Skip Header

 
Contribute Send feedback

Reviewed, UniProtKB/Swiss-Prot Q1LCS4 (3HAO_RALME)

Last modified November 4, 2008. Version 23. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    3-hydroxyanthranilate 3,4-dioxygenase
    EC=1.13.11.6
Alternative name(s):
    3-hydroxyanthranilic acid dioxygenase
      Short name=HAD
    3-hydroxyanthranilate oxygenase
      Short name=3-HAO
Gene names
Ordered Locus Names: Rmet_5193
Encoded onPlasmid megaplasmid
OrganismRalstonia metallidurans (strain CH34 / ATCC 43123 / DSM 2839) [Complete proteome] [HAMAP]
Taxonomic identifier266264 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeCupriavidus

Protein attributes

Sequence length174 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
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.

Catalytic activity

3-hydroxyanthranilate + O(2) = 2-amino-3-carboxymuconate semialdehyde.

Cofactor

Binds 2 Fe(2+) ions per subunit.

Enzyme regulation

Inhibited by 4-chloro-3-hydroxyanthranilate. Mechanism of inactivation involves the oxidation of the catalytic active site Fe(2+) to the catalytically inactive Fe(3+) oxidation state, superoxide production, and formation of two disulfide bonds between Cys-125 and Cys-128, and Cys-162 and Cys-165. Enzyme can be reactivated under reducing conditions.

Subunit structure

Homodimer.

Sequence similarities

Belongs to the 3-HAO family.

Biophysicochemical properties

Kinetic parameters:

KM=22.4 µM for 3-hydroxyanthranilate

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 1741743-hydroxyanthranilate 3,4-dioxygenase
PRO_0000245477

Sites

Metal binding511Iron 1; catalytic
Metal binding571Iron 1; catalytic
Metal binding951Iron 1; catalytic
Metal binding1251Iron 2
Metal binding1281Iron 2
Metal binding1621Iron 2
Metal binding1651Iron 2
Binding site471Dioxygen
Binding site571Substrate
Binding site991Substrate
Binding site1101Substrate

Experimental info

Mutagenesis471R → A: Increases KM for 3-hydroxyanthranilate 7-fold. Decreases activity 1000-fold
Mutagenesis991R → A: Increases KM for 3-hydroxyanthranilate 40-fold. Decreases activity 5000-fold
Mutagenesis1101E → A: Decreases KM for 3-hydroxyanthranilate 2-fold. Decreases activity 2000-fold

Secondary structure

...................................... 174
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q1LCS4-1 [UniParc].

Last modified May 30, 2006. Version 1.
Checksum: 385F2E3DEB3947B8

FASTA17420,028
        10         20         30         40         50         60 
MLTYGAPFNF PRWIDEHAHL LKPPVGNRQV WQDSDFIVTV VGGPNHRTDY HDDPLEEFFY 

        70         80         90        100        110        120 
QLRGNAYLNL WVDGRRERAD LKEGDIFLLP PHVRHSPQRP EAGSACLVIE RQRPAGMLDG 

       130        140        150        160        170 
FEWYCDACGH LVHRVEVQLK SIVTDLPPLF ESFYASEDKR RCPHCGQVHP GRAA 

« Hide

References

« Hide 'large scale' references
[1]"Complete sequence of the megaplasmid of Ralstonia metallidurans CH34."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Martinez M., Goltsman E., Pitluck S., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N. expand/collapse author list , Kim E., Mergeay M., Benotmane M.A., Vallaeys T., Michaux A., Monchy S., Dunn J., McCorkle S., Taghavi S., van der Lelie D., Richardson P.
Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[2]"The mechanism of inactivation of 3-hydroxyanthranilate-3,4-dioxygenase by 4-chloro-3-hydroxyanthranilate."
Colabroy K.L., Zhai H., Li T., Ge Y., Zhang Y., Liu A., Ealick S.E., McLafferty F.W., Begley T.P.
Biochemistry 44:7623-7631(2005) [PubMed: 15909977] [Abstract]
Cited for: FUNCTION, ENZYME REGULATION, MASS SPECTROMETRY.
[3]"Structural studies on 3-hydroxyanthranilate-3,4-dioxygenase: the catalytic mechanism of a complex oxidation involved in NAD biosynthesis."
Zhang Y., Colabroy K.L., Begley T.P., Ealick S.E.
Biochemistry 44:7632-7643(2005) [PubMed: 15909978] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF NATIVE PROTEIN AND COMPLEXES WITH SUBSTRATES OR INHIBITOR AND IRON, COFACTOR, KINETIC PARAMETERS, MUTAGENESIS OF ARG-47; ARG-99 AND GLU-110, SUBUNIT, REACTION MECHANISM.

Cross-references

Sequence databases

CP000353 Genomic DNA. Translation: ABF12052.1.
RefSeqYP_587321.1.

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1YFUX-ray1.90A/B1-174[»]
1YFWX-ray2.00A/B1-174[»]
1YFXX-ray2.00A/B1-174[»]
1YFYX-ray3.20A/B1-174[»]
ModBaseSearch...

Genome annotation databases

GeneID4042054.
GenomeReviewsGene locus Rmet_5193 in contig CP000353_GR.
KEGGrme:Rmet_5193.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ1LCS4.

Enzyme and pathway databases

BioCycRMET266264:RMET_5193-MON.

Family and domain databases

HAMAPMF_00825.
[Tree]
InterProIPR010329. 3hydroanth_dOase.
[Graphical view]
PfamPF06052. 3-HAO. 1 hit.
[Graphical view]
TIGRFAMsTIGR03037. anthran_nbaC. 1 hit.
ProtoNetSearch...

Entry information

Entry name3HAO_RALME
AccessionPrimary (citable) accession number: Q1LCS4
Entry history
Integrated into UniProtKB/Swiss-Prot: July 11, 2006
Last sequence update: May 30, 2006
Last modified: November 4, 2008
This is version 23 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents