Reviewed, UniProtKB/Swiss-Prot Q54S02 (3HAO_DICDI)

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:	haao
ORF Names:	DDB_G0282743

Organism

Dictyostelium discoideum (Slime mold) [Complete proteome]

Taxonomic identifier

44689 [NCBI]

Taxonomic lineage

Eukaryota › Amoebozoa › Mycetozoa › Dictyosteliida › Dictyostelium

Protein attributes

Sequence length	182 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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.
Catalytic activity	3-hydroxyanthranilate + O2 = 2-amino-3-carboxymuconate semialdehyde.
Cofactor	Fe2+ ion By similarity.
Pathway	Cofactor biosynthesis; NAD(+) biosynthesis; pyridine-2,3-dicarboxylate from L-kynurenine: step 3/3.
Subcellular location	Cytoplasm By similarity.
Sequence similarities	Belongs to the 3-HAO family.

Ontologies

Keywords
Biological process	Pyridine nucleotide biosynthesis
Cellular component	Cytoplasm
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 pyridine nucleotide biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	3-hydroxyanthranilate 3,4-dioxygenase activity Inferred from electronic annotation. Source: EC iron ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 182	182	3-hydroxyanthranilate 3,4-dioxygenase		PRO_0000328344
Sites
	Metal binding	50	1	Iron; catalytic By similarity
	Metal binding	56	1	Iron; catalytic By similarity
	Metal binding	95	1	Iron; catalytic By similarity
	Metal binding	124	1	Divalent metal cation By similarity
	Metal binding	129	1	Divalent metal cation By similarity
	Metal binding	165	1	Divalent metal cation By similarity
	Metal binding	168	1	Divalent metal cation By similarity
	Binding site	46	1	Dioxygen By similarity
	Binding site	56	1	Substrate By similarity
	Binding site	99	1	Substrate By similarity
	Binding site	109	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q54S02-1 [UniParc]. Last modified May 24, 2005. Version 1. Checksum: AB372715BAA44ED4	FASTA	182	21,210
	10 20 30 40 50 60 MLPPININKW IEENKSLLQP PVGAKLLYTD IDSTFVVMIV GGPNQRTDYH VNETDEFFYQ 70 80 90 100 110 120 FKGDMILKIV DKDGSFRDIN IREGETFILP GNTPHSPQRY RDTIGLVIEK KRSSENIDKL 130 140 150 160 170 180 LWFCDNKDCR KLLFSRSFHV DDLDLGKQLT PIINEFYGNE ENRTCKHCNH ISQKPTVNDY IQ

References

[1]

"The genome of the social amoeba Dictyostelium discoideum." Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R., Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B., Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T., Lehmann R., Hamlin N. , Davies R., Gaudet P., Fey P., Pilcher K., Chen G., Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N., Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E., Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N., Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D., Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T., Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D., Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A., Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M., Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A., Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y., Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C., Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R., Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A. Nature 435:43-57(2005) [PubMed: 15875012] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: AX4.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AAFI02000047 Genomic DNA. Translation: EAL66231.1.
RefSeq	XP_640237.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	3391292.
KEGG	ddi:DDB_0231359.
Organism-specific databases
dictyBase	DDB_G0282743. haao.
Phylogenomic databases
OMA	Q54S02. RHSPQRP.
Enzyme and pathway databases
BRENDA	1.13.11.6. 424.
Family and domain databases
InterPro	IPR010329. 3hydroanth_dOase. [Graphical view]
Pfam	PF06052. 3-HAO. 1 hit. [Graphical view]
TIGRFAMs	TIGR03037. anthran_nbaC. 1 hit.
ProtoNet	Search...

Entry information

Entry name

3HAO_DICDI

Accession

Primary (citable) accession number: Q54S02

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 8, 2008
Last sequence update:	May 24, 2005
Last modified:	June 16, 2009
This is version 35 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)