P11861 (NAHC1_PSEPU) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
1,2-dihydroxynaphthalene dioxygenase
EC=1.13.11.-

Gene names

Name:

nahC

Encoded on

Plasmid NAH7

Organism

Pseudomonas putida (Arthrobacter siderocapsulatus)

Taxonomic identifier

303 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Pseudomonadaceae › Pseudomonas

Protein attributes

Sequence length	302 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Catalyzes the meta-cleavage of the substrate's aromatic ring.
Cofactor	Fe2+ ion.
Pathway	Aromatic compound metabolism; naphthalene degradation.
Sequence similarities	Belongs to the extradiol ring-cleavage dioxygenase family.

Ontologies

Keywords
Biological process	Aromatic hydrocarbons catabolism
Ligand	Iron Metal-binding
Molecular function	Dioxygenase Oxidoreductase
Technical term	Plasmid
Gene Ontology (GO)
Biological process	aromatic compound catabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	ferrous iron binding Inferred from electronic annotation. Source: InterPro oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 302	302	1,2-dihydroxynaphthalene dioxygenase		PRO_0000085021
Sites
	Metal binding	152	1	Iron By similarity
	Metal binding	215	1	Iron By similarity
	Metal binding	266	1	Iron By similarity

Sequences

	Sequence		Length	Mass (Da)
	P11861 [UniParc]. Last modified October 1, 1989. Version 1. Checksum: D05D7457842AC40D	FASTA	302	33,883
	10 20 30 40 50 60 MSKQAAVIEL GYMGISVKDP DAWKSFAMNM LGLQVLDEGE KDRFYLRMDY WHHRIVVHHS 70 80 90 100 110 120 AEDDLEYLGW RVAGKPEFEA LGQKLIDAGY KIRVCDKVEA QERMVLGLMK TEDPGGNPTE 130 140 150 160 170 180 IFWGPRIDMS NPFHPGRPLH GKFVTGDQGL GHCIVRQTDV AAAHKFYSLL GFRGDVEYRI 190 200 210 220 230 240 PLPNGMTAEL SFMHCNARDH SIAFGAMPAA KRLNHLMLEY THMEDLGYTH QQFVKNEIDI 250 260 270 280 290 300 ALQLGIHAND KALTFYGATP SGWLIEPGWR GATAIDEAEY YVGDIFGHGV EAPGYGLDVK LS

References

[1]	"Bacterial aromatic ring-cleavage enzymes are classified into two different gene families." Harayama S., Rekik M. J. Biol. Chem. 264:15328-15333(1989) [PubMed: 2670937] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 17485 / DSM 50208 / JCM 6158 / NCIMB 12092 / Stanier 111 / Biotype A.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	J04994 Genomic DNA. Translation: AAA91577.1.
PIR	A34343.
RefSeq	YP_534826.1. NC_007926.1.
3D structure databases
ProteinModelPortal	P11861.
SMR	P11861. Positions 4-302.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	3974212.
Phylogenomic databases
ProtClustDB	CLSK862341.
Family and domain databases
InterPro	IPR004360. Glyas_Fos-R_dOase. IPR000486. Xdiol_ring_cleave_dOase_1/2. [Graphical view]
Pfam	PF00903. Glyoxalase. 1 hit. [Graphical view]
PROSITE	PS00082. EXTRADIOL_DIOXYGENAS. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

NAHC1_PSEPU

Accession

Primary (citable) accession number: P11861

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1989
Last sequence update:	October 1, 1989
Last modified:	September 21, 2011
This is version 65 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program