3-hydroxyanthranilate 3,4-dioxygenase - Rattus norvegicus (Rat)

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P46953 (3HAO_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 96. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

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

Organism

Rattus norvegicus (Rat) [Reference proteome]

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	286 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

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
Subunit structure	Monomer By similarity.
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
PTM	Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	NAD biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway neuron homeostasis Inferred from electronic annotation. Source: Compara quinolinate metabolic process Inferred from direct assay PubMed 2940338 PubMed 3112306 PubMed 9870556. Source: RGD response to cadmium ion Inferred from electronic annotation. Source: Compara response to zinc ion Inferred from electronic annotation. Source: Compara
Cellular_component	cytosol Inferred from electronic annotation. Source: Compara mitochondrial membrane Inferred from direct assay PubMed 3346732. Source: RGD
Molecular_function	3-hydroxyanthranilate 3,4-dioxygenase activity Inferred from direct assay PubMed 2940338 PubMed 3112306 PubMed 9870556. Source: RGD ferrous iron binding Inferred from electronic annotation. Source: Compara iron ion binding Inferred from direct assay PubMed 2940338 PubMed 3112306 PubMed 9870556. Source: RGD oxygen binding Inferred from direct assay PubMed 9870556. Source: RGD
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 286

286

3-hydroxyanthranilate 3,4-dioxygenase HAMAP-Rule MF_03019

PRO_0000064374

Regions

Region

1 – 160

160

Domain A (catalytic) By similarity

Region

161 – 177

Linker By similarity

Region

178 – 286

109

Domain B By similarity

Sites

Metal binding

Iron; catalytic By similarity

Metal binding

Iron; catalytic By similarity

Metal binding

Iron; catalytic By similarity

Binding site

Dioxygen By similarity

Binding site

Substrate By similarity

Binding site

Substrate By similarity

Binding site

105

Substrate By similarity

Amino acid modifications

Modified residue

Phosphoserine By similarity

Experimental info

Sequence conflict

R → Q in AAH85739. Ref.2

Sequence conflict

K → S AA sequence Ref.3

Sequence conflict

199

S → F AA sequence Ref.3

Sequence conflict

204

G → C AA sequence Ref.3

Sequence conflict

214

H → Y AA sequence Ref.3

Sequence conflict

229

W → P AA sequence Ref.3

Sequences

Sequence

Length

Mass (Da)

Tools

P46953 [UniParc].

Last modified December 15, 1998. Version 2.
Checksum: B4F535AD8949DAB7
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FASTA

286

32,582

        10         20         30         40         50         60 
MERCVRVKSW VEENRASFQP PVCNKLMHRE QLKIMFVGGP NTRKDYHIEE GEEVFYQLEG 

        70         80         90        100        110        120 
DMVLRVLEQG EHRDVVIRQG EIFLLPARVP HSPQRFANTM GLVIERRRME TELDGLRYYV 

       130        140        150        160        170        180 
GDTEDVLFEK WFHCKDLGTQ LAPIIQEFFH SEQYRTGKPN PDQLLKEPPF PLSTRSVMEP 

       190        200        210        220        230        240 
MSLKAWLESH SRELQAGTSL SLFGDSYETQ VIAHGQGSSK GPRQDVDVWL WQLEGSSKVT 

       250        260        270        280 
MGGQCVALAP DDSLLVPAGF SYMWERAQGS VALSVTQDPA CKKPLG

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Increase in the level of mRNA for 3-hydroxyanthranilate 3,4-dioxygenase in brain of epilepsy-prone El mice." Nakagawa Y., Asai H., Mori H., Kitoh J., Nakano K. Biosci. Biotechnol. Biochem. 59:2191-2192(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: Sprague-Dawley. Tissue: Liver.
[2]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Kidney.
[3]	"Molecular cloning and functional expression of human 3-hydroxyanthranilic-acid dioxygenase." Malherbe P., Kohler C., da Prada M., Lang G., Kiefer V., Schwarcz R., Lahm H., Cesura A.M. J. Biol. Chem. 269:13792-13797(1994) [PubMed] [Europe PMC] [Abstract] Cited for: PARTIAL NUCLEOTIDE SEQUENCE [MRNA] OF 44-236, PARTIAL PROTEIN SEQUENCE.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	D44494 mRNA. Translation: BAA07937.1. BC085739 mRNA. Translation: AAH85739.1. D28339 mRNA. Translation: BAA21019.1.
IPI	IPI00339188.
RefSeq	NP_064461.1. NM_020076.2.
UniGene	Rn.48675.
3D structure databases
ProteinModelPortal	P46953.
SMR	P46953. Positions 2-286.
ModBase	Search...
PTM databases
PhosphoSite	P46953.
Proteomic databases
PaxDb	P46953.
PRIDE	P46953.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSRNOT00000045996; ENSRNOP00000043835; ENSRNOG00000031263.
GeneID	56823.
KEGG	rno:56823.
UCSC	RGD:71071. rat.
Organism-specific databases
CTD	23498.
RGD	71071. Haao.
Phylogenomic databases
eggNOG	NOG77058.
GeneTree	ENSGT00390000013008.
HOGENOM	HOG000218448.
HOVERGEN	HBG000018.
KO	K00452.
OrthoDB	EOG4F4SBR.
Enzyme and pathway databases
UniPathway	UPA00253; UER00330.
Gene expression databases
Genevestigator	P46953.
GermOnline	ENSRNOG00000031263. Rattus norvegicus.
Family and domain databases
Gene3D	2.60.120.10. 2 hits.
HAMAP	MF_00825. 3_HAO.
InterPro	IPR010329. 3hydroanth_dOase. IPR016700. 3hydroanth_dOase_met. IPR014710. RmlC-like_jellyroll. IPR011051. RmlC_Cupin. [Graphical view]
Pfam	PF06052. 3-HAO. 1 hit. [Graphical view]
PIRSF	PIRSF017681. 3hydroanth_dOase_animal. 1 hit.
SUPFAM	SSF51182. RmlC_like_cupin. 2 hits.
TIGRFAMs	TIGR03037. anthran_nbaC. 1 hit.
ProtoNet	Search...
Other
NextBio	611253.

Entry information

Entry name

3HAO_RAT

Accession

Primary (citable) accession number: P46953
Secondary accession number(s): P70474, Q5RKK0, Q64556

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	December 15, 1998
Last modified:	April 3, 2013
This is version 96 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents