Reviewed, UniProtKB/Swiss-Prot P07771 (BENC_ACIAD)

Names and origin

Protein names

Recommended name:
    Benzoate 1,2-dioxygenase electron transfer component
Including 2 domains:
  Recommended name:
      Ferredoxin
  Recommended name:
      Ferredoxin--NAD(+) reductase
      EC=1.18.1.3

Gene names

Name:	benC
Ordered Locus Names:	ACIAD1438

Organism

Acinetobacter sp. (strain ADP1) [Complete proteome] [HAMAP]

Taxonomic identifier

62977 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Moraxellaceae › Acinetobacter

Protein attributes

Sequence length	348 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence 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.
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.

Ontologies

Keywords
Biological process	Aromatic hydrocarbons catabolism
Ligand	2Fe-2S FAD Flavoprotein Iron Iron-sulfur Metal-binding NAD
Molecular function	Oxidoreductase
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Molecular function	ferredoxin-NAD+ reductase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Molecule processing

Chain

1 – 348

348

Benzoate 1,2-dioxygenase electron transfer component

Regions

Domain

14 – 109

96

2Fe-2S ferredoxin-type

Domain

116 – 217

102

FAD-binding FR-type

Region

111 – 348

238

Ferredoxin-reductase

Sites

Metal binding

51

1

Iron-sulfur (2Fe-2S) By similarity

Metal binding

56

1

Iron-sulfur (2Fe-2S) By similarity

Metal binding

59

1

Iron-sulfur (2Fe-2S) By similarity

Metal binding

93

1

Iron-sulfur (2Fe-2S) By similarity

Experimental info

Sequence conflict

29

1

R → C in AAC46438. Ref.1

Sequence conflict

55

1

A → E in AAC46438. Ref.1

Secondary structure

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348

Helix Strand Turn

Details...

Beta strand

14 – 19

6

Beta strand

25 – 30

6

Helix

36 – 42

7

Beta strand

52 – 56

5

Beta strand

60 – 65

6

Helix

72 – 74

3

Turn

77 – 79

3

Helix

82 – 87

6

Beta strand

89 – 91

3

Turn

92 – 94

3

Beta strand

96 – 107

12

Helix

111 – 113

3

Beta strand

117 – 140

24

Beta strand

154 – 158

5

Beta strand

165 – 169

5

Beta strand

177 – 184

8

Helix

190 – 196

7

Beta strand

204 – 211

8

Beta strand

223 – 228

6

Helix

229 – 231

3

Helix

232 – 245

14

Beta strand

251 – 259

9

Helix

260 – 262

3

Helix

266 – 275

10

Beta strand

279 – 285

7

Beta strand

290 – 296

7

Helix

299 – 301

3

Helix

304 – 310

7

Beta strand

312 – 319

8

Helix

320 – 333

14

Beta strand

338 – 345

8

Sequences

	Sequence		Length	Mass (Da)
	P07771-1 [UniParc]. Last modified August 31, 2004. Version 2. Checksum: AAD68A290C7D51F6	FASTA	348	38,783
	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

References

	« Hide 'large scale' referencesShow '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].

Cross-references

Sequence databases

EMBLGenBankDDBJ

AF009224 Genomic DNA. Translation: AAC46438.1.
CR543861 Genomic DNA. Translation: CAG68302.1.

PIR

S23479.

RefSeq

YP_046124.2.

3D structure databases

PDBMSD

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1KRH	X-ray	1.50	A/B	11-348	[»]

ModBase

Search...

Genome annotation databases

GeneID

2880892.

GenomeReviews

Gene locus ACIAD1438 in contig CR543861_GR.

KEGG

aci:ACIAD1438.

NMPDR

fig|62977.3.peg.796.

Organism-specific databases

CMR

Search...

Phylogenomic databases

HOGENOM

P07771.

Enzyme and pathway databases

BioCyc

ASP62977:ACIAD1438-MON.

Family and domain databases

InterPro

IPR006058. 2Fe2S_fd_BS.
IPR012675. b-grasp_ferredoxin-like.
IPR001041. Ferredoxin.
IPR001709. FPN_cyt_redctse.
IPR008333. OxRdtase_FAD-bd.
IPR001433. OxRdtase_FAD/NAD_bd.
IPR001221. Phe_hydroxylase.
[Graphical view]

Gene3D

G3DSA:3.10.20.30. Ferredoxin_fold. 1 hit.

Pfam

PF00970. FAD_binding_6. 1 hit.
PF00111. Fer2. 1 hit.
PF00175. NAD_binding_1. 1 hit.
[Graphical view]

PRINTS

PR00371. FPNCR.
PR00410. PHEHYDRXLASE.

PROSITE

PS00197. 2FE2S_FER_1. 1 hit.
PS51085. 2FE2S_FER_2. 1 hit.
PS51384. FAD_FR. 1 hit.
[Graphical view]

ProDom

P07771.
[Graphical view] [Entries sharing at least one domain]

BLOCKS

Search...

Other Resources

ProtoNet

Search...

Entry information

Entry name

BENC_ACIAD

Accession

Primary (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:	July 22, 2008
This is version 79 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

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