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Protein

Dihydrolipoyl dehydrogenase

Gene

lpdA

Organism
Buchnera aphidicola subsp. Schizaphis graminum (strain Sg)
Status
Reviewed-Annotation score: -Protein inferred from homologyi

Functioni

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

Miscellaneous

The active site is a redox-active disulfide bond.By similarity

Catalytic activityi

Protein N6-(dihydrolipoyl)lysine + NAD+ = protein N6-(lipoyl)lysine + NADH.

Cofactori

FADBy similarityNote: Binds 1 FAD per subunit.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei54FADBy similarity1
Binding sitei117FAD; via amide nitrogen and carbonyl oxygenBy similarity1
Binding sitei205NADBy similarity1
Binding sitei238NAD; via amide nitrogenBy similarity1
Binding sitei314FADBy similarity1
Binding sitei322FAD; via amide nitrogenBy similarity1
Active sitei446Proton acceptorBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi36 – 45FADBy similarity10
Nucleotide bindingi182 – 186NADBy similarity5
Nucleotide bindingi271 – 274NADBy similarity4

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionOxidoreductase
Biological processGlycolysis
LigandFAD, Flavoprotein, NAD

Enzyme and pathway databases

BioCyciBAPH198804:G1FZU-215-MONOMER

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:lpdA
Ordered Locus Names:BUsg_201
OrganismiBuchnera aphidicola subsp. Schizaphis graminum (strain Sg)
Taxonomic identifieri198804 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesErwiniaceaeBuchnera
Proteomesi
  • UP000000416 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000680201 – 476Dihydrolipoyl dehydrogenaseAdd BLAST476

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi45 ↔ 50Redox-activeBy similarity

Keywords - PTMi

Disulfide bond

Proteomic databases

PRIDEiQ8K9T7

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

STRINGi198804.BUsg201

Structurei

3D structure databases

ProteinModelPortaliQ8K9T7
SMRiQ8K9T7
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Redox-active center

Phylogenomic databases

eggNOGiENOG4107QN2 Bacteria
COG1249 LUCA
KOiK00382
OMAiTMSEAVM
OrthoDBiPOG091H0239

Family and domain databases

Gene3Di3.30.390.30, 1 hit
3.50.50.60, 3 hits
InterProiView protein in InterPro
IPR036188 FAD/NAD-bd_sf
IPR023753 FAD/NAD-binding_dom
IPR016156 FAD/NAD-linked_Rdtase_dimer_sf
IPR006258 Lipoamide_DH
IPR001100 Pyr_nuc-diS_OxRdtase
IPR004099 Pyr_nucl-diS_OxRdtase_dimer
IPR012999 Pyr_OxRdtase_I_AS
PfamiView protein in Pfam
PF07992 Pyr_redox_2, 1 hit
PF02852 Pyr_redox_dim, 1 hit
PIRSFiPIRSF000350 Mercury_reductase_MerA, 1 hit
SUPFAMiSSF51905 SSF51905, 1 hit
SSF55424 SSF55424, 1 hit
TIGRFAMsiTIGR01350 lipoamide_DH, 1 hit
PROSITEiView protein in PROSITE
PS00076 PYRIDINE_REDOX_1, 1 hit

Sequencei

Sequence statusi: Complete.

Q8K9T7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MHQEIQSEVV IIGSGPAGYS AAFRCADLGL ETVLIEHQER LGGVCLNVGC
60 70 80 90 100
IPSKSLLHIA KIIKDASELS ESGVFFNKPI IDIKKINNWK EKIIKKLTTG
110 120 130 140 150
LSNMGEKRKV RIVQGKALFN TDHSVLVKNK KNDFTIFFKH AIIATGSKPI
160 170 180 190 200
KIPSLPNEDN RIWNSTDALS LKSIPNRFLI IGGGIIGLEM ATIYSALGSK
210 220 230 240 250
VDIVDRFNAF LPSVDKDITD IYIKSIKKRF KLLLNTHVKS VEKSKDNDLI
260 270 280 290 300
VKIAEENSDE NVCCYDNILV AIGRSPNVDF LGLEKIGLKL NESGFIEINQ
310 320 330 340 350
QLKTNISHIY AIGDVTGFPM LAHKAVQQAH IAAEVISGKK HYFEPKVIPS
360 370 380 390 400
VAYTDPEIAW VGLSEKEAEN NDIDYEVSLF PWSASGRAHA SNCTLGMTKL
410 420 430 440 450
IFNKNTNKII GGSIIGTNAS ELISEIGLAI EMGSDAEDIS LTIHPHPTLS
460 470
ESISLASEVF QGTITDLLNL KKSLLN
Length:476
Mass (Da):52,187
Last modified:October 1, 2002 - v1
Checksum:i2BCD5F1ECB08BA58
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE013218 Genomic DNA Translation: AAM67765.1
RefSeqiWP_011053732.1, NC_004061.1

Genome annotation databases

EnsemblBacteriaiAAM67765; AAM67765; BUsg_201
KEGGibas:BUsg_201

Similar proteinsi

Entry informationi

Entry nameiDLDH_BUCAP
AccessioniPrimary (citable) accession number: Q8K9T7
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 15, 2002
Last sequence update: October 1, 2002
Last modified: May 23, 2018
This is version 117 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome

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