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Protein

Dihydrolipoyl dehydrogenase

Gene

lpdA

Organism
Synechocystis sp. (strain PCC 6803 / Kazusa)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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

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 sitei53 – 531FADBy similarity
Binding sitei119 – 1191FAD; via amide nitrogen and carbonyl oxygenBy similarity
Binding sitei207 – 2071NADBy similarity
Binding sitei323 – 3231FADBy similarity
Binding sitei331 – 3311FAD; via amide nitrogenBy similarity
Active sitei459 – 4591Proton acceptorBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi36 – 449FADBy similarity
Nucleotide bindingi184 – 1885NADBy similarity
Nucleotide bindingi275 – 2784NADBy 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
Short name:
LPD
E3 component of pyruvate complex
Gene namesi
Name:lpdA
Synonyms:pdhD
Ordered Locus Names:slr1096
OrganismiSynechocystis sp. (strain PCC 6803 / Kazusa)
Taxonomic identifieri1111708 [NCBI]
Taxonomic lineageiBacteriaCyanobacteriaOscillatoriophycideaeChroococcalesSynechocystis
Proteomesi
  • UP000001425 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell inner membrane, Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved1 Publication
Chaini2 – 474473Dihydrolipoyl dehydrogenasePRO_0000068051Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi44 ↔ 49Redox-activeBy similarity

Keywords - PTMi

Disulfide bond

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

IntActiP72740. 2 interactions.

Structurei

3D structure databases

ProteinModelPortaliP72740.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Redox-active center

Phylogenomic databases

HOGENOMiHOG000276708.
InParanoidiP72740.
KOiK00382.
OMAiVYTQPEI.
OrthoDBiEOG6QCD6D.
PhylomeDBiP72740.

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. 3 hits.
SSF55424. SSF55424. 1 hit.
TIGRFAMsiTIGR01350. lipoamide_DH. 1 hit.
PROSITEiPS00076. PYRIDINE_REDOX_1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P72740-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSQDFDYDLV IIGAGVGGHG AALHAVKCGL KTAIIEAKDM GGTCVNRGCI
60 70 80 90 100
PSKALLAASG RVREMSDQDH LQQLGIQING VTFTREAIAA HANDLVSKIQ
110 120 130 140 150
SDLTNSLTRL KVDTIRGWGK VSGPQEVTVI GDNETRILKA KEIMLCPGSV
160 170 180 190 200
PFVPPGIEID HKTVFTSDEA VKLETLPQWI AIIGSGYIGL EFSDVYTALG
210 220 230 240 250
CEVTMIEALP DLMPGFDPEI AKIAERVLIK SRDIETYTGV FATKIKAGSP
260 270 280 290 300
VEIELTDAKT KEVIDTLEVD ACLVATGRIP ATKNLGLETV GVETDRRGFI
310 320 330 340 350
EVNDQMQVIK DGKPVPHLWA VGDATGKMML AHAASGQGVV AVENICGRKT
360 370 380 390 400
EVDYRAIPAA AFTHPEISYV GLTEAQAKEL GEKEGFVVST AKTYFKGNSK
410 420 430 440 450
ALAEKETDGI AKVVYRQDTG ELLGAHIIGI HASDLIQEAA QAIADRKSVR
460 470
ELAFHVHAHP TLSEVLDEAY KRAV
Length:474
Mass (Da):50,832
Last modified:January 23, 2007 - v3
Checksum:iA2EFD28D8D9C69E1
GO

Sequence cautioni

The sequence BAA16755.1 differs from that shown. Reason: Erroneous initiation. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000022 Genomic DNA. Translation: BAA16755.1. Different initiation.
Z48564 Genomic DNA. Translation: CAA88451.1.
PIRiS74603.

Genome annotation databases

EnsemblBacteriaiBAA16755; BAA16755; BAA16755.
KEGGisyn:slr1096.
PATRICi23837234. VBISynSp132158_0191.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000022 Genomic DNA. Translation: BAA16755.1. Different initiation.
Z48564 Genomic DNA. Translation: CAA88451.1.
PIRiS74603.

3D structure databases

ProteinModelPortaliP72740.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP72740. 2 interactions.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAA16755; BAA16755; BAA16755.
KEGGisyn:slr1096.
PATRICi23837234. VBISynSp132158_0191.

Phylogenomic databases

HOGENOMiHOG000276708.
InParanoidiP72740.
KOiK00382.
OMAiVYTQPEI.
OrthoDBiEOG6QCD6D.
PhylomeDBiP72740.

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. 3 hits.
SSF55424. SSF55424. 1 hit.
TIGRFAMsiTIGR01350. lipoamide_DH. 1 hit.
PROSITEiPS00076. PYRIDINE_REDOX_1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Sequence analysis of the genome of the unicellular cyanobacterium Synechocystis sp. strain PCC6803. II. Sequence determination of the entire genome and assignment of potential protein-coding regions."
    Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y., Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T., Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.
    , Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.
    DNA Res. 3:109-136(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: PCC 6803 / Kazusa.
  2. "Characterization of a gene encoding dihydrolipoamide dehydrogenase of the cyanobacterium Synechocystis sp. strain PCC 6803."
    Engels A., Pistorius E.K.
    Microbiology 143:3543-3553(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-18, CHARACTERIZATION.

Entry informationi

Entry nameiDLDH_SYNY3
AccessioniPrimary (citable) accession number: P72740
Secondary accession number(s): Q53395
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: January 23, 2007
Last modified: March 16, 2016
This is version 129 of the entry and version 3 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, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Synechocystis PCC 6803
    Synechocystis (strain PCC 6803): entries and gene names

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.