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Protein

Dihydrolipoyl dehydrogenase

Gene

acoD

Organism
Klebsiella pneumoniae
Status
Unreviewed-Annotation score: Annotation score: 2 out of 5-Protein predictedi

Functioni

Catalytic activityi

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

Cofactori

FADUniRule annotationNote: Binds 1 FAD per subunit.UniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

OxidoreductaseUniRule annotation

Keywords - Biological processi

GlycolysisSAAS annotation

Keywords - Ligandi

FADUniRule annotation, Flavoprotein, NADUniRule annotation

Names & Taxonomyi

Protein namesi
Recommended name:
Dihydrolipoyl dehydrogenaseUniRule annotation (EC:1.8.1.4UniRule annotation)
Gene namesi
Name:acoDImported
OrganismiKlebsiella pneumoniaeImported
Taxonomic identifieri573 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeKlebsiella

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Structurei

3D structure databases

ProteinModelPortaliQ48419.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini5 – 325321FAD/NAD-binding_domInterPro annotationAdd
BLAST
Domaini346 – 454109Pyr_redox_dimInterPro annotationAdd
BLAST

Keywords - Domaini

Redox-active centerUniRule annotation

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.

Q48419-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MHDKYDVLII GGGPGGYVAA IRAGQLGLRT VLVEKQHLGG ICLNWGCIPT
60 70 80 90 100
KALLHGAEVA HTITHASQLG ISVGEVNVDL QKLVQFSRTV SQQLTAGVAY
110 120 130 140 150
LLKKNGVRVI DGTARLRGKG QITVEDARGE ARDYRADHVI LATGARPRAL
160 170 180 190 200
PGIAPDGEHI WTYFEALRPK LLPKSLLIIG SGAIGVEFAS LYNDLGCKVT
210 220 230 240 250
LVELASQILP VEDAEVSAAV RKSFEKRGIQ IHTQTLVTQV QLTDTGVRCT
260 270 280 290 300
LNNTGGEYSQ DVERVLLAVG VQPNIEDLGL ETLGVELDRG FIKTDAACRT
310 320 330 340 350
NVFGLYAIGD VAGPPCLAHK ASHEGVLCVE TLAGVEGAHP LDRDYVPGCT
360 370 380 390 400
YARPQVASLG LTESTALARG RPIRIGKFSY QSNGKALVSG ETEGFVKTIF
410 420 430 440 450
DAETGELLGA HMVGAQVTEQ IQGFGIARHL EATDESLLSM IFAHPTLSEA
460
MHESILAACD QPLHQ
Length:465
Mass (Da):49,568
Last modified:July 5, 2004 - v3
Checksum:i064A892F2DC2865F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U30887 Genomic DNA. Translation: AAB40885.1.
PIRiJC4793.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U30887 Genomic DNA. Translation: AAB40885.1.
PIRiJC4793.

3D structure databases

ProteinModelPortaliQ48419.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

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...

Publicationsi

  1. Peng H.
    Submitted (JUL-1995) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: CG43Imported.
  2. "Identification and characterization of the acoD gene encoding a dihydrolipoamide dehydrogenase of the Klebsiella pneumoniae acetoin dehydrogenase system."
    Peng H.L., Deng W.L., Yang Y.H., Chang H.Y.
    J. Biochem. 119:1118-1123(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: CG43Imported.

Entry informationi

Entry nameiQ48419_KLEPN
AccessioniPrimary (citable) accession number: Q48419
Secondary accession number(s): Q48410
Entry historyi
Integrated into UniProtKB/TrEMBL: November 1, 1996
Last sequence update: July 5, 2004
Last modified: April 13, 2016
This is version 92 of the entry and version 3 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Miscellaneous

The active site is a redox-active disulfide bond.UniRule annotation

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.