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Q1LCS4

- 3HAO_RALME

UniProt

Q1LCS4 - 3HAO_RALME

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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: 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 PublicationUniRule annotation

Catalytic activityi

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

Cofactori

Binds 2 Fe2+ ions per subunit.1 PublicationUniRule annotation

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.1 PublicationUniRule annotation

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 – 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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ1LCS4.

Family & Domainsi

Sequence similaritiesi

Belongs to the 3-HAO family.UniRule annotation

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 [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:
EMBL
GenBank
DDBJ
Links Updated
CP000353 Genomic DNA. Translation: ABF12052.1.
RefSeqiWP_011519599.1. NC_007974.2.
YP_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 WP_011519599.1. NC_007974.2.
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: October 29, 2014
This is version 66 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