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

Dihydrolipoyl dehydrogenase

Gene

acoL

Organism
Bacillus subtilis (strain 168)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Catalytic activityi

Protein N(6)-(dihydrolipoyl)lysine + NAD+ = protein N(6)-(lipoyl)lysine + NADH.

Cofactori

FADBy similarityNote: Binds 1 FAD per subunit.By similarity

Pathwayi: acetoin degradation

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei47FADBy similarity1
Binding sitei112FAD; via amide nitrogen and carbonyl oxygenBy similarity1
Binding sitei200NADBy similarity1
Binding sitei305FADBy similarity1
Binding sitei313FAD; via amide nitrogenBy similarity1
Active sitei437Proton acceptorBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi30 – 38FADBy similarity9
Nucleotide bindingi177 – 181NADBy similarity5
Nucleotide bindingi263 – 266NADBy similarity4

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Acetoin catabolism, Glycolysis

Keywords - Ligandi

FAD, Flavoprotein, NAD

Enzyme and pathway databases

BioCyciBSUB:BSU08090-MONOMER.
UniPathwayiUPA00040.

Names & Taxonomyi

Protein namesi
Recommended name:
Dihydrolipoyl dehydrogenase (EC:1.8.1.4)
Alternative name(s):
Dihydrolipoamide dehydrogenase
E3 component of acetoin cleaving system
Gene namesi
Name:acoL
Synonyms:yfjH
Ordered Locus Names:BSU08090
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
Proteomesi
  • UP000001570 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000680181 – 458Dihydrolipoyl dehydrogenaseAdd BLAST458

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi38 ↔ 43Redox-activeBy similarity

Keywords - PTMi

Disulfide bond

Proteomic databases

PaxDbiO34324.

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

STRINGi224308.Bsubs1_010100004503.

Structurei

3D structure databases

ProteinModelPortaliO34324.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Redox-active center

Phylogenomic databases

eggNOGiCOG1249. LUCA.
HOGENOMiHOG000276708.
InParanoidiO34324.
KOiK00382.
OMAiNSSHAMS.
PhylomeDBiO34324.

Family and domain databases

Gene3Di3.30.390.30. 1 hit.
3.50.50.60. 2 hits.
InterProiIPR023753. FAD/NAD-binding_dom.
IPR016156. FAD/NAD-linked_Rdtase_dimer.
IPR006258. Lipoamide_DH.
IPR004099. Pyr_nucl-diS_OxRdtase_dimer.
IPR012999. Pyr_OxRdtase_I_AS.
[Graphical view]
PfamiPF07992. Pyr_redox_2. 1 hit.
PF02852. Pyr_redox_dim. 1 hit.
[Graphical view]
SUPFAMiSSF51905. SSF51905. 1 hit.
SSF55424. SSF55424. 1 hit.
TIGRFAMsiTIGR01350. lipoamide_DH. 1 hit.
PROSITEiPS00076. PYRIDINE_REDOX_1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O34324-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTLAIIGGGP AGYAAAVSAA QQGRNVLLID KGKLGGTCLN EGCIPTKSLL
60 70 80 90 100
ESANVLDKIK HADSFGIELP AGAISVDWSK MQSRKQQVVS QLVQGVQYLM
110 120 130 140 150
KKNQIQVVKG TASFLSERKL LIEGENGKEI READQVLIAS GSEPIELPFA
160 170 180 190 200
PFDGEWILDS KDALSLSEIP SSLVIVGGGV IGCEYAGLFA RLGSQVTIIE
210 220 230 240 250
TADRLIPAED EDIARLFQEK LEEDGVEVHT SSRLGRVDQT AKTAIWKSGQ
260 270 280 290 300
REFKTKADYV LVAIGRKPRL DGLQLEQAGV DFSPKGIPVN GHMQTNVPHI
310 320 330 340 350
YACGDAIGGI QLAHAAFHEG IIAASHASGR DVKINEKHVP RCIYTSPEIA
360 370 380 390 400
CIGMTERQAR SIYGDVKIGE FSFSANGKAL IKQQAEGKVK IMAEPEFGEI
410 420 430 440 450
VGVSMIGPDV TELIGQAAAI MNGEMTADMA EHFIAAHPTL SETLHEALLS

TIGLAVHA
Length:458
Mass (Da):48,853
Last modified:January 1, 1998 - v1
Checksum:i2496832534945183
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF006075 Genomic DNA. Translation: AAC05585.1.
D78509 Genomic DNA. Translation: BAA24293.1.
AL009126 Genomic DNA. Translation: CAB12638.1.
PIRiG69581.
RefSeqiNP_388690.1. NC_000964.3.
WP_003243007.1. NZ_JNCM01000032.1.

Genome annotation databases

EnsemblBacteriaiCAB12638; CAB12638; BSU08090.
GeneIDi939702.
KEGGibsu:BSU08090.
PATRICi18973268. VBIBacSub10457_0848.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF006075 Genomic DNA. Translation: AAC05585.1.
D78509 Genomic DNA. Translation: BAA24293.1.
AL009126 Genomic DNA. Translation: CAB12638.1.
PIRiG69581.
RefSeqiNP_388690.1. NC_000964.3.
WP_003243007.1. NZ_JNCM01000032.1.

3D structure databases

ProteinModelPortaliO34324.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi224308.Bsubs1_010100004503.

Proteomic databases

PaxDbiO34324.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAB12638; CAB12638; BSU08090.
GeneIDi939702.
KEGGibsu:BSU08090.
PATRICi18973268. VBIBacSub10457_0848.

Phylogenomic databases

eggNOGiCOG1249. LUCA.
HOGENOMiHOG000276708.
InParanoidiO34324.
KOiK00382.
OMAiNSSHAMS.
PhylomeDBiO34324.

Enzyme and pathway databases

UniPathwayiUPA00040.
BioCyciBSUB:BSU08090-MONOMER.

Family and domain databases

Gene3Di3.30.390.30. 1 hit.
3.50.50.60. 2 hits.
InterProiIPR023753. FAD/NAD-binding_dom.
IPR016156. FAD/NAD-linked_Rdtase_dimer.
IPR006258. Lipoamide_DH.
IPR004099. Pyr_nucl-diS_OxRdtase_dimer.
IPR012999. Pyr_OxRdtase_I_AS.
[Graphical view]
PfamiPF07992. Pyr_redox_2. 1 hit.
PF02852. Pyr_redox_dim. 1 hit.
[Graphical view]
SUPFAMiSSF51905. SSF51905. 1 hit.
SSF55424. SSF55424. 1 hit.
TIGRFAMsiTIGR01350. lipoamide_DH. 1 hit.
PROSITEiPS00076. PYRIDINE_REDOX_1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiDLDH3_BACSU
AccessioniPrimary (citable) accession number: O34324
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: January 1, 1998
Last modified: October 5, 2016
This is version 134 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

The active site is a redox-active disulfide bond.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Bacillus subtilis
    Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  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.