Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Benzoate 1,2-dioxygenase electron transfer component

Gene

benC

Organism
Acinetobacter baylyi (strain ATCC 33305 / BD413 / ADP1)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

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

Caution

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

Catalytic activityi

Reduced ferredoxin + NAD+ = oxidized ferredoxin + NADH.

Cofactori

Protein has several cofactor binding sites:

Pathwayi: toluene degradation

This protein is involved in the pathway toluene degradation, which is part of Xenobiotic degradation.
View all proteins of this organism that are known to be involved in the pathway toluene degradation and in Xenobiotic degradation.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi51Iron-sulfur (2Fe-2S)PROSITE-ProRule annotation1
Metal bindingi56Iron-sulfur (2Fe-2S)PROSITE-ProRule annotation1
Metal bindingi59Iron-sulfur (2Fe-2S)PROSITE-ProRule annotation1
Metal bindingi93Iron-sulfur (2Fe-2S)PROSITE-ProRule annotation1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionOxidoreductase
Biological processAromatic hydrocarbons catabolism
Ligand2Fe-2S, FAD, Flavoprotein, Iron, Iron-sulfur, Metal-binding, NAD

Enzyme and pathway databases

UniPathwayiUPA00273

Names & Taxonomyi

Protein namesi
Recommended name:
Benzoate 1,2-dioxygenase electron transfer component
Including the following 2 domains:
Ferredoxin
Ferredoxin--NAD(+) reductase (EC:1.18.1.3)
Gene namesi
Name:benC
Ordered Locus Names:ACIAD1438
OrganismiAcinetobacter baylyi (strain ATCC 33305 / BD413 / ADP1)
Taxonomic identifieri62977 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesMoraxellaceaeAcinetobacter
Proteomesi
  • UP000000430 Componenti: Chromosome

Pathology & Biotechi

Chemistry databases

DrugBankiDB03147 Flavin adenine dinucleotide

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001676551 – 348Benzoate 1,2-dioxygenase electron transfer componentAdd BLAST348

Proteomic databases

PRIDEiP07771

Interactioni

Subunit structurei

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

Protein-protein interaction databases

STRINGi62977.ACIAD1438

Structurei

Secondary structure

1348
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi14 – 19Combined sources6
Beta strandi25 – 30Combined sources6
Helixi36 – 42Combined sources7
Beta strandi52 – 56Combined sources5
Beta strandi60 – 65Combined sources6
Helixi72 – 74Combined sources3
Turni77 – 79Combined sources3
Helixi82 – 87Combined sources6
Beta strandi89 – 91Combined sources3
Turni92 – 94Combined sources3
Beta strandi96 – 107Combined sources12
Helixi111 – 113Combined sources3
Beta strandi117 – 140Combined sources24
Beta strandi154 – 158Combined sources5
Beta strandi165 – 169Combined sources5
Beta strandi177 – 184Combined sources8
Helixi190 – 196Combined sources7
Beta strandi204 – 211Combined sources8
Beta strandi223 – 228Combined sources6
Helixi229 – 231Combined sources3
Helixi232 – 245Combined sources14
Beta strandi251 – 259Combined sources9
Helixi260 – 262Combined sources3
Helixi266 – 275Combined sources10
Beta strandi279 – 285Combined sources7
Beta strandi290 – 296Combined sources7
Helixi299 – 301Combined sources3
Helixi304 – 310Combined sources7
Beta strandi312 – 319Combined sources8
Helixi320 – 333Combined sources14
Beta strandi338 – 345Combined sources8

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1KRHX-ray1.50A/B11-348[»]
ProteinModelPortaliP07771
SMRiP07771
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP07771

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini14 – 1092Fe-2S ferredoxin-typePROSITE-ProRule annotationAdd BLAST96
Domaini116 – 217FAD-binding FR-typePROSITE-ProRule annotationAdd BLAST102

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni111 – 348Ferredoxin-reductaseAdd BLAST238

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4108JA0 Bacteria
COG0543 LUCA
HOGENOMiHOG000263663
KOiK05784
OMAiCGTCKCH
OrthoDBiPOG091H05I4

Family and domain databases

CDDicd00207 fer2, 1 hit
Gene3Di3.10.20.30, 1 hit
InterProiView protein in InterPro
IPR036010 2Fe-2S_ferredoxin-like_sf
IPR001041 2Fe-2S_ferredoxin-type
IPR006058 2Fe2S_fd_BS
IPR012675 Beta-grasp_dom_sf
IPR017927 Fd_Rdtase_FAD-bd
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
PfamiView protein in Pfam
PF00970 FAD_binding_6, 1 hit
PF00111 Fer2, 1 hit
PF00175 NAD_binding_1, 1 hit
PRINTSiPR00371 FPNCR
PR00410 PHEHYDRXLASE
SUPFAMiSSF54292 SSF54292, 1 hit
SSF63380 SSF63380, 1 hit
PROSITEiView protein in PROSITE
PS00197 2FE2S_FER_1, 1 hit
PS51085 2FE2S_FER_2, 1 hit
PS51384 FAD_FR, 1 hit

Sequencei

Sequence statusi: Complete.

P07771-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSLYLNRIPA MSNHQVALQF EDGVTRFIRI AQGETLSDAA YRQQINIPMD
60 70 80 90 100
CREGACGTCR AFCESGNYDM PEDNYIEDAL TPEEAQQGYV LACQCRPTSD
110 120 130 140 150
AVFQIQASSE VCKTKIHHFE GTLARVENLS DSTITFDIQL DDGQPDIHFL
160 170 180 190 200
AGQYVNVTLP GTTETRSYSF SSQPGNRLTG FVVRNVPQGK MSEYLSVQAK
210 220 230 240 250
AGDKMSFTGP FGSFYLRDVK RPVLMLAGGT GIAPFLSMLQ VLEQKGSEHP
260 270 280 290 300
VRLVFGVTQD CDLVALEQLD ALQQKLPWFE YRTVVAHAES QHERKGYVTG
310 320 330 340
HIEYDWLNGG EVDVYLCGPV PMVEAVRSWL DTQGIQPANF LFEKFSAN
Length:348
Mass (Da):38,783
Last modified:August 31, 2004 - v2
Checksum:iAAD68A290C7D51F6
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti29R → C in AAC46438 (PubMed:1885518).Curated1
Sequence conflicti55A → E in AAC46438 (PubMed:1885518).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF009224 Genomic DNA Translation: AAC46438.1
CR543861 Genomic DNA Translation: CAG68302.1
PIRiS23479

Genome annotation databases

EnsemblBacteriaiCAG68302; CAG68302; ACIAD1438
KEGGiaci:ACIAD1438

Similar proteinsi

Entry informationi

Entry nameiBENC_ACIAD
AccessioniPrimary (citable) accession number: P07771
Secondary accession number(s): Q6FCA9
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1991
Last sequence update: August 31, 2004
Last modified: May 23, 2018
This is version 137 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Cookie policy

We would like to use anonymized google analytics cookies to gather statistics on how uniprot.org is used in aggregate. Learn more

UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health