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Q5LSJ4 (3HAO_RUEPO) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 66. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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:nbaC
Ordered Locus Names:SPO1774
OrganismRuegeria pomeroyi (strain ATCC 700808 / DSM 15171 / DSS-3) (Silicibacter pomeroyi) [Complete proteome] [HAMAP]
Taxonomic identifier246200 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhodobacteralesRhodobacteraceaeRuegeria

Protein attributes

Sequence length180 AA.
Sequence statusComplete.
Protein existenceInferred 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_00825

Catalytic activity

3-hydroxyanthranilate + O2 = 2-amino-3-carboxymuconate semialdehyde. HAMAP-Rule MF_00825

Cofactor

Binds 2 Fe2+ ions per subunit By similarity. HAMAP-Rule MF_00825

Pathway

Cofactor biosynthesis; NAD(+) biosynthesis; quinolinate from L-kynurenine: step 3/3. HAMAP-Rule MF_00825

Subunit structure

Homodimer By similarity. HAMAP-Rule MF_00825

Sequence similarities

Belongs to the 3-HAO family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 1801803-hydroxyanthranilate 3,4-dioxygenase HAMAP-Rule MF_00825
PRO_0000245478

Sites

Metal binding501Iron 1; catalytic By similarity
Metal binding561Iron 1; catalytic By similarity
Metal binding941Iron 1; catalytic By similarity
Metal binding1241Iron 2 By similarity
Metal binding1271Iron 2 By similarity
Metal binding1611Iron 2 By similarity
Metal binding1641Iron 2 By similarity
Binding site461Dioxygen By similarity
Binding site561Substrate By similarity
Binding site981Substrate By similarity
Binding site1091Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5LSJ4 [UniParc].

Last modified February 1, 2005. Version 1.
Checksum: 53B08A94EFFE38BA

FASTA18020,575
        10         20         30         40         50         60 
MARLSAFNFQ KWIDEHKHLL KPPVGNQQVW EDADLMVTVV GGPNKRTDYH DDPVEEFFYQ 

        70         80         90        100        110        120 
LKGDMVLKLY EGGEFYDVPI REGDIFLLPP HVRHSPQRPQ EGSIGLVIEP KRPEGAHDAI 

       130        140        150        160        170        180 
EWFCFGCGSL VHRAELLLES IVRDLPPVYQ AFYADEQART CPNCGEIHPG KEPPEGWVKL 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000031 Genomic DNA. Translation: AAV95053.1.
RefSeqYP_167011.1. NC_003911.12.

3D structure databases

ProteinModelPortalQ5LSJ4.
SMRQ5LSJ4. Positions 5-171.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING246200.SPO1774.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAV95053; AAV95053; SPO1774.
GeneID3192877.
KEGGsil:SPO1774.
PATRIC23376873. VBIRuePom114501_1798.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGNOG77058.
HOGENOMHOG000218448.
KOK00452.
OMAHINQTPE.
OrthoDBEOG6PW234.
ProtClustDBPRK13264.

Enzyme and pathway databases

UniPathwayUPA00253; UER00330.

Family and domain databases

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

Entry information

Entry name3HAO_RUEPO
AccessionPrimary (citable) accession number: Q5LSJ4
Entry history
Integrated into UniProtKB/Swiss-Prot: July 11, 2006
Last sequence update: February 1, 2005
Last modified: February 19, 2014
This is version 66 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways