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Protein

Dihydrolipoyl dehydrogenase

Gene

lpd

Organism
Rhodobacter capsulatus (Rhodopseudomonas capsulata)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Lipoamide dehydrogenase is a component of the alpha-ketoacid dehydrogenase complexes.By similarity

Catalytic activityi

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

Cofactori

FADBy similarityNote: Binds 1 FAD per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei51 – 511FADBy similarity
Binding sitei107 – 1071FAD; via amide nitrogen and carbonyl oxygenBy similarity
Binding sitei191 – 1911NADBy similarity
Binding sitei225 – 2251NAD; via amide nitrogenBy similarity
Binding sitei301 – 3011FADBy similarity
Binding sitei309 – 3091FAD; via amide nitrogenBy similarity
Active sitei433 – 4331Proton acceptorBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi33 – 4210FADBy similarity
Nucleotide bindingi168 – 1725NADBy similarity
Nucleotide bindingi258 – 2614NADBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Glycolysis

Keywords - Ligandi

FAD, Flavoprotein, NAD

Names & Taxonomyi

Protein namesi
Recommended name:
Dihydrolipoyl dehydrogenase (EC:1.8.1.4)
Alternative name(s):
Dihydrolipoamide dehydrogenase
E3 component of pyruvate and 2-oxoglutarate dehydrogenases complexes
Gene namesi
Name:lpd
OrganismiRhodobacter capsulatus (Rhodopseudomonas capsulata)
Taxonomic identifieri1061 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhodobacteralesRhodobacteraceaeRhodobacter

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 454454Dihydrolipoyl dehydrogenasePRO_0000068042Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi42 ↔ 47Redox-activeBy similarity

Keywords - PTMi

Disulfide bond

Proteomic databases

PRIDEiP95596.

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

STRINGi272942.RCAP_rcc00726.

Structurei

3D structure databases

ProteinModelPortaliP95596.
SMRiP95596. Positions 3-453.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Redox-active center

Phylogenomic databases

eggNOGiENOG4107QN2. Bacteria.
COG1249. LUCA.

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.

P95596-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAEFDVIIIG GGPGGYVCAI RCAQLGLKTA CVEGRGALGG TCLNVGCIPS
60 70 80 90 100
KALLHATHEL HEVHENFEKM GLMGAKVKVD WAKIDGNTKG IEFLFKKNKV
110 120 130 140 150
TYLRGWGSIP APGQVKVGDE VHTAKNIVIA TGSESSGLPG IEIDEQTVVT
160 170 180 190 200
STGALSLAKV PKSMVVIGAG VIGLELGSVY ARLGAEVTVV EYLDAITPGM
210 220 230 240 250
DAEVAKGLQR ILTRQGLKFV LGAAVQGVDK AKGKNTVRYT LRKDESAHAI
260 270 280 290 300
EAEVVLVATG RKPFTKGLGL EALGVEMLPR GQVKADSHWA TNVPGLYAIG
310 320 330 340 350
DAIVGPMLAH KAEDEGMAVA EVIAGKHGHV NYDVIPGVIY TTPEVAAVGK
360 370 380 390 400
TEDALKQEGR AYKVGKFSFM GNGRAKAVFQ AEGFVKILAD AATDRILGAH
410 420 430 440 450
IIGPSAGDMI HEICVAMEFG ASAQDLALTC HAHPTYSEAV REAALACGDG

AIHA
Length:454
Mass (Da):47,376
Last modified:May 1, 1997 - v1
Checksum:i3C45E995CCE1F37D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U84577 Genomic DNA. Translation: AAC45483.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U84577 Genomic DNA. Translation: AAC45483.1.

3D structure databases

ProteinModelPortaliP95596.
SMRiP95596. Positions 3-453.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi272942.RCAP_rcc00726.

Proteomic databases

PRIDEiP95596.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiENOG4107QN2. Bacteria.
COG1249. LUCA.

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. "Cloning, sequencing, and oxygen regulation of the Rhodobacter capsulatus alpha-ketoglutarate dehydrogenase operon."
    Dastoor F.P., Forrest M.E., Beatty J.T.
    J. Bacteriol. 179:4559-4566(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 33303 / B10.

Entry informationi

Entry nameiDLDH_RHOCA
AccessioniPrimary (citable) accession number: P95596
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: May 1, 1997
Last modified: November 11, 2015
This is version 100 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.

Documents

  1. 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.