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Q0VCA8 (3HAO_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 69. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismBos taurus (Bovine) [Reference proteome]
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos

Protein attributes

Sequence length286 AA.
Sequence statusComplete.
Protein existenceEvidence 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.

Pathway

Cofactor biosynthesis; NAD(+) biosynthesis; quinolinate from L-kynurenine: step 3/3. HAMAP-Rule MF_03019

Subunit structure

Monomer. Ref.2

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_03019.

Sequence similarities

Belongs to the 3-HAO family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 2862863-hydroxyanthranilate 3,4-dioxygenase HAMAP-Rule MF_03019
PRO_0000283033

Regions

Region1 – 160160Domain A (catalytic) HAMAP-Rule MF_03019
Region161 – 17717Linker HAMAP-Rule MF_03019
Region178 – 286109Domain B HAMAP-Rule MF_03019

Sites

Metal binding471Iron; catalytic
Metal binding531Iron; catalytic
Metal binding911Iron; catalytic
Binding site431Dioxygen By similarity
Binding site531Substrate By similarity
Binding site951Substrate By similarity
Binding site1051Substrate By similarity

Secondary structure

........................................................... 286
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q0VCA8 [UniParc].

Last modified September 5, 2006. Version 1.
Checksum: 6887DDB93B861F8E

FASTA28632,493
        10         20         30         40         50         60 
MERPVRVKAW VEENRGSFLP PVCNKLLHQK QLKIMFVGGP NTRKDYHIEE GEEVFYQLEG 

        70         80         90        100        110        120 
DMLLRVLERG KHRDVVIRQG EIFLLPAGVP HSPQRFANTV GLVIERRRLK TELDGLRYYV 

       130        140        150        160        170        180 
GDTTDVLFEK WFYCEDLGTQ LAPIIQEFFS SEQYRTGKPN PDQLLKEPPF PLSTRSVMEP 

       190        200        210        220        230        240 
MCLEAWLDGH RKELQAGTPL SLFGDTYESQ VMVHGQGSSE GLRRDVDVWL WQLEGSSVVT 

       250        260        270        280 
MEGQRLSLTL DDSLLVPAGT LYGWERGQGS VALSVTQDPA CKKSLG 

« Hide

References

« Hide 'large scale' references
[1]NIH - Mammalian Gene Collection (MGC) project
Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Hereford.
Tissue: Fetal liver.
[2]"Crystal structure of bovine 3-hydroxyanthranilate 3,4-dioxygenase."
Dilovic I., Gliubich F., Malpeli G., Zanotti G., Matkovic-Calogovic D.
Biopolymers 91:1189-1195(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.51 ANGSTROMS) OF 2-286, SUBUNIT, IRON-BINDING SITES.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BC120265 mRNA. Translation: AAI20266.1.
RefSeqNP_001068926.1. NM_001075458.2.
UniGeneBt.20241.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3FE5X-ray2.51A2-286[»]
ProteinModelPortalQ0VCA8.
SMRQ0VCA8. Positions 2-286.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9913.ENSBTAP00000006132.

Proteomic databases

PRIDEQ0VCA8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSBTAT00000006132; ENSBTAP00000006132; ENSBTAG00000004674.
GeneID510602.
KEGGbta:510602.

Organism-specific databases

CTD23498.

Phylogenomic databases

eggNOGNOG77058.
GeneTreeENSGT00390000013008.
HOGENOMHOG000218448.
HOVERGENHBG000018.
InParanoidQ0VCA8.
KOK00452.
OMADMCLKVI.
OrthoDBEOG7FFMS4.
TreeFamTF300246.

Enzyme and pathway databases

UniPathwayUPA00253; UER00330.

Family and domain databases

Gene3D2.60.120.10. 2 hits.
HAMAPMF_00825. 3_HAO.
InterProIPR010329. 3hydroanth_dOase.
IPR016700. 3hydroanth_dOase_met.
IPR014710. RmlC-like_jellyroll.
IPR011051. RmlC_Cupin.
[Graphical view]
PANTHERPTHR15497. PTHR15497. 1 hit.
PfamPF06052. 3-HAO. 1 hit.
[Graphical view]
PIRSFPIRSF017681. 3hydroanth_dOase_animal. 1 hit.
SUPFAMSSF51182. SSF51182. 2 hits.
TIGRFAMsTIGR03037. anthran_nbaC. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceQ0VCA8.
NextBio20869529.

Entry information

Entry name3HAO_BOVIN
AccessionPrimary (citable) accession number: Q0VCA8
Entry history
Integrated into UniProtKB/Swiss-Prot: April 3, 2007
Last sequence update: September 5, 2006
Last modified: June 11, 2014
This is version 69 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways