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Protein

Putative acyl-CoA dehydrogenase AidB

Gene

aidB

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Part of the adaptive DNA-repair response to alkylating agents. Could prevent alkylation damage by protecting DNA and destroying alkylating agents that have yet to reach their DNA target. Binds to double-stranded DNA with a preference for a DNA region that includes its own promoter. Shows weak isovaleryl-CoA dehydrogenase activity in vitro.3 Publications

Cofactori

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei185 – 1851FAD1 Publication
Binding sitei191 – 1911FAD1 Publication
Binding sitei218 – 2181FAD1 Publication
Binding sitei429 – 4291FAD1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi182 – 19110FAD1 Publication
Nucleotide bindingi216 – 2183FAD1 Publication
Nucleotide bindingi423 – 43311FAD1 PublicationAdd
BLAST

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Stress response

Keywords - Ligandi

DNA-binding, FAD, Flavoprotein

Enzyme and pathway databases

BioCyciEcoCyc:EG11811-MONOMER.
ECOL316407:JW5867-MONOMER.
MetaCyc:EG11811-MONOMER.
RETL1328306-WGS:GSTH-1667-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Putative acyl-CoA dehydrogenase AidB (EC:1.3.99.-)
Gene namesi
Name:aidB
Ordered Locus Names:b4187, JW5867
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG11811. aidB.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi437 – 4371R → Q: Does not affect DNA binding affinity. 1 Publication
Mutagenesisi518 – 5181R → Q: Reduces DNA binding affinity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 541541Putative acyl-CoA dehydrogenase AidBPRO_0000201192Add
BLAST

Proteomic databases

PaxDbiP33224.
PRIDEiP33224.

Expressioni

Inductioni

Regulated by Ada in response to alkylating agents. Also induced by anaerobiosis or by acetate at pH 6.5, via RpoS. Represses its own synthesis during normal cell growth.2 Publications

Interactioni

Subunit structurei

Homotetramer. Dimer of dimers.2 Publications

Protein-protein interaction databases

BioGridi4262695. 235 interactions.
DIPiDIP-9078N.
IntActiP33224. 32 interactions.
MINTiMINT-1221527.
STRINGi511145.b4187.

Structurei

Secondary structure

1
541
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni20 – 234Combined sources
Helixi25 – 339Combined sources
Helixi37 – 393Combined sources
Helixi40 – 5011Combined sources
Helixi53 – 6412Combined sources
Beta strandi68 – 725Combined sources
Beta strandi78 – 836Combined sources
Helixi86 – 9712Combined sources
Turni98 – 1025Combined sources
Helixi103 – 1053Combined sources
Helixi113 – 12715Combined sources
Helixi132 – 14817Combined sources
Helixi151 – 1566Combined sources
Helixi157 – 1604Combined sources
Helixi172 – 1743Combined sources
Beta strandi175 – 1773Combined sources
Beta strandi180 – 1834Combined sources
Beta strandi189 – 1913Combined sources
Helixi193 – 1953Combined sources
Beta strandi199 – 2024Combined sources
Beta strandi208 – 21811Combined sources
Beta strandi222 – 23110Combined sources
Beta strandi234 – 24310Combined sources
Beta strandi251 – 2577Combined sources
Beta strandi260 – 2623Combined sources
Beta strandi268 – 28316Combined sources
Helixi287 – 2904Combined sources
Helixi292 – 32332Combined sources
Helixi331 – 3333Combined sources
Helixi335 – 36329Combined sources
Turni364 – 3663Combined sources
Helixi368 – 40033Combined sources
Helixi401 – 4055Combined sources
Helixi411 – 42313Combined sources
Helixi424 – 4263Combined sources
Helixi427 – 44115Combined sources
Helixi445 – 45410Combined sources
Turni455 – 4584Combined sources
Helixi461 – 47313Combined sources
Helixi479 – 4813Combined sources
Helixi482 – 50120Combined sources
Helixi504 – 51512Combined sources
Helixi525 – 53410Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3DJLX-ray1.70A1-541[»]
3U33X-ray2.80A/B/C/D/E/F/G/H/I/J/K/L1-541[»]
ProteinModelPortaliP33224.
SMRiP33224. Positions 1-540.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP33224.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni445 – 54197dsDNA-bindingAdd
BLAST

Domaini

The N-terminal region contains FAD-dependent dehydrogenase activity and the C-terminal region contains DNA-binding activity.1 Publication

Sequence similaritiesi

Belongs to the acyl-CoA dehydrogenase family.Curated

Phylogenomic databases

eggNOGiENOG4105CSU. Bacteria.
COG1960. LUCA.
HOGENOMiHOG000253935.
InParanoidiP33224.
KOiK09456.
OMAiTLCPITM.
PhylomeDBiP33224.

Family and domain databases

InterProiIPR006089. Acyl-CoA_DH_CS.
IPR006091. Acyl-CoA_Oxase/DH_cen-dom.
IPR009075. AcylCo_DH/oxidase_C.
IPR009100. AcylCoA_DH/oxidase_NM_dom.
[Graphical view]
PfamiPF00441. Acyl-CoA_dh_1. 1 hit.
PF02770. Acyl-CoA_dh_M. 1 hit.
[Graphical view]
SUPFAMiSSF47203. SSF47203. 1 hit.
SSF56645. SSF56645. 1 hit.
PROSITEiPS00072. ACYL_COA_DH_1. 1 hit.
PS00073. ACYL_COA_DH_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P33224-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MHWQTHTVFN QPIPLNNSNL YLSDGALCEA VTREGAGWDS DFLASIGQQL
60 70 80 90 100
GTAESLELGR LANVNPPELL RYDAQGRRLD DVRFHPAWHL LMQALCTNRV
110 120 130 140 150
HNLAWEEDAR SGAFVARAAR FMLHAQVEAG SLCPITMTFA ATPLLLQMLP
160 170 180 190 200
APFQDWTTPL LSDRYDSHLL PGGQKRGLLI GMGMTEKQGG SDVMSNTTRA
210 220 230 240 250
ERLEDGSYRL VGHKWFFSVP QSDAHLVLAQ TAGGLSCFFV PRFLPDGQRN
260 270 280 290 300
AIRLERLKDK LGNRSNASCE VEFQDAIGWL LGLEGEGIRL ILKMGGMTRF
310 320 330 340 350
DCALGSHAMM RRAFSLAIYH AHQRHVFGNP LIQQPLMRHV LSRMALQLEG
360 370 380 390 400
QTALLFRLAR AWDRRADAKE ALWARLFTPA AKFVICKRGM PFVAEAMEVL
410 420 430 440 450
GGIGYCEESE LPRLYREMPV NSIWEGSGNI MCLDVLRVLN KQAGVYDLLS
460 470 480 490 500
EAFVEVKGQD RYFDRAVRRL QQQLRKPAEE LGREITHQLF LLGCGAQMLK
510 520 530 540
YASPPMAQAW CQVMLDTRGG VRLSEQIQND LLLRATGGVC V
Length:541
Mass (Da):60,590
Last modified:December 1, 2000 - v3
Checksum:iD609E364E3A99208
GO

Sequence cautioni

The sequence AAA97083 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence AAC18889 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L20915 Genomic DNA. Translation: AAC18889.1. Different initiation.
L20915 Genomic DNA. Translation: AAC18890.1.
U14003 Genomic DNA. Translation: AAA97083.1. Different initiation.
U00096 Genomic DNA. Translation: AAC77144.2.
AP009048 Genomic DNA. Translation: BAE78188.1.
PIRiI41124.
RefSeqiNP_418608.6. NC_000913.3.
WP_001350567.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC77144; AAC77144; b4187.
BAE78188; BAE78188; BAE78188.
GeneIDi948710.
KEGGiecj:JW5867.
eco:b4187.
PATRICi32123949. VBIEscCol129921_4319.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L20915 Genomic DNA. Translation: AAC18889.1. Different initiation.
L20915 Genomic DNA. Translation: AAC18890.1.
U14003 Genomic DNA. Translation: AAA97083.1. Different initiation.
U00096 Genomic DNA. Translation: AAC77144.2.
AP009048 Genomic DNA. Translation: BAE78188.1.
PIRiI41124.
RefSeqiNP_418608.6. NC_000913.3.
WP_001350567.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3DJLX-ray1.70A1-541[»]
3U33X-ray2.80A/B/C/D/E/F/G/H/I/J/K/L1-541[»]
ProteinModelPortaliP33224.
SMRiP33224. Positions 1-540.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4262695. 235 interactions.
DIPiDIP-9078N.
IntActiP33224. 32 interactions.
MINTiMINT-1221527.
STRINGi511145.b4187.

Proteomic databases

PaxDbiP33224.
PRIDEiP33224.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC77144; AAC77144; b4187.
BAE78188; BAE78188; BAE78188.
GeneIDi948710.
KEGGiecj:JW5867.
eco:b4187.
PATRICi32123949. VBIEscCol129921_4319.

Organism-specific databases

EchoBASEiEB1759.
EcoGeneiEG11811. aidB.

Phylogenomic databases

eggNOGiENOG4105CSU. Bacteria.
COG1960. LUCA.
HOGENOMiHOG000253935.
InParanoidiP33224.
KOiK09456.
OMAiTLCPITM.
PhylomeDBiP33224.

Enzyme and pathway databases

BioCyciEcoCyc:EG11811-MONOMER.
ECOL316407:JW5867-MONOMER.
MetaCyc:EG11811-MONOMER.
RETL1328306-WGS:GSTH-1667-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP33224.
PROiP33224.

Family and domain databases

InterProiIPR006089. Acyl-CoA_DH_CS.
IPR006091. Acyl-CoA_Oxase/DH_cen-dom.
IPR009075. AcylCo_DH/oxidase_C.
IPR009100. AcylCoA_DH/oxidase_NM_dom.
[Graphical view]
PfamiPF00441. Acyl-CoA_dh_1. 1 hit.
PF02770. Acyl-CoA_dh_M. 1 hit.
[Graphical view]
SUPFAMiSSF47203. SSF47203. 1 hit.
SSF56645. SSF56645. 1 hit.
PROSITEiPS00072. ACYL_COA_DH_1. 1 hit.
PS00073. ACYL_COA_DH_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiAIDB_ECOLI
AccessioniPrimary (citable) accession number: P33224
Secondary accession number(s): P33223, Q2M6B8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: December 1, 2000
Last modified: September 7, 2016
This is version 135 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  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.