Q04829 (DLDH_HALVD) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Dihydrolipoyl dehydrogenase
EC=1.8.1.4

Alternative name(s):
Dihydrolipoamide dehydrogenase

Gene names

Name:	lpdA
Synonyms:	lpd
Ordered Locus Names:	HVO_2961

Organism

Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2) (Halobacterium volcanii) [Complete proteome] [HAMAP]

Taxonomic identifier

309800 [NCBI]

Taxonomic lineage

cellular organisms › Archaea › Euryarchaeota › Halobacteria › Halobacteriales › Halobacteriaceae › Haloferax › Haloferax volcanii

Protein attributes

Sequence length	475 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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 process	Glycolysis
Cellular component	Cytoplasm
Domain	Redox-active center
Ligand	FAD Flavoprotein NAD
Molecular function	Oxidoreductase
PTM	Disulfide bond
Technical term	Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological_process	cell redox homeostasis Inferred from electronic annotation. Source: InterPro glycolysis Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	dihydrolipoyl 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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed Ref.3
	Chain	2 – 475	474	Dihydrolipoyl dehydrogenase		PRO_0000068058
Regions
	Nucleotide binding	39 – 47	9	FAD By similarity
	Nucleotide binding	186 – 190	5	NAD By similarity
	Nucleotide binding	275 – 278	4	NAD By similarity
Sites
	Active site	451	1	Proton acceptor By similarity
	Binding site	56	1	FAD By similarity
	Binding site	118	1	FAD; via amide nitrogen and carbonyl oxygen By similarity
	Binding site	209	1	NAD By similarity
	Binding site	318	1	FAD By similarity
	Binding site	327	1	FAD; via amide nitrogen By similarity
Amino acid modifications
	Disulfide bond	47 ↔ 52		Redox-active By similarity
Experimental info
	Sequence conflict	244	1	S → T in AAA72340. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q04829 [UniParc]. Last modified July 13, 2010. Version 3. Checksum: 48FFBB56B8EAE65A	FASTA	475	49,974
	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

References

	« Hide 'large scale' referencesShow '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.
PIR	A56824.
RefSeq	YP_003536966.1. NC_013967.1.
3D structure databases
ProteinModelPortal	Q04829.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	ADE04480; ADE04480; HVO_2961.
GeneID	8924221.
KEGG	hvo:HVO_2961.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HOG000276708.
KO	K00382.
OMA	GMAAEIY.
ProtClustDB	CLSK299101.
Enzyme and pathway databases
BioCyc	HVOL309800:GCOK-2967-MONOMER.
Family and domain databases
Gene3D	3.30.390.30. 1 hit.
InterPro	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]
Pfam	PF00070. Pyr_redox. 1 hit. PF07992. Pyr_redox_2. 1 hit. PF02852. Pyr_redox_dim. 1 hit. [Graphical view]
PRINTS	PR00368. FADPNR.
SUPFAM	SSF55424. FAD/NAD-linked_reductase_dimer. 1 hit.
TIGRFAMs	TIGR01350. lipoamide_DH. 1 hit.
PROSITE	PS00076. PYRIDINE_REDOX_1. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

DLDH_HALVD

Accession

Primary (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 status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program