Reviewed, UniProtKB/Swiss-Prot Q07946 (BEDA_PSEPU)

Names and origin

Protein names

Recommended name:
    Benzene 1,2-dioxygenase system ferredoxin--NAD(+) reductase subunit
    EC=1.18.1.3

Gene names

Name:

bedA

Encoded on

Plasmid pHMT112

Organism

Pseudomonas putida

Taxonomic identifier

303 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Pseudomonadaceae › Pseudomonas

Protein attributes

Sequence length	410 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Part of the electron transfer component of benzene 1,2-dioxygenase, transfers electrons from ferredoxin to NADH.
Catalytic activity	Reduced ferredoxin + NAD+ = oxidized ferredoxin + NADH.
Cofactor	FAD.
Pathway	Aromatic compound metabolism; benzene degradation; catechol from benzene: step 1/2.
Subunit structure	This dioxygenase system consists of four proteins: the two subunits of the hydroxylase component (bedC1 and bedC2), a ferredoxin (bedB) and a ferredoxin reductase (bedA).
Sequence similarities	Belongs to the bacterial ring-hydroxylating dioxygenase ferredoxin reductase family.

Ontologies

Keywords
Biological process	Aromatic hydrocarbons catabolism
Ligand	FAD Flavoprotein NAD
Molecular function	Oxidoreductase
Technical term	Direct protein sequencing Plasmid
Gene Ontology (GO)
Biological process	aromatic compound catabolic process Inferred from electronic annotation. Source: UniProtKB-KW cell redox homeostasis Inferred from electronic annotation. Source: InterPro oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: InterPro
Molecular function	FAD binding Inferred from electronic annotation. Source: InterPro ferredoxin-NAD+ reductase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 410	410	Benzene 1,2-dioxygenase system ferredoxin--NAD(+) reductase subunit		PRO_0000167652
Regions
	Nucleotide binding	4 – 35	32	FAD Potential
	Nucleotide binding	145 – 173	29	NAD Potential

Sequences

	Sequence		Length	Mass (Da)
	Q07946-1 [UniParc]. Last modified November 1, 1995. Version 1. Checksum: 1852467DC01D41EA	FASTA	410	43,587
	10 20 30 40 50 60 MANHVAIIGN GVAGFTTAQA LRAEGYEGRI SLIGEEQHLP YDRPSLSKAV LDGSFEQPPR 70 80 90 100 110 120 LAEADWYSEA SIEMLTGSEV TDLDTQKKMI SLNDGSTISA DAIVIATGSR ARMLSLPGSQ 130 140 150 160 170 180 LPGVVTLRTY GDVQLLRDSW TPNTRLLIVG GGLIGCEVAT TARKLGLSVT ILEAGDELLV 190 200 210 220 230 240 RVLGRRIGAW LRGLLTEQGV QVELKTGVSG FSGEGQLEKV MVNDGRSFIA DNALICVGAD 250 260 270 280 290 300 PADQLARQAG LECDRGVVVD HRGATSAKGI FAVGDVATWP LHSGGKRSLE TYMNAQRQAT 310 320 330 340 350 360 AVAKAILGKE VSAPQLPVSW TEIAGHRMQM AGDIEGPGEY VLRGTLGIGS ALLFRLLDGR 370 380 390 400 410 IQAVVAVDAP RDFALANRLV EAQVIIEPEK LADVSNNMRD IVRANEGNQK

References

[1]

"The Pseudomonas putida ML2 plasmid-encoded genes for benzene dioxygenase are unusual in codon usage and low in G+C content." Tan H.-M., Tang H.-Y., Joannou C., Abdel-Wahab N.H., Mason J.R. Gene 130:33-39(1993) [PubMed: 8344526] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 3-14. Strain: ML2.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF148496 Genomic DNA. Translation: AAA17761.1.
PIR	JN0810.
3D structure databases
ModBase	Search...
Enzyme and pathway databases
BioCyc	MetaCyc:MONOMER-12882.
BRENDA	1.18.1.3. 403.
Family and domain databases
InterPro	IPR016156. FAD/NAD-linked_Rdtase_dimer. IPR013027. FAD_pyr_nucl-diS_OxRdtase. IPR004099. Pyr_nucl-diS_OxRdtase_dimer. IPR001327. Pyr_OxRdtase_NAD_bd. [Graphical view]
Gene3D	G3DSA:3.30.390.30. Pyr_redox_dim. 1 hit.
Pfam	PF00070. Pyr_redox. 1 hit. PF07992. Pyr_redox_2. 1 hit. [Graphical view]
PRINTS	PR00368. FADPNR.
ProtoNet	Search...

Entry information

Entry name

BEDA_PSEPU

Accession

Primary (citable) accession number: Q07946

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	November 1, 1995
Last modified:	February 9, 2010
This is version 62 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)