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

Names and origin

Protein names

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 names

Name:	nbaC
Ordered Locus Names:	Rmet_5193

Encoded on

Plasmid megaplasmid

Organism

Ralstonia metallidurans (strain CH34 / ATCC 43123 / DSM 2839) [Complete proteome] [HAMAP]

Taxonomic identifier

266264 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Burkholderiaceae › Cupriavidus › Cupriavidus metallidurans

Protein attributes

Sequence length	174 AA.
Sequence status	Complete.
Protein existence	Evidence 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

Ontologies

Keywords
Biological process	Pyridine nucleotide biosynthesis
Ligand	Iron Metal-binding
Molecular function	Dioxygenase Oxidoreductase
Technical term	3D-structure Complete proteome Plasmid
Gene Ontology (GO)
Biological_process	anthranilate metabolic process Inferred from electronic annotation. Source: HAMAP de novo NAD biosynthetic process from tryptophan Inferred from electronic annotation. Source: HAMAP quinolinate biosynthetic process Inferred from electronic annotation. Source: HAMAP tryptophan catabolic process Inferred from electronic annotation. Source: HAMAP
Molecular_function	3-hydroxyanthranilate 3,4-dioxygenase activity Inferred from electronic annotation. Source: HAMAP ferrous iron binding Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 174

174

3-hydroxyanthranilate 3,4-dioxygenase HAMAP-Rule MF_00825

PRO_0000245477

Sites

Metal binding

51

1

Iron 1; catalytic

Metal binding

57

1

Iron 1; catalytic

Metal binding

95

1

Iron 1; catalytic

Metal binding

125

1

Iron 2

Metal binding

128

1

Iron 2

Metal binding

162

1

Iron 2

Metal binding

165

1

Iron 2

Binding site

47

1

Dioxygen

Binding site

57

1

Substrate

Binding site

99

1

Substrate

Binding site

110

1

Substrate

Experimental info

Mutagenesis

47

1

R → A: Increases KM for 3-hydroxyanthranilate 7-fold. Decreases activity 1000-fold. Ref.3

Mutagenesis

99

1

R → A: Increases KM for 3-hydroxyanthranilate 40-fold. Decreases activity 5000-fold. Ref.3

Mutagenesis

110

1

E → A: Decreases KM for 3-hydroxyanthranilate 2-fold. Decreases activity 2000-fold. Ref.3

Secondary structure

1

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174

Helix Strand Turn

Details...

Helix

10 – 16

7

Helix

17 – 20

4

Turn

23 – 25

3

Beta strand

27 – 33

7

Beta strand

35 – 41

7

Beta strand

50 – 52

3

Beta strand

57 – 64

8

Beta strand

66 – 72

7

Beta strand

75 – 81

7

Beta strand

86 – 89

4

Beta strand

95 – 99

5

Beta strand

105 – 111

7

Beta strand

119 – 124

6

Turn

126 – 128

3

Beta strand

131 – 137

7

Helix

142 – 145

4

Helix

147 – 154

8

Helix

157 – 160

4

Turn

163 – 165

3

Helix

171 – 173

3

Sequences

	Sequence		Length	Mass (Da)
	Q1LCS4 [UniParc]. Last modified May 30, 2006. Version 1. Checksum: 385F2E3DEB3947B8	FASTA	174	20,028
	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

References

	« Hide 'large scale' referencesShow '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. , 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, 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.

RefSeq

YP_587321.1. NC_007974.2.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

Q1LCS4.

SMR

Q1LCS4. Positions 1-174.

ModBase

Search...

Protein-protein interaction databases

STRING

266264.Rmet_5193.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

ABF12052; ABF12052; Rmet_5193.

GeneID

4042054.

KEGG

rme:Rmet_5193.

PATRIC

20295146. VBIRalMet4734_5615.

Organism-specific databases

CMR

Search...

Phylogenomic databases

eggNOG

NOG77058.

HOGENOM

HOG000218448.

KO

K00452.

OMA

HSPQRPE.

ProtClustDB

PRK13264.

Enzyme and pathway databases

BioCyc

CMET266264:GJ5G-5688-MONOMER.

SABIO-RK

Q1LCS4.

UniPathway

UPA00253; UER00330.

Family and domain databases

Gene3D

2.60.120.10. 1 hit.

HAMAP

MF_00825. 3_HAO.

InterPro

IPR010329. 3hydroanth_dOase.
IPR026014. 3hydroanth_dOase_bac.
IPR014710. RmlC-like_jellyroll.
IPR011051. RmlC_Cupin.
[Graphical view]

PANTHER

PTHR15497. PTHR15497. 1 hit.

Pfam

PF06052. 3-HAO. 1 hit.
[Graphical view]

SUPFAM

SSF51182. RmlC_like_cupin. 1 hit.

TIGRFAMs

TIGR03037. anthran_nbaC. 1 hit.

ProtoNet

Search...

Other

EvolutionaryTrace

Q1LCS4.

Entry information

Entry name

3HAO_RALME

Accession

Primary (citable) accession number: Q1LCS4

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 11, 2006
Last sequence update:	May 30, 2006
Last modified:	May 1, 2013
This is version 56 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program