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UniProtKB/Swiss-Prot entry Q1LCS4

[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name 3HAO_RALME
Primary accession number Q1LCS4
Secondary accession numbers None
Integrated into Swiss-Prot on July 11, 2006
Sequence was last modified on May 30, 2006 (Sequence version 1)
Annotations were last modified on    September 2, 2008 (Entry version 22)
Name and origin of the protein
Protein name 3-hydroxyanthranilate 3,4-dioxygenase
Synonyms EC 1.13.11.6
3-hydroxyanthranilic acid dioxygenase
HAD
3-hydroxyanthranilate oxygenase
3-HAO
Gene name
OrderedLocusNames: Rmet_5193
From
Ralstonia metallidurans (strain CH34 / ATCC 43123 / DSM 2839) [TaxID: 266264] [HAMAP proteome]
Encoded on Plasmid megaplasmid.
Taxonomy Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; Burkholderiaceae; Cupriavidus.
Protein existence 1: Evidence at protein level;
References
[1]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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., 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.;
"Complete sequence of the megaplasmid of Ralstonia metallidurans CH34.";
Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases.
[2]
 FUNCTION, ENZYME REGULATION, AND MASS SPECTROMETRY.
DOI=10.1021/bi0473455; PubMed=15909977 [NCBI, ExPASy, EBI, Israel, Japan]
Colabroy K.L., Zhai H., Li T., Ge Y., Zhang Y., Liu A., Ealick S.E., McLafferty F.W., Begley T.P.;
"The mechanism of inactivation of 3-hydroxyanthranilate-3,4-dioxygenase by 4-chloro-3-hydroxyanthranilate.";
Biochemistry 44:7623-7631(2005).
[3]
 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, AND REACTION MECHANISM.
DOI=10.1021/bi047353l; PubMed=15909978 [NCBI, ExPASy, EBI, Israel, Japan]
Zhang Y., Colabroy K.L., Begley T.P., Ealick S.E.;
"Structural studies on 3-hydroxyanthranilate-3,4-dioxygenase: the catalytic mechanism of a complex oxidation involved in NAD biosynthesis.";
Biochemistry 44:7632-7643(2005).
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 + O2 = 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.
  • BIOPHYSICOCHEMICAL PROPERTIES:
    Kinetic parameters:   KM=22.4 µM for 3-hydroxyanthranilate;
  • SUBUNIT: Homodimer.
  • SIMILARITY: Belongs to the 3-HAO family.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
CP000353; ABF12052.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq YP_587321.1; -.
3D structure databases
PDB
1YFU; X-ray; 1.90 A; A/B=1-174.[ExPASy / RCSB / EBI]
1YFW; X-ray; 2.00 A; A/B=1-174.[ExPASy / RCSB / EBI]
1YFX; X-ray; 2.00 A; A/B=1-174.[ExPASy / RCSB / EBI]
1YFY; X-ray; 3.20 A; A/B=1-174.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1YFU; -.
1YFW; -.
1YFX; -.
1YFY; -.
ModBase Q1LCS4.
Enzyme and pathway databases
BioCyc RMET266264:RMET_5193-MON; -.
Ontologies
GO
GO:0000334; Molecular function: 3-hydroxyanthranilate 3,4-dioxygenase activity (inferred from electronic annotation from HAMAP).
GO:0008198; Molecular function: ferrous iron binding (inferred from electronic annotation from HAMAP).
QuickGo view.
Family and domain databases
HAMAP MF_00825; -; 1.
PBIL [Tree]
InterPro IPR010329; 3hydroanth_dOase.
Graphical view of domain structure.
Pfam PF06052; 3-HAO; 1.
Pfam graphical view of domain structure.
TIGRFAMs TIGR03037; anthran_nbaC; 1.
BLOCKS Q1LCS4.
Genome annotation databases
GeneID 4042054; -.
GenomeReviews CP000353_GR; Rmet_5193.
KEGG rme:Rmet_5193; -.
Phylogenomic databases
HOGENOM Q1LCS4; -.
Genome annotation databases
CMR Q1LCS4; Rmet_5193.
Other
ProtoNet Q1LCS4.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Complete proteome; Dioxygenase; Iron; Metal-binding; Oxidoreductase; Plasmid.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   174  174     3-hydroxyanthranilate 3,4-dioxygenase. PRO_0000245477
METAL   51    51        Iron 1; catalytic. 
METAL   57    57        Iron 1; catalytic. 
METAL   95    95        Iron 1; catalytic. 
METAL   125   125        Iron 2. 
METAL   128   128        Iron 2. 
METAL   162   162        Iron 2. 
METAL   165   165        Iron 2. 
BINDING   47    47        Dioxygen. 
BINDING   57    57        Substrate. 
BINDING   99    99        Substrate. 
BINDING   110   110        Substrate. 
MUTAGEN   47    47        R->A: Increases KM for 3-hydroxyanthranilate 7-fold. Decreases activity 1000-fold. 
MUTAGEN   99    99        R->A: Increases KM for 3-hydroxyanthranilate 40-fold. Decreases activity 5000-fold. 
MUTAGEN   110   110        E->A: Decreases KM for 3-hydroxyanthranilate 2-fold. Decreases activity 2000-fold. 
HELIX   10    16  7      
HELIX   17    20  4      
TURN   23    25  3      
STRAND   27    33  7      
STRAND   35    41  7      
STRAND   50    52  3      
STRAND   57    64  8      
STRAND   66    72  7      
STRAND   75    81  7      
STRAND   85    89  5      
STRAND   95    99  5      
STRAND   105   111  7      
STRAND   119   124  6      
TURN   126   128  3      
STRAND   131   137  7      
HELIX   142   145  4      
HELIX   147   154  8      
HELIX   157   160  4      
TURN   163   165  3      
Sequence information
Length: 174 AA [This is the length of the unprocessed precursor] Molecular weight: 20028 Da [This is the MW of the unprocessed precursor] CRC64: 385F2E3DEB3947B8 [This is a checksum on the sequence] 
        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
Q1LCS4 in FASTA format

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