Reviewed, UniProtKB/Swiss-Prot Q5UWH2 (DLDH3_HALMA)

Names and origin

Protein names

Recommended name:
    Dihydrolipoyl dehydrogenase 3
    EC=1.8.1.4
Alternative name(s):
    Dihydrolipoamide dehydrogenase 3

Gene names

Name:	lpdA3
Ordered Locus Names:	rrnB0197

Organism

Haloarcula marismortui (Halobacterium marismortui) [Complete proteome] [HAMAP]

Taxonomic identifier

2238 [NCBI]

Taxonomic lineage

Archaea › Euryarchaeota › Halobacteria › Halobacteriales › Halobacteriaceae › Haloarcula

Protein attributes

Sequence length	477 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
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
	Chain	1 – 477	477	Dihydrolipoyl dehydrogenase 3		PRO_0000068056
Regions
	Nucleotide binding	39 – 47	9	FAD By similarity
	Nucleotide binding	186 – 190	5	NAD By similarity
	Nucleotide binding	279 – 282	4	NAD By similarity
Sites
	Active site	454	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	322	1	FAD By similarity
	Binding site	330	1	FAD; via amide nitrogen By similarity
Amino acid modifications
	Disulfide bond	47 ↔ 52		Redox-active By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q5UWH2-1 [UniParc]. Last modified December 7, 2004. Version 1. Checksum: 6F17C108465077C1	FASTA	477	50,121
	10 20 30 40 50 60 MVVGDVTTST DVLVIGAGPG GYVAAIRAAQ LALDVTLVEK GEYGGACLNR GCIPSKALIH 70 80 90 100 110 120 GSKLASEAGQ AEELGIYADP TVALDEMINW KDGVVDQLTS GIEQLCTAAG VNLLKGTAEF 130 140 150 160 170 180 ADENKVRIIH QGEGQGSESL KFENCIIATG SRPIEIPGFG FEDERIVSSD GALNFDTVPD 190 200 210 220 230 240 ELVIVGAGYI GMELATVYSR LGSDVSVIEM LEQALPSYEE DIASIVRKRA ERLGVDFHFG 250 260 270 280 290 300 YTADSWAASD GKAVLTAVPA DEAAHDSDIE LTADRILVAV GRRPVTDTLS IDDAGVETNA 310 320 330 340 350 360 QGFIPTDSTC RTNKEHIFAV GDVAGEPMLA HKGSKEGEVA AEVIAGEPAA VDYQALPAAV 370 380 390 400 410 420 FTDPEIGTVG LTENEAANKG MTPVTGEFQF QASGRALTAN RAEGFVRIIA TKETERVIGA 430 440 450 460 470 QIVGPEASEL IAEIAAMIEM GAKLEDIGST VHTHPTLSEA IMEAAQNARE KAIHRRN

References

[1]

"Genome sequence of Haloarcula marismortui: a halophilic archaeon from the Dead Sea." Baliga N.S., Bonneau R., Facciotti M.T., Pan M., Glusman G., Deutsch E.W., Shannon P., Chiu Y., Weng R.S., Gan R.R., Hung P., Date S.V., Marcotte E., Hood L., Ng W.V. Genome Res. 14:2221-2234(2004) [PubMed: 15520287] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 43049 / DSM 3752 / JCM 8966.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AY596298 Genomic DNA. Translation: AAV48381.1.
RefSeq	YP_138087.1.
3D structure databases
SMR	Q5UWH2. Positions 9-468.
ModBase	Search...
Genome annotation databases
GeneID	3130663.
GenomeReviews	Gene locus rrnB0197 in contig AY596298_GR.
KEGG	hma:rrnB0197.
NMPDR	fig|272569.1.peg.3845.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG515043.
OMA	DVVGEPM.
Enzyme and pathway databases
BioCyc	HMAR272569:RRNB0197-MONOMER.
BRENDA	1.8.1.4. 88.
Family and domain databases
InterPro	IPR016156. FAD/NAD-linked_Rdtase_dimer. 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.
TIGRFAMs	TIGR01350. lipoamide_DH. 1 hit.
PROSITE	PS00076. PYRIDINE_REDOX_1. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

DLDH3_HALMA

Accession

Primary (citable) accession number: Q5UWH2

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 21, 2005
Last sequence update:	December 7, 2004
Last modified:	February 9, 2010
This is version 46 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

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