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P07771 (BENC_ACIAD) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 102. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Benzoate 1,2-dioxygenase electron transfer component

Including the following 2 domains:

  1. Ferredoxin
  2. Ferredoxin--NAD(+) reductase
    EC=1.18.1.3
Gene names
Name:benC
Ordered Locus Names:ACIAD1438
OrganismAcinetobacter sp. (strain ADP1) [Complete proteome] [HAMAP]
Taxonomic identifier62977 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Moraxellaceae › Acinetobacter

Protein attributes

Sequence length348 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Electron transfer component of benzoate 1,2-dioxygenase system.

Catalytic activity

Reduced ferredoxin + NAD+ = oxidized ferredoxin + NADH.

Cofactor

FAD.

Binds 1 2Fe-2S cluster per subunit By similarity.

Pathway

Xenobiotic degradation; toluene degradation.

Subunit structure

This dioxygenase system consists of three proteins: the two subunits of the hydroxylase component (BenA and BenB), and an electron transfer component (BenC).

Sequence similarities

Belongs to the bacterial ring-hydroxylating dioxygenase ferredoxin reductase family.

Contains 1 2Fe-2S ferredoxin-type domain.

Contains 1 FAD-binding FR-type domain.

Caution

It is uncertain whether Met-1 or Met-11 is the initiator.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 348348Benzoate 1,2-dioxygenase electron transfer component
PRO_0000167655

Regions

Domain14 – 109962Fe-2S ferredoxin-type
Domain116 – 217102FAD-binding FR-type
Region111 – 348238Ferredoxin-reductase

Sites

Metal binding511Iron-sulfur (2Fe-2S) By similarity
Metal binding561Iron-sulfur (2Fe-2S) By similarity
Metal binding591Iron-sulfur (2Fe-2S) By similarity
Metal binding931Iron-sulfur (2Fe-2S) By similarity

Experimental info

Sequence conflict291R → C in AAC46438. Ref.1
Sequence conflict551A → E in AAC46438. Ref.1

Secondary structure

1 .......................................................... 348
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P07771 [UniParc].

Last modified August 31, 2004. Version 2.
Checksum: AAD68A290C7D51F6

FASTA34838,783
        10         20         30         40         50         60 
MSLYLNRIPA MSNHQVALQF EDGVTRFIRI AQGETLSDAA YRQQINIPMD CREGACGTCR 

        70         80         90        100        110        120 
AFCESGNYDM PEDNYIEDAL TPEEAQQGYV LACQCRPTSD AVFQIQASSE VCKTKIHHFE 

       130        140        150        160        170        180 
GTLARVENLS DSTITFDIQL DDGQPDIHFL AGQYVNVTLP GTTETRSYSF SSQPGNRLTG 

       190        200        210        220        230        240 
FVVRNVPQGK MSEYLSVQAK AGDKMSFTGP FGSFYLRDVK RPVLMLAGGT GIAPFLSMLQ 

       250        260        270        280        290        300 
VLEQKGSEHP VRLVFGVTQD CDLVALEQLD ALQQKLPWFE YRTVVAHAES QHERKGYVTG 

       310        320        330        340 
HIEYDWLNGG EVDVYLCGPV PMVEAVRSWL DTQGIQPANF LFEKFSAN

« Hide

References

« Hide 'large scale' references
[1]"Nucleotide sequences of the Acinetobacter calcoaceticus benABC genes for benzoate 1,2-dioxygenase reveal evolutionary relationships among multicomponent oxygenases."
Neidle E.L., Hartnett C., Ornston N.L., Bairoch A., Rekik M., Harayama S.
J. Bacteriol. 173:5385-5395(1991) [PubMed: 1885518] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Unique features revealed by the genome sequence of Acinetobacter sp. ADP1, a versatile and naturally transformation competent bacterium."
Barbe V., Vallenet D., Fonknechten N., Kreimeyer A., Oztas S., Labarre L., Cruveiller S., Robert C., Duprat S., Wincker P., Ornston L.N., Weissenbach J., Marliere P., Cohen G.N., Medigue C.
Nucleic Acids Res. 32:5766-5779(2004) [PubMed: 15514110] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ADP1.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AF009224 Genomic DNA. Translation: AAC46438.1.
CR543861 Genomic DNA. Translation: CAG68302.1.
PIRS23479.
RefSeqYP_046124.2. NC_005966.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1KRHX-ray1.50A/B11-338[»]
ProteinModelPortalP07771.
SMRP07771. Positions 12-348.
ModBaseSearch...

Protein-protein interaction databases

STRINGP07771.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID2880892.
GenomeReviewsGene locus ACIAD1438 in contig CR543861_GR.
KEGGaci:ACIAD1438.
NMPDRfig|62977.3.peg.796.
PATRIC20740688. VBIAciSp98416_1296.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0543.
HOGENOMHBG680293.
OMANYYRLTI.
PhylomeDBP07771.
ProtClustDBCLSK2329305.

Enzyme and pathway databases

BioCycASP62977:ACIAD1438-MONOMER.

Family and domain databases

InterProIPR006058. 2Fe2S_fd_BS.
IPR012675. Beta-grasp_ferredoxin-type.
IPR017927. Fd_Rdtase_FAD-bd.
IPR001041. Ferredoxin.
IPR001709. Flavoprot_Pyr_Nucl_cyt_Rdtase.
IPR008333. OxRdtase_FAD-bd_dom.
IPR001433. OxRdtase_FAD/NAD-bd.
IPR001221. Phe_hydroxylase.
IPR017938. Riboflavin_synthase-like_b-brl.
[Graphical view]
Gene3DG3DSA:3.10.20.30. Ferredoxin_fold. 1 hit.
KOK05784.
PfamPF00970. FAD_binding_6. 1 hit.
PF00111. Fer2. 1 hit.
PF00175. NAD_binding_1. 1 hit.
[Graphical view]
PRINTSPR00371. FPNCR.
PR00410. PHEHYDRXLASE.
SUPFAMSSF54292. Ferredoxin. 1 hit.
SSF63380. Riboflavin_synthase_like_b-brl. 1 hit.
PROSITEPS00197. 2FE2S_FER_1. 1 hit.
PS51085. 2FE2S_FER_2. 1 hit.
PS51384. FAD_FR. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameBENC_ACIAD
AccessionPrimary (citable) accession number: P07771
Secondary accession number(s): Q6FCA9
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1991
Last sequence update: August 31, 2004
Last modified: January 25, 2012
This is version 102 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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