citri (Citrus canker) [Complete proteome] [HAMAP]

Taxonomic identifier

92829 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Xanthomonadales › Xanthomonadaceae › Xanthomonas

Protein attributesHide

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

General annotation (Comments)Hide

Function	Catalyzes the oxidative ring opening of 3-hydroxyanthranilate to 2-amino-3-carboxymuconate semialdehyde, which spontaneously cyclizes to quinolinate By similarity. HAMAP MF_00825
Catalytic activity	3-hydroxyanthranilate + O2 = 2-amino-3-carboxymuconate semialdehyde. HAMAP MF_00825
Cofactor	Binds 2 Fe2+ ions per subunit By similarity. HAMAP MF_00825
Subunit structure	Homodimer By similarity. HAMAP MF_00825
Sequence similarities	Belongs to the 3-HAO family.

OntologiesHide

Keywords
Ligand	Iron Metal-binding
Molecular function	Dioxygenase Oxidoreductase
Technical term	Complete proteome
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)Hide

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 176	176	3-hydroxyanthranilate 3,4-dioxygenase HAMAP MF_00825		PRO_0000245479
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

SequencesHide

	Sequence		Length	Mass (Da)
	Q8PM31-1 [UniParc]. Last modified October 1, 2002. Version 1. Checksum: FBDAA5A96755F310	FASTA	176	20,155
	10 20 30 40 50 60 MLTPPINLHA WIEEHRHLLK PPVGNKCIQQ DGFIIMVVGG PNARTDYHYD EGPEWFFQLE 70 80 90 100 110 120 GEMVLKVQDE GVARDIPIRA GEVFLLPPKV PHSPQRADGS IGLVIERERL PTEQDGLQWY 130 140 150 160 170 CPQCNHKLYE AMFPLKNIET DFPPVFDRFY RSPALRTCSQ CGHLHPAPER YATVEG

ReferencesHide

[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: 12024217] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 306.

Cross-referencesHide

Sequence databases
EMBL GenBank DDBJ	AE008923 Genomic DNA. Translation: AAM36471.1.
RefSeq	NP_641935.1.
3D structure databases
SMR	Q8PM31. Positions 2-168.
ModBase	Search...
Genome annotation databases
GeneID	1155674.
GenomeReviews	Gene locus XAC1603 in contig AE008923_GR.
KEGG	xac:XAC1603.
NMPDR	fig|190486.1.peg.1579.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG341987.
OMA	LKPPVNN.
ProtClustDB	PRK13264.
Enzyme and pathway databases
BioCyc	XAXO190486:XAC1603-MONOMER.
BRENDA	1.13.11.6. 289771.
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]
SUPFAM	SSF51182. RmlC_like_cupin. 1 hit.
TIGRFAMs	TIGR03037. anthran_nbaC. 1 hit.
ProtoNet	Search...

Entry informationHide

Entry name

3HAO_XANAC

Accession

Primary (citable) accession number: Q8PM31

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 11, 2006
Last sequence update:	October 1, 2002
Last modified:	July 13, 2010
This is version 51 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)