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: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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

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)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi51 – 511Iron-sulfur (2Fe-2S)PROSITE-ProRule annotation
Metal bindingi56 – 561Iron-sulfur (2Fe-2S)PROSITE-ProRule annotation
Metal bindingi59 – 591Iron-sulfur (2Fe-2S)PROSITE-ProRule annotation
Metal bindingi93 – 931Iron-sulfur (2Fe-2S)PROSITE-ProRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Aromatic hydrocarbons catabolism

Keywords - Ligandi

2Fe-2S, FAD, Flavoprotein, Iron, Iron-sulfur, Metal-binding, NAD

Enzyme and pathway databases

BioCyciASP62977:GJVV-1366-MONOMER.
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

DrugBankiDB03147. Flavin adenine dinucleotide.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 348348Benzoate 1,2-dioxygenase electron transfer componentPRO_0000167655Add
BLAST

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

1
348
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi14 – 196Combined sources
Beta strandi25 – 306Combined sources
Helixi36 – 427Combined sources
Beta strandi52 – 565Combined sources
Beta strandi60 – 656Combined sources
Helixi72 – 743Combined sources
Turni77 – 793Combined sources
Helixi82 – 876Combined sources
Beta strandi89 – 913Combined sources
Turni92 – 943Combined sources
Beta strandi96 – 10712Combined sources
Helixi111 – 1133Combined sources
Beta strandi117 – 14024Combined sources
Beta strandi154 – 1585Combined sources
Beta strandi165 – 1695Combined sources
Beta strandi177 – 1848Combined sources
Helixi190 – 1967Combined sources
Beta strandi204 – 2118Combined sources
Beta strandi223 – 2286Combined sources
Helixi229 – 2313Combined sources
Helixi232 – 24514Combined sources
Beta strandi251 – 2599Combined sources
Helixi260 – 2623Combined sources
Helixi266 – 27510Combined sources
Beta strandi279 – 2857Combined sources
Beta strandi290 – 2967Combined sources
Helixi299 – 3013Combined sources
Helixi304 – 3107Combined sources
Beta strandi312 – 3198Combined sources
Helixi320 – 33314Combined sources
Beta strandi338 – 3458Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1KRHX-ray1.50A/B11-348[»]
ProteinModelPortaliP07771.
SMRiP07771. Positions 12-348.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP07771.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini14 – 109962Fe-2S ferredoxin-typePROSITE-ProRule annotationAdd
BLAST
Domaini116 – 217102FAD-binding FR-typePROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni111 – 348238Ferredoxin-reductaseAdd
BLAST

Sequence similaritiesi

Contains 1 2Fe-2S ferredoxin-type domain.PROSITE-ProRule annotation
Contains 1 FAD-binding FR-type domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiENOG4108JA0. Bacteria.
COG0543. LUCA.
HOGENOMiHOG000263663.
KOiK05784.
OMAiLASERYH.
OrthoDBiPOG091H05I4.

Family and domain databases

CDDicd00207. fer2. 1 hit.
Gene3Di3.10.20.30. 1 hit.
InterProiIPR001041. 2Fe-2S_ferredoxin-type.
IPR006058. 2Fe2S_fd_BS.
IPR012675. Beta-grasp_dom.
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.
[Graphical view]
PfamiPF00970. FAD_binding_6. 1 hit.
PF00111. Fer2. 1 hit.
PF00175. NAD_binding_1. 1 hit.
[Graphical view]
PRINTSiPR00371. FPNCR.
PR00410. PHEHYDRXLASE.
SUPFAMiSSF54292. SSF54292. 1 hit.
SSF63380. SSF63380. 1 hit.
PROSITEiPS00197. 2FE2S_FER_1. 1 hit.
PS51085. 2FE2S_FER_2. 1 hit.
PS51384. FAD_FR. 1 hit.
[Graphical view]

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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti29 – 291R → C in AAC46438 (PubMed:1885518).Curated
Sequence conflicti55 – 551A → E in AAC46438 (PubMed:1885518).Curated

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.
PATRICi20740688. VBIAciSp98416_1296.

Cross-referencesi

Sequence databases

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1KRHX-ray1.50A/B11-348[»]
ProteinModelPortaliP07771.
SMRiP07771. Positions 12-348.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi62977.ACIAD1438.

Chemistry

DrugBankiDB03147. Flavin adenine dinucleotide.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAG68302; CAG68302; ACIAD1438.
KEGGiaci:ACIAD1438.
PATRICi20740688. VBIAciSp98416_1296.

Phylogenomic databases

eggNOGiENOG4108JA0. Bacteria.
COG0543. LUCA.
HOGENOMiHOG000263663.
KOiK05784.
OMAiLASERYH.
OrthoDBiPOG091H05I4.

Enzyme and pathway databases

UniPathwayiUPA00273.
BioCyciASP62977:GJVV-1366-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP07771.

Family and domain databases

CDDicd00207. fer2. 1 hit.
Gene3Di3.10.20.30. 1 hit.
InterProiIPR001041. 2Fe-2S_ferredoxin-type.
IPR006058. 2Fe2S_fd_BS.
IPR012675. Beta-grasp_dom.
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.
[Graphical view]
PfamiPF00970. FAD_binding_6. 1 hit.
PF00111. Fer2. 1 hit.
PF00175. NAD_binding_1. 1 hit.
[Graphical view]
PRINTSiPR00371. FPNCR.
PR00410. PHEHYDRXLASE.
SUPFAMiSSF54292. SSF54292. 1 hit.
SSF63380. SSF63380. 1 hit.
PROSITEiPS00197. 2FE2S_FER_1. 1 hit.
PS51085. 2FE2S_FER_2. 1 hit.
PS51384. FAD_FR. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiBENC_ACIAD
AccessioniPrimary (citable) accession number: P07771
Secondary accession number(s): Q6FCA9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1991
Last sequence update: August 31, 2004
Last modified: September 7, 2016
This is version 128 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Caution

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

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.