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Q9HN74 (DLDH_HALSA) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 82. 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
Ordered Locus Names:VNG_2220G
OrganismHalobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1) (Halobacterium halobium) [Reference proteome] [HAMAP]
Taxonomic identifier64091 [NCBI]
Taxonomic lineageArchaea › Euryarchaeota › Halobacteria › Halobacteriales › Halobacteriaceae › Halobacterium ›

Protein attributes

Sequence length474 AA.
Sequence statusComplete.
Protein existenceInferred from homology

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 By similarity.

Subcellular location

Cytoplasm By similarity.

Miscellaneous

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

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
Reference proteome
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

Chain1 – 474474Dihydrolipoyl dehydrogenase
PRO_0000068057

Regions

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

Sites

Active site4501Proton 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 site3261FAD; via amide nitrogen By similarity

Amino acid modifications

Disulfide bond47 ↔ 52Redox-active By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9HN74 [UniParc].

Last modified March 1, 2001. Version 1.
Checksum: 82A3B7B8C58DB70F

FASTA47449,151
        10         20         30         40         50         60 
MVVGDISTGT DVAVVGAGPG GYVAAIRAGQ LGLDVTLVEK DAYGGTCLNY GCIPSKAMIT 

        70         80         90        100        110        120 
ASGVAHEAGH AEEMGVYADP DVDVAEMVDW KDGVVDQLTG GVEKLCKANG VNLIEGRAEF 

       130        140        150        160        170        180 
AGSDKLRVVH GGDGQGSETI EYEHAIVSTG SRPIEVPGFD FGDDPVLDSR QALAMAELPS 

       190        200        210        220        230        240 
SMVIVGGGYI GMELSTVFAK LGVDVTVVEM LDGILPQYGD DIARPVRQRA EELGIDFHFG 

       250        260        270        280        290        300 
LAADSWTDTD DGIVVTAADE DGEETEFETE KVLVAVGRQP VTDTLNLDAV GLEPNDDGRL 

       310        320        330        340        350        360 
ETDHEARTDV ENVFAIGDVA PGPMLAHKAS KEGEVAAEVI AGEPAALDYQ AVPAAVFTDP 

       370        380        390        400        410        420 
EIGTVGLTED DAAAQGFDPV VGTFPFNASG RALTTGHDDG FVEVVADEES GFLLGAQIVG 

       430        440        450        460        470 
PEASELVAEL GLAIEMGATL EDVASTIHTH PTLSEATMEA AEHALGHAVH TLNR

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE004437 Genomic DNA. Translation: AAG20347.1.
PIRG84372.
RefSeqNP_280867.1. NC_002607.1.

3D structure databases

ProteinModelPortalQ9HN74.
ModBaseSearch...

Protein-protein interaction databases

STRING64091.VNG2220G.

Proteomic databases

PaxDbQ9HN74.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAG20347; AAG20347; VNG_2220G.
GeneID1448649.
KEGGhal:VNG2220G.

Phylogenomic databases

eggNOGCOG1249.
KOK00382.
OMAGFEKQMS.
ProtClustDBCLSK299101.

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]
PANTHERPTHR22912:SF20. PTHR22912:SF20. 1 hit.
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_HALSA
AccessionPrimary (citable) accession number: Q9HN74
Entry history
Integrated into UniProtKB/Swiss-Prot: June 21, 2005
Last sequence update: March 1, 2001
Last modified: May 1, 2013
This is version 82 of the entry and version 1 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

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