A0A9Q5HYH4 · A0A9Q5HYH4_SANBA
- Protein3-hydroxyanthranilate 3,4-dioxygenase
- GeneBNA1
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids914 (go to sequence)
- Protein existenceInferred from homology
- Annotation score4/5
Function
function
Catalyzes the oxidative ring opening of 3-hydroxyanthranilate to 2-amino-3-carboxymuconate semialdehyde, which spontaneously cyclizes to quinolinate.
Catalytic activity
- 3-hydroxyanthranilate + O2 = (2Z,4Z)-2-amino-3-carboxymuconate 6-semialdehyde
Cofactor
Pathway
Cofactor biosynthesis; NAD+ biosynthesis; quinolinate from L-kynurenine: step 3/3.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 46 | O2 (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 50 | Fe cation (UniProtKB | ChEBI); catalytic | ||||
Sequence: H | ||||||
Binding site | 56 | Fe cation (UniProtKB | ChEBI); catalytic | ||||
Sequence: E | ||||||
Binding site | 56 | substrate | ||||
Sequence: E | ||||||
Binding site | 94 | Fe cation (UniProtKB | ChEBI); catalytic | ||||
Sequence: H | ||||||
Binding site | 98 | substrate | ||||
Sequence: R | ||||||
Binding site | 108 | substrate | ||||
Sequence: E |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Molecular Function | 3-hydroxyanthranilate 3,4-dioxygenase activity | |
Molecular Function | ferrous iron binding | |
Molecular Function | RNA binding | |
Biological Process | 'de novo' NAD biosynthetic process from tryptophan | |
Biological Process | anthranilate metabolic process | |
Biological Process | quinolinate biosynthetic process | |
Biological Process | tryptophan catabolic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended name3-hydroxyanthranilate 3,4-dioxygenase
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Basidiomycota > Agaricomycotina > Agaricomycetes > Hymenochaetales > Hymenochaetaceae > Sanghuangporus
Accessions
- Primary accessionA0A9Q5HYH4
Proteomes
Subcellular Location
Structure
Family & Domains
Features
Showing features for region, compositional bias, domain, repeat.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 253-316 | Disordered | ||||
Sequence: VVAEVSDKTDEESDDEQSEEDDWEDLASSGVDFEEIEGEEAEFEDSDESGMSVGEEAKPKSAVV | ||||||
Compositional bias | 260-302 | Acidic residues | ||||
Sequence: KTDEESDDEQSEEDDWEDLASSGVDFEEIEGEEAEFEDSDESG | ||||||
Domain | 376-764 | PUM-HD | ||||
Sequence: ERARRKNLSPEERKKHVGELMEIVRGKVQDVVFKHDASRIIQTLVKYGSQDMRDEVARELKGRYKDLAQNKYSKFIVTKLIRILPKHRVSILLEFRGHVIRLLLHREASSVIADAYELYANAFERSLLLYDFYGKEVNLFSSALKRGNIADADAKEKEMLKKGLKGVLEDADSERRKRVLAAVKENLELVMNNPEKGAMSHAIFHRVLWEYLSQINELKDEALQEKCQEQMAEMVHTKDGSRVVREVIAQGTAKDRKQIVKVLKPHIERICNDEEAQNVLFTALDVIDDTKLTGKSLVPEITSRAQVLYKSPQGRRALLYLLVPRVSRHFTPVQTAILEETDPIRAKTSKKDERIRREEVLRAASPVLIELLKEKERTERMLRDPGGSL | ||||||
Repeat | 434-469 | Pumilio | ||||
Sequence: ELKGRYKDLAQNKYSKFIVTKLIRILPKHRVSILLE | ||||||
Repeat | 597-636 | Pumilio | ||||
Sequence: ALQEKCQEQMAEMVHTKDGSRVVREVIAQGTAKDRKQIVK |
Sequence similarities
Belongs to the 3-HAO family.
Keywords
- Domain
Family and domain databases
Sequence
- Sequence statusComplete
- Length914
- Mass (Da)104,040
- Last updated2023-09-13 v1
- Checksum26D052746216931B
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 260-302 | Acidic residues | ||||
Sequence: KTDEESDDEQSEEDDWEDLASSGVDFEEIEGEEAEFEDSDESG |
Keywords
- Technical term