Q9HN74 (DLDH_HALSA) 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
Ordered Locus Names:	VNG_2220G

Organism

Halobacterium salinarium (strain ATCC 700922 / JCM 11081 / NRC-1) (Halobacterium halobium)

Taxonomic identifier

64091 [NCBI]

Taxonomic lineage

Archaea › Euryarchaeota › Halobacteria › Halobacteriales › Halobacteriaceae › Halobacterium

Protein attributes

Sequence length	474 AA.
Sequence status	Complete.
Protein existence	Inferred 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 process	Glycolysis
Cellular component	Cytoplasm
Domain	Redox-active center
Ligand	FAD Flavoprotein NAD
Molecular function	Oxidoreductase
PTM	Disulfide bond
Technical term	Complete proteome Reference proteome
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
	Chain	1 – 474	474	Dihydrolipoyl dehydrogenase		PRO_0000068057
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	450	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	326	1	FAD; via amide nitrogen By similarity
Amino acid modifications
	Disulfide bond	47 ↔ 52		Redox-active By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9HN74 [UniParc]. Last modified March 1, 2001. Version 1. Checksum: 82A3B7B8C58DB70F	FASTA	474	49,151
	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

References

[1]

"Genome sequence of Halobacterium species NRC-1." Ng W.V., Kennedy S.P., Mahairas G.G., Berquist B., Pan M., Shukla H.D., Lasky S.R., Baliga N.S., Thorsson V., Sbrogna J., Swartzell S., Weir D., Hall J., Dahl T.A., Welti R., Goo Y.A., Leithauser B., Keller K. , Cruz R., Danson M.J., Hough D.W., Maddocks D.G., Jablonski P.E., Krebs M.P., Angevine C.M., Dale H., Isenbarger T.A., Peck R.F., Pohlschroder M., Spudich J.L., Jung K.-H., Alam M., Freitas T., Hou S., Daniels C.J., Dennis P.P., Omer A.D., Ebhardt H., Lowe T.M., Liang P., Riley M., Hood L., DasSarma S. Proc. Natl. Acad. Sci. U.S.A. 97:12176-12181(2000) [PubMed: 11016950] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 700922 / JCM 11081 / NRC-1.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE004437 Genomic DNA. Translation: AAG20347.1.
PIR	G84372.
RefSeq	NP_280867.1. NC_002607.1.
3D structure databases
ProteinModelPortal	Q9HN74.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	1448649.
GenomeReviews	Gene locus VNG_2220G in contig AE004437_GR.
KEGG	hal:VNG2220G.
NMPDR	fig|64091.1.peg.1893.
Phylogenomic databases
HOGENOM	HBG515043.
OMA	IPAICFT.
PhylomeDB	Q9HN74.
ProtClustDB	CLSK299101.
Enzyme and pathway databases
BioCyc	HSP64091:VNG2220G-MONOMER.
Family and domain databases
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]
Gene3D	G3DSA:3.30.390.30. Pyr_redox_dim. 1 hit.
KO	K00382.
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.
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_HALSA

Accession

Primary (citable) accession number: Q9HN74

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 21, 2005
Last sequence update:	March 1, 2001
Last modified:	December 14, 2011
This is version 74 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program