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Q8K9T7

- DLDH_BUCAP

UniProt

Q8K9T7 - DLDH_BUCAP

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Protein

Dihydrolipoyl dehydrogenase

Gene

lpdA

Organism
Buchnera aphidicola subsp. Schizaphis graminum (strain Sg)
Status
Reviewed - 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

Binds 1 FAD per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei54 – 541FADBy similarity
Binding sitei117 – 1171FAD; via amide nitrogen and carbonyl oxygenBy similarity
Binding sitei205 – 2051NADBy similarity
Binding sitei238 – 2381NAD; via amide nitrogenBy similarity
Binding sitei314 – 3141FADBy similarity
Binding sitei322 – 3221FAD; via amide nitrogenBy similarity
Active sitei446 – 4461Proton acceptorBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi36 – 4510FADBy similarity
Nucleotide bindingi182 – 1865NADBy similarity
Nucleotide bindingi271 – 2744NADBy similarity

GO - Molecular functioni

  1. dihydrolipoyl dehydrogenase activity Source: UniProtKB-EC
  2. flavin adenine dinucleotide binding Source: InterPro

GO - Biological processi

  1. cell redox homeostasis Source: InterPro
  2. glycolytic process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Glycolysis

Keywords - Ligandi

FAD, Flavoprotein, NAD

Enzyme and pathway databases

BioCyciBAPH198804:GHMG-211-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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeBuchnera
ProteomesiUP000000416: Chromosome

Subcellular locationi

Cytoplasm By similarity

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 476476Dihydrolipoyl dehydrogenasePRO_0000068020Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi45 ↔ 50Redox-activeBy similarity

Keywords - PTMi

Disulfide bond

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

STRINGi198804.BUsg201.

Structurei

3D structure databases

ProteinModelPortaliQ8K9T7.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Redox-active center

Phylogenomic databases

eggNOGiCOG1249.
KOiK00382.
OMAiIWNSTDA.
OrthoDBiEOG6QCD6D.

Family and domain databases

Gene3Di3.30.390.30. 1 hit.
InterProiIPR016156. FAD/NAD-linked_Rdtase_dimer.
IPR013027. FAD_pyr_nucl-diS_OxRdtase.
IPR006258. Lipoamide_DH.
IPR004099. Pyr_nucl-diS_OxRdtase_dimer.
IPR023753. Pyr_nucl-diS_OxRdtase_FAD/NAD.
IPR012999. Pyr_OxRdtase_I_AS.
IPR001327. Pyr_OxRdtase_NAD-bd_dom.
[Graphical view]
PfamiPF00070. Pyr_redox. 1 hit.
PF07992. Pyr_redox_2. 1 hit.
PF02852. Pyr_redox_dim. 1 hit.
[Graphical view]
PRINTSiPR00368. FADPNR.
SUPFAMiSSF55424. SSF55424. 1 hit.
TIGRFAMsiTIGR01350. lipoamide_DH. 1 hit.
PROSITEiPS00076. PYRIDINE_REDOX_1. 1 hit.
[Graphical view]

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:
EMBL
GenBank
DDBJ
Links Updated
AE013218 Genomic DNA. Translation: AAM67765.1.
RefSeqiNP_660554.1. NC_004061.1.
WP_011053732.1. NC_004061.1.

Genome annotation databases

EnsemblBacteriaiAAM67765; AAM67765; BUsg_201.
GeneIDi1005398.
KEGGibas:BUsg201.
PATRICi21247189. VBIBucAph100086_0208.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE013218 Genomic DNA. Translation: AAM67765.1 .
RefSeqi NP_660554.1. NC_004061.1.
WP_011053732.1. NC_004061.1.

3D structure databases

ProteinModelPortali Q8K9T7.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 198804.BUsg201.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAM67765 ; AAM67765 ; BUsg_201 .
GeneIDi 1005398.
KEGGi bas:BUsg201.
PATRICi 21247189. VBIBucAph100086_0208.

Phylogenomic databases

eggNOGi COG1249.
KOi K00382.
OMAi IWNSTDA.
OrthoDBi EOG6QCD6D.

Enzyme and pathway databases

BioCyci BAPH198804:GHMG-211-MONOMER.

Family and domain databases

Gene3Di 3.30.390.30. 1 hit.
InterProi IPR016156. FAD/NAD-linked_Rdtase_dimer.
IPR013027. FAD_pyr_nucl-diS_OxRdtase.
IPR006258. Lipoamide_DH.
IPR004099. Pyr_nucl-diS_OxRdtase_dimer.
IPR023753. Pyr_nucl-diS_OxRdtase_FAD/NAD.
IPR012999. Pyr_OxRdtase_I_AS.
IPR001327. Pyr_OxRdtase_NAD-bd_dom.
[Graphical view ]
Pfami PF00070. Pyr_redox. 1 hit.
PF07992. Pyr_redox_2. 1 hit.
PF02852. Pyr_redox_dim. 1 hit.
[Graphical view ]
PRINTSi PR00368. FADPNR.
SUPFAMi SSF55424. SSF55424. 1 hit.
TIGRFAMsi TIGR01350. lipoamide_DH. 1 hit.
PROSITEi PS00076. PYRIDINE_REDOX_1. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Sg.

Entry informationi

Entry nameiDLDH_BUCAP
AccessioniPrimary (citable) accession number: Q8K9T7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 15, 2002
Last sequence update: October 1, 2002
Last modified: October 29, 2014
This is version 95 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.By similarity

Keywords - Technical termi

Complete proteome

Documents

  1. Buchnera aphidicola (subsp. Schizaphis graminum)
    Buchnera aphidicola (subsp. Schizaphis graminum): entries and gene names
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3