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Q04829 (DLDH_HALVD) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 98. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Dihydrolipoyl dehydrogenase

EC=1.8.1.4
Alternative name(s):
Dihydrolipoamide dehydrogenase
Gene names
Name:lpdA
Synonyms:lpd
Ordered Locus Names:HVO_2961
OrganismHaloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2) (Halobacterium volcanii) [Complete proteome] [HAMAP]
Taxonomic identifier309800 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaHalobacteriaHalobacterialesHalobacteriaceaeHaloferax

Protein attributes

Sequence length475 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

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

Cofactor

Binds 1 FAD per subunit By similarity.

Subunit structure

Homodimer.

Subcellular location

Cytoplasm.

Miscellaneous

The active site is a redox-active disulfide bond.

Sequence similarities

Belongs to the class-I pyridine nucleotide-disulfide oxidoreductase family.

Ontologies

Keywords
   Biological processGlycolysis
   Cellular componentCytoplasm
   DomainRedox-active center
   LigandFAD
Flavoprotein
NAD
   Molecular functionOxidoreductase
   PTMDisulfide bond
   Technical termComplete proteome
Direct protein sequencing
Gene Ontology (GO)
   Biological_processcell redox homeostasis

Inferred from electronic annotation. Source: InterPro

glycolysis

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functiondihydrolipoyl dehydrogenase activity

Inferred from electronic annotation. Source: EC

flavin adenine dinucleotide binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.3
Chain2 – 475474Dihydrolipoyl dehydrogenase
PRO_0000068058

Regions

Nucleotide binding39 – 479FAD By similarity
Nucleotide binding186 – 1905NAD By similarity
Nucleotide binding275 – 2784NAD By similarity

Sites

Active site4511Proton acceptor By similarity
Binding site561FAD By similarity
Binding site1181FAD; via amide nitrogen and carbonyl oxygen By similarity
Binding site2091NAD By similarity
Binding site3181FAD By similarity
Binding site3271FAD; via amide nitrogen By similarity

Amino acid modifications

Disulfide bond47 ↔ 52Redox-active By similarity

Experimental info

Sequence conflict2441S → T in AAA72340. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q04829 [UniParc].

Last modified July 13, 2010. Version 3.
Checksum: 48FFBB56B8EAE65A

FASTA47549,974
        10         20         30         40         50         60 
MVVGDIATGT ELLVIGAGPG GYVAAIRAAQ NGIDTTLVEK DAYGGTCLNY GCIPSKALIT 

        70         80         90        100        110        120 
GANLAHEAGN AEEMGIHADP VVDMSQLRDW KSGVVDQLTG GVEKLCKANG VNLVEGTARF 

       130        140        150        160        170        180 
KDENAVRIAH GGEGQGSETI EFEHCIIATG SRVIQIPGFD FGDEPVWSSR DALEADTVPE 

       190        200        210        220        230        240 
RLVVVGGGYI GMELSTTFAK LGADVTVVEM LDDILPGYES DVARVVRKRA EELGIDMHLG 

       250        260        270        280        290        300 
EGASGWREED DGIMVTTETE DGEENEYRAD KVLVAVGRSP VTDTMDIENA GLEADDRGFL 

       310        320        330        340        350        360 
SVDDRRRTDV EHIYAVGDVV EDTPMLAHVA SKEGIVAAEH VAGEPVAFDS QAVPAAVFTD 

       370        380        390        400        410        420 
PEIGTVGMTE ADAEEAGFTP VVGQMPFRAS GRALTTNHAD GFVRVVADEE SGFVLGAQIV 

       430        440        450        460        470 
GPEASELIAE LAFAIEMGAT LEDVASTIHT HPTLAEAVME AAENALGQAI HTLNR 

« Hide

References

« Hide 'large scale' references
[1]"Dihydrolipoamide dehydrogenase from Haloferax volcanii: gene cloning, complete primary structure, and comparison to other dihydrolipoamide dehydrogenases."
Vettakkorumakankav N.N., Stevenson K.J.
Biochem. Cell Biol. 70:656-663(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 326-348.
[2]"The complete genome sequence of Haloferax volcanii DS2, a model archaeon."
Hartman A.L., Norais C., Badger J.H., Delmas S., Haldenby S., Madupu R., Robinson J., Khouri H., Ren Q., Lowe T.M., Maupin-Furlow J., Pohlschroder M., Daniels C., Pfeiffer F., Allers T., Eisen J.A.
PLoS ONE 5:E9605-E9605(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2.
[3]"Dihydrolipoamide dehydrogenase from the halophilic archaebacterium Haloferax volcanii: characterization and N-terminal sequence."
Vettakkorumakankav N.N., Danson M.J., Hough D.W., Stevenson K.J., Davison M., Young J.
Biochem. Cell Biol. 70:70-75(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-49.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L09733 Genomic DNA. Translation: AAA72340.1.
CP001956 Genomic DNA. Translation: ADE04480.1.
PIRA56824.
RefSeqYP_003536966.1. NC_013967.1.

3D structure databases

ProteinModelPortalQ04829.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaADE04480; ADE04480; HVO_2961.
GeneID8924221.
KEGGhvo:HVO_2961.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHOG000276708.
KOK00382.
OMAGMAAEIY.
ProtClustDBCLSK299101.

Enzyme and pathway databases

BioCycHVOL309800:GCOK-2967-MONOMER.

Family and domain databases

Gene3D3.30.390.30. 1 hit.
InterProIPR016156. 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]
PfamPF00070. Pyr_redox. 1 hit.
PF07992. Pyr_redox_2. 1 hit.
PF02852. Pyr_redox_dim. 1 hit.
[Graphical view]
PRINTSPR00368. FADPNR.
SUPFAMSSF55424. FAD/NAD-linked_reductase_dimer. 1 hit.
TIGRFAMsTIGR01350. lipoamide_DH. 1 hit.
PROSITEPS00076. PYRIDINE_REDOX_1. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameDLDH_HALVD
AccessionPrimary (citable) accession number: Q04829
Secondary accession number(s): D4GY21
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: July 13, 2010
Last modified: May 29, 2013
This is version 98 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families