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Q1LCS4

- 3HAO_RALME

UniProt

Q1LCS4 - 3HAO_RALME

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Protein
3-hydroxyanthranilate 3,4-dioxygenase
Gene
nbaC, Rmet_5193
Organism
Ralstonia metallidurans (strain CH34 / ATCC 43123 / DSM 2839)
Status
Reviewed - 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.1 Publication

Catalytic activityi

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

Cofactori

Binds 2 Fe2+ ions per subunit.1 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-dioxygenase (EC:1.13.11.6)
Alternative name(s):
3-hydroxyanthranilate oxygenase
Short name:
3-HAO
3-hydroxyanthranilic acid dioxygenase
Short name:
HAD
Gene namesi
Name:nbaC
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-dioxygenaseUniRule annotation
PRO_0000245477Add
BLAST

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

STRINGi266264.Rmet_5193.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
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.

Miscellaneous databases

EvolutionaryTraceiQ1LCS4.

Family & Domainsi

Sequence similaritiesi

Belongs to the 3-HAO family.

Phylogenomic databases

eggNOGiNOG77058.
HOGENOMiHOG000218448.
KOiK00452.
OMAiHINQTPE.
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

MLTYGAPFNF PRWIDEHAHL LKPPVGNRQV WQDSDFIVTV VGGPNHRTDY    50
HDDPLEEFFY QLRGNAYLNL WVDGRRERAD LKEGDIFLLP PHVRHSPQRP 100
EAGSACLVIE RQRPAGMLDG FEWYCDACGH LVHRVEVQLK SIVTDLPPLF 150
ESFYASEDKR RCPHCGQVHP GRAA 174
Length:174
Mass (Da):20,028
Last modified:May 30, 2006 - v1
Checksum:i385F2E3DEB3947B8
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
Links Updated
CP000353 Genomic DNA. Translation: ABF12052.1 .
RefSeqi YP_587321.1. NC_007974.2.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1YFU X-ray 1.90 A 1-174 [» ]
1YFW X-ray 2.00 A 1-174 [» ]
1YFX X-ray 2.00 A 1-174 [» ]
1YFY X-ray 3.20 A 1-174 [» ]
4HSL X-ray 2.00 A 1-174 [» ]
4HVO X-ray 1.75 A 1-174 [» ]
4HVQ X-ray 2.81 A 1-154 [» ]
4HVR X-ray 2.70 A 1-174 [» ]
4I3P X-ray 1.96 A 1-174 [» ]
ProteinModelPortali Q1LCS4.
SMRi Q1LCS4. Positions 1-174.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 266264.Rmet_5193.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABF12052 ; ABF12052 ; Rmet_5193 .
GeneIDi 4042054.
KEGGi rme:Rmet_5193.
PATRICi 20295146. VBIRalMet4734_5615.

Phylogenomic databases

eggNOGi NOG77058.
HOGENOMi HOG000218448.
KOi K00452.
OMAi HINQTPE.
OrthoDBi EOG6PW234.

Enzyme and pathway databases

UniPathwayi UPA00253 ; UER00330 .
BioCyci CMET266264:GJ5G-5688-MONOMER.
SABIO-RK Q1LCS4.

Miscellaneous databases

EvolutionaryTracei Q1LCS4.

Family and domain databases

Gene3Di 2.60.120.10. 1 hit.
HAMAPi MF_00825. 3_HAO.
InterProi IPR010329. 3hydroanth_dOase.
IPR014710. RmlC-like_jellyroll.
IPR011051. RmlC_Cupin.
[Graphical view ]
PANTHERi PTHR15497. PTHR15497. 1 hit.
Pfami PF06052. 3-HAO. 1 hit.
[Graphical view ]
SUPFAMi SSF51182. SSF51182. 1 hit.
TIGRFAMsi TIGR03037. anthran_nbaC. 1 hit.
ProtoNeti Search...

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: May 14, 2014
This is version 64 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

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

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