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Protein

3-hydroxyanthranilate 3,4-dioxygenase

Gene

nbaC

Organism
Ralstonia metallidurans (strain CH34 / ATCC 43123 / DSM 2839)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the oxidative ring opening of 3-hydroxyanthranilate to 2-amino-3-carboxymuconate semialdehyde, which spontaneously cyclizes to quinolinate.UniRule annotation1 Publication

Catalytic activityi

3-hydroxyanthranilate + O2 = 2-amino-3-carboxymuconate semialdehyde.UniRule annotation

Cofactori

Fe2+UniRule annotation1 PublicationNote: Binds 2 Fe2+ ions per subunit.UniRule annotation1 Publication

Enzyme regulationi

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.1 Publication

Kineticsi

  1. KM=22.4 µM for 3-hydroxyanthranilate1 Publication

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei47 – 471Dioxygen
Metal bindingi51 – 511Iron 1; catalytic
Metal bindingi57 – 571Iron 1; catalytic
Binding sitei57 – 571Substrate
Metal bindingi95 – 951Iron 1; catalytic
Binding sitei99 – 991Substrate
Binding sitei110 – 1101Substrate
Metal bindingi125 – 1251Iron 2
Metal bindingi128 – 1281Iron 2
Metal bindingi162 – 1621Iron 2
Metal bindingi165 – 1651Iron 2

GO - Molecular functioni

  1. 3-hydroxyanthranilate 3,4-dioxygenase activity Source: UniProtKB-HAMAP
  2. ferrous iron binding Source: UniProtKB-HAMAP

GO - Biological processi

  1. 'de novo' NAD biosynthetic process from tryptophan Source: UniProtKB-HAMAP
  2. anthranilate metabolic process Source: UniProtKB-HAMAP
  3. quinolinate biosynthetic process Source: UniProtKB-HAMAP
  4. tryptophan catabolic process Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Dioxygenase, Oxidoreductase

Keywords - Biological processi

Pyridine nucleotide biosynthesis

Keywords - Ligandi

Iron, Metal-binding

Enzyme and pathway databases

BioCyciCMET266264:GJ5G-5688-MONOMER.
SABIO-RKQ1LCS4.
UniPathwayiUPA00253; UER00330.

Names & Taxonomyi

Protein namesi
Recommended name:
3-hydroxyanthranilate 3,4-dioxygenaseUniRule annotation (EC:1.13.11.6UniRule annotation)
Alternative name(s):
3-hydroxyanthranilate oxygenaseUniRule annotation
Short name:
3-HAOUniRule annotation
3-hydroxyanthranilic acid dioxygenaseUniRule annotation
Short name:
HADUniRule annotation
Gene namesi
Name:nbaCUniRule annotation
Ordered Locus Names:Rmet_5193
Encoded oniPlasmid megaplasmid0 Publication
OrganismiRalstonia metallidurans (strain CH34 / ATCC 43123 / DSM 2839)
Taxonomic identifieri266264 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeCupriavidus
ProteomesiUP000002429: Plasmid megaplasmid CH34

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi47 – 471R → A: Increases KM for 3-hydroxyanthranilate 7-fold. Decreases activity 1000-fold. 1 Publication
Mutagenesisi99 – 991R → A: Increases KM for 3-hydroxyanthranilate 40-fold. Decreases activity 5000-fold. 1 Publication
Mutagenesisi110 – 1101E → A: Decreases KM for 3-hydroxyanthranilate 2-fold. Decreases activity 2000-fold. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 1741743-hydroxyanthranilate 3,4-dioxygenasePRO_0000245477Add
BLAST

Interactioni

Subunit structurei

Homodimer.UniRule annotation1 Publication

Protein-protein interaction databases

STRINGi266264.Rmet_5193.

