Q54S02 (3HAO_DICDI) 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:	haao
ORF Names:	DDB_G0282743

Organism

Dictyostelium discoideum (Slime mold) [Reference proteome]

Taxonomic identifier

44689 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Amoebozoa › Mycetozoa › Dictyosteliida › Dictyostelium

Protein attributes

Sequence length	182 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_03019
Catalytic activity	3-hydroxyanthranilate + O2 = 2-amino-3-carboxymuconate semialdehyde. HAMAP-Rule MF_03019
Cofactor	Fe2+ ion By similarity.
Pathway	Cofactor biosynthesis; NAD(+) biosynthesis; quinolinate from L-kynurenine: step 3/3. HAMAP-Rule MF_03019
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 Reference proteome
Gene Ontology (GO)
Biological_process	NAD biosynthetic process Inferred from sequence or structural similarity. Source: dictyBase
Cellular_component	cytoplasm Inferred from sequence or structural similarity. Source: dictyBase
Molecular_function	3-hydroxyanthranilate 3,4-dioxygenase activity Inferred from sequence or structural similarity. Source: dictyBase iron ion binding Inferred from electronic annotation. Source: InterPro
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 HAMAP-Rule MF_03019		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 [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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: AX4.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AAFI02000047 Genomic DNA. Translation: EAL66231.1.
RefSeq	XP_640237.1. XM_635145.1.
3D structure databases
HSSP	HSSP built from PDB template 1ZVF based on UniProtKB P47096.
ProteinModelPortal	Q54S02.
ModBase	Search...
Protein-protein interaction databases
STRING	44689.DDB_0231359.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblProtists	DDB0231359; DDB0231359; DDB_G0282743.
GeneID	8623776.
KEGG	ddi:DDB_G0282743.
Organism-specific databases
dictyBase	DDB_G0282743. haao.
Phylogenomic databases
eggNOG	NOG77058.
KO	K00452.
OMA	HSPQRPE.
ProtClustDB	CLSZ2729014.
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. 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_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:	May 1, 2013
This is version 65 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)