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

Last modified April 16, 2014. Version 63. 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:nbaC
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.
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. Ref.2

Catalytic activity

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

Cofactor

Binds 2 Fe2+ ions per subunit. Ref.3

Enzyme regulation

Inhibited by 4-chloro-3-hydroxyanthranilate. Mechanism of inactivation involves the oxidation of the catalytic active site Fe2+ to the catalytically inactive Fe3+ 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. Ref.2

Pathway

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

Subunit structure

Homodimer. Ref.3

Sequence similarities

Belongs to the 3-HAO family.

Biophysicochemical properties

Kinetic parameters:

KM=22.4 µM for 3-hydroxyanthranilate Ref.3

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 1741743-hydroxyanthranilate 3,4-dioxygenase HAMAP-Rule MF_00825
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. Ref.3
Mutagenesis991R → A: Increases KM for 3-hydroxyanthranilate 40-fold. Decreases activity 5000-fold. Ref.3
Mutagenesis1101E → A: Decreases KM for 3-hydroxyanthranilate 2-fold. Decreases activity 2000-fold. Ref.3

Secondary structure

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

Details...

Sequences

Sequence LengthMass (Da)Tools
Q1LCS4 [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."
US DOE Joint Genome Institute
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].
Strain: CH34 / ATCC 43123 / DSM 2839.
[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] [Europe PMC] [Abstract]
Cited for: FUNCTION, ENZYME REGULATION, IDENTIFICATION BY 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] [Europe PMC] [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

EMBL
GenBank
DDBJ
CP000353 Genomic DNA. Translation: ABF12052.1.
RefSeqYP_587321.1. NC_007974.2.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1YFUX-ray1.90A1-174[»]
1YFWX-ray2.00A1-174[»]
1YFXX-ray2.00A1-174[»]
1YFYX-ray3.20A1-174[»]
4HSLX-ray2.00A1-174[»]
4HVOX-ray1.75A1-174[»]
4HVQX-ray2.81A1-154[»]
4HVRX-ray2.70A1-174[»]
4I3PX-ray1.96A1-174[»]
ProteinModelPortalQ1LCS4.
SMRQ1LCS4. Positions 1-174.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING266264.Rmet_5193.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABF12052; ABF12052; Rmet_5193.
GeneID4042054.
KEGGrme:Rmet_5193.
PATRIC20295146. VBIRalMet4734_5615.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCycCMET266264:GJ5G-5688-MONOMER.
SABIO-RKQ1LCS4.
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...

Other

EvolutionaryTraceQ1LCS4.

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: April 16, 2014
This is version 63 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways