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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)DescriptionActionsGraphical viewLength
Binding sitei185FAD1 Publication1
Binding sitei191FAD1 Publication1
Binding sitei218FAD1 Publication1
Binding sitei429FAD1 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi182 – 191FAD1 Publication10
Nucleotide bindingi216 – 218FAD1 Publication3
Nucleotide bindingi423 – 433FAD1 PublicationAdd BLAST11

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.

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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
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)DescriptionActionsGraphical viewLength
Mutagenesisi437R → Q: Does not affect DNA binding affinity. 1 Publication1
Mutagenesisi518R → Q: Reduces DNA binding affinity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002011921 – 541Putative acyl-CoA dehydrogenase AidBAdd BLAST541

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 interactors.
DIPiDIP-9078N.
IntActiP33224. 32 interactors.
MINTiMINT-1221527.
STRINGi511145.b4187.

Structurei

Secondary structure

1541
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni20 – 23Combined sources4
Helixi25 – 33Combined sources9
Helixi37 – 39Combined sources3
Helixi40 – 50Combined sources11
Helixi53 – 64Combined sources12
Beta strandi68 – 72Combined sources5
Beta strandi78 – 83Combined sources6
Helixi86 – 97Combined sources12
Turni98 – 102Combined sources5
Helixi103 – 105Combined sources3
Helixi113 – 127Combined sources15
Helixi132 – 148Combined sources17
Helixi151 – 156Combined sources6
Helixi157 – 160Combined sources4
Helixi172 – 174Combined sources3
Beta strandi175 – 177Combined sources3
Beta strandi180 – 183Combined sources4
Beta strandi189 – 191Combined sources3
Helixi193 – 195Combined sources3
Beta strandi199 – 202Combined sources4
Beta strandi208 – 218Combined sources11
Beta strandi222 – 231Combined sources10
Beta strandi234 – 243Combined sources10
Beta strandi251 – 257Combined sources7
Beta strandi260 – 262Combined sources3
Beta strandi268 – 283Combined sources16
Helixi287 – 290Combined sources4
Helixi292 – 323Combined sources32
Helixi331 – 333Combined sources3
Helixi335 – 363Combined sources29
Turni364 – 366Combined sources3
Helixi368 – 400Combined sources33
Helixi401 – 405Combined sources5
Helixi411 – 423Combined sources13
Helixi424 – 426Combined sources3
Helixi427 – 441Combined sources15
Helixi445 – 454Combined sources10
Turni455 – 458Combined sources4
Helixi461 – 473Combined sources13
Helixi479 – 481Combined sources3
Helixi482 – 501Combined sources20
Helixi504 – 515Combined sources12
Helixi525 – 534Combined sources10

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiP33224.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni445 – 541dsDNA-bindingAdd BLAST97

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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3DJLX-ray1.70A1-541[»]
3U33X-ray2.80A/B/C/D/E/F/G/H/I/J/K/L1-541[»]
ProteinModelPortaliP33224.
SMRiP33224.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4262695. 235 interactors.
DIPiDIP-9078N.
IntActiP33224. 32 interactors.
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.

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: November 2, 2016
This is version 137 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.