Reviewed, UniProtKB/Swiss-Prot Q04829 (DLDH_HALVO)

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

Organism

Halobacterium volcanii (Haloferax volcanii)

Taxonomic identifier

2246 [NCBI]

Taxonomic lineage

Archaea › Euryarchaeota › Halobacteria › Halobacteriales › Halobacteriaceae › Haloferax

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	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 oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	FAD binding Inferred from electronic annotation. Source: InterPro dihydrolipoyl dehydrogenase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed Ref.2
	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

Sequences

	Sequence		Length	Mass (Da)
	Q04829-1 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: 6894BDE536D205D5	FASTA	475	49,988
	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 EGATGWREED 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

[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: 1339281] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 326-348. Strain: ATCC 29605 / DS2 / DSM 3757 / IFO 14742 / NCIMB 2012.
[2]	"Dihydrolipoamide dehydrogenase from the halophilic archaebacterium Haloferax volcanii: characterization and N-terminal sequence." Vettakkorumakankav N.N., Danson M.J., Hough D.W. Biochem. Cell Biol. 70:70-75(1992) [PubMed: 1581034] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-49.

Cross-references

Sequence databases
EMBLGenBankDDBJ	L09733 Genomic DNA. Translation: AAA72340.1.
PIR	A56824.
3D structure databases
HSSP	HSSP built from PDB template 1EBD based on UniProtKB P11959.
ModBase	Search...
Enzyme and pathway databases
BRENDA	1.8.1.4. 430.
Family and domain databases
InterPro	IPR013027. FAD_pyr_nucl-diS_OxRdtase. IPR000815. Hg_reductase. IPR006258. Lipoamide_DH. IPR004099. Pyr_nucl-diS_OxRdtase_dimer. IPR012999. Pyr_OxRdtase_I_AS. IPR001327. Pyr_OxRdtase_NAD_bd. [Graphical view]
Gene3D	G3DSA:3.30.390.30. Pyr_redox_dim. 1 hit.
PANTHER	PTHR22912:SF20. Lipoamide_DH. 1 hit.
Pfam	PF00070. Pyr_redox. 1 hit. PF07992. Pyr_redox_2. 1 hit. PF02852. Pyr_redox_dim. 1 hit. [Graphical view]
PRINTS	PR00368. FADPNR. PR00945. HGRDTASE.
ProDom	PD000139. FAD_pyr_redox. 1 hit. [Graphical view] [Entries sharing at least one domain]
TIGRFAMs	TIGR01350. lipoamide_DH. 1 hit.
PROSITE	PS00076. PYRIDINE_REDOX_1. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

DLDH_HALVO

Accession

Primary (citable) accession number: Q04829

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1994
Last sequence update:	January 23, 2007
Last modified:	June 16, 2009
This is version 70 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)