Structurei

Secondary structure

1
174
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi10 – 167Combined sources
Helixi17 – 204Combined sources
Turni23 – 253Combined sources
Beta strandi27 – 337Combined sources
Beta strandi35 – 417Combined sources
Beta strandi43 – 453Combined sources
Beta strandi50 – 523Combined sources
Beta strandi57 – 648Combined sources
Beta strandi66 – 727Combined sources
Beta strandi75 – 817Combined sources
Beta strandi86 – 894Combined sources
Beta strandi95 – 995Combined sources
Beta strandi105 – 1117Combined sources
Beta strandi119 – 1246Combined sources
Turni126 – 1283Combined sources
Beta strandi131 – 1377Combined sources
Helixi142 – 1454Combined sources
Helixi147 – 1559Combined sources
Helixi157 – 1604Combined sources
Turni163 – 1653Combined sources
Helixi171 – 1733Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliQ1LCS4.
SMRiQ1LCS4. Positions 1-174.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ1LCS4.

Family & Domainsi

Sequence similaritiesi

Belongs to the 3-HAO family.UniRule annotation

Phylogenomic databases

eggNOGiNOG77058.
HOGENOMiHOG000218448.
KOiK00452.
OMAiKPPVGNQ.
OrthoDBiEOG6PW234.

Family and domain databases

Gene3Di2.60.120.10. 1 hit.
HAMAPiMF_00825. 3_HAO.
InterProiIPR010329. 3hydroanth_dOase.
IPR014710. RmlC-like_jellyroll.
IPR011051. RmlC_Cupin.
[Graphical view]
PANTHERiPTHR15497. PTHR15497. 1 hit.
PfamiPF06052. 3-HAO. 1 hit.
[Graphical view]
SUPFAMiSSF51182. SSF51182. 1 hit.
TIGRFAMsiTIGR03037. anthran_nbaC. 1 hit.

Sequencei

Sequence statusi: Complete.

Q1LCS4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLTYGAPFNF PRWIDEHAHL LKPPVGNRQV WQDSDFIVTV VGGPNHRTDY
60 70 80 90 100
HDDPLEEFFY QLRGNAYLNL WVDGRRERAD LKEGDIFLLP PHVRHSPQRP
110 120 130 140 150
EAGSACLVIE RQRPAGMLDG FEWYCDACGH LVHRVEVQLK SIVTDLPPLF
160 170
ESFYASEDKR RCPHCGQVHP GRAA
Length:174
Mass (Da):20,028
Last modified:May 30, 2006 - v1
Checksum:i385F2E3DEB3947B8
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000353 Genomic DNA. Translation: ABF12052.1.
RefSeqiYP_587321.1. NC_007974.2.

Genome annotation databases

EnsemblBacteriaiABF12052; ABF12052; Rmet_5193.
GeneIDi4042054.
KEGGirme:Rmet_5193.
PATRICi20295146. VBIRalMet4734_5615.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000353 Genomic DNA. Translation: ABF12052.1.
RefSeqiYP_587321.1. NC_007974.2.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliQ1LCS4.
SMRiQ1LCS4. Positions 1-174.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi266264.Rmet_5193.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABF12052; ABF12052; Rmet_5193.
GeneIDi4042054.
KEGGirme:Rmet_5193.
PATRICi20295146. VBIRalMet4734_5615.

Phylogenomic databases

eggNOGiNOG77058.
HOGENOMiHOG000218448.
KOiK00452.
OMAiKPPVGNQ.
OrthoDBiEOG6PW234.

Enzyme and pathway databases

UniPathwayiUPA00253; UER00330.
BioCyciCMET266264:GJ5G-5688-MONOMER.
SABIO-RKQ1LCS4.

Miscellaneous databases

EvolutionaryTraceiQ1LCS4.

Family and domain databases

Gene3Di2.60.120.10. 1 hit.
HAMAPiMF_00825. 3_HAO.
InterProiIPR010329. 3hydroanth_dOase.
IPR014710. RmlC-like_jellyroll.
IPR011051. RmlC_Cupin.
[Graphical view]
PANTHERiPTHR15497. PTHR15497. 1 hit.
PfamiPF06052. 3-HAO. 1 hit.
[Graphical view]
SUPFAMiSSF51182. SSF51182. 1 hit.
TIGRFAMsiTIGR03037. anthran_nbaC. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. 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.

Entry informationi

Entry namei3HAO_RALME
AccessioniPrimary (citable) accession number: Q1LCS4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 11, 2006
Last sequence update: May 30, 2006
Last modified: March 4, 2015
This is version 69 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Plasmid, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.