Reviewed, UniProtKB/Swiss-Prot P85207 (DLDH_THESC)

Names and origin

Protein names

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

Gene names

Name:

lpd

Organism

Thermus scotoductus

Taxonomic identifier

37636 [NCBI]

Taxonomic lineage

Bacteria › Deinococcus-Thermus › Deinococci › Thermales › Thermaceae › Thermus

Protein attributes

Sequence length	461 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Has chromate reductase activity. Ref.1
Catalytic activity	Protein N(6)-(dihydrolipoyl)lysine + NAD+ = protein N(6)-(lipoyl)lysine + NADH. UniProtKB P11959
Cofactor	Binds 1 FAD per subunit. Ref.1
Subunit structure	Homodimer By similarity. UniProtKB P11959
Subcellular location	Membrane; Peripheral membrane protein Ref.1.
Miscellaneous	The active site is a redox-active disulfide bond By similarity. UniProtKB P11959
Sequence similarities	Belongs to the class-I pyridine nucleotide-disulfide oxidoreductase family.
Biophysicochemical properties	Kinetic parameters: KM=55.46 µM for Cr(VI) Ref.1 Vmax=2.262 µmol/min/mg enzyme toward Cr(VI) Ref.1 pH dependence: Optimum pH is 6.5. Ref.1 Temperature dependence: Optimum temperature is 65 degrees Celsius. Ref.1

Ontologies

Keywords
Biological process	Glycolysis
Cellular component	Membrane
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: InterPro extrinsic to membrane 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 – 461	461	Dihydrolipoyl dehydrogenase		PRO_0000315941
Regions
	Nucleotide binding	33 – 41	9	FAD By similarity UniProtKB P11959
	Nucleotide binding	173 – 177	5	NAD By similarity
	Nucleotide binding	263 – 266	4	NAD By similarity
Sites
	Active site	437	1	Proton acceptor By similarity UniProtKB P11959
	Binding site	50	1	FAD By similarity
	Binding site	112	1	FAD; via amide nitrogen and carbonyl oxygen By similarity
	Binding site	196	1	NAD By similarity
	Binding site	306	1	FAD By similarity
	Binding site	314	1	FAD; via amide nitrogen By similarity
Amino acid modifications
	Disulfide bond	41 ↔ 46		Redox-active By similarity UniProtKB P11959

Sequences

	Sequence		Length	Mass (Da)
	P85207-1 [UniParc]. Last modified February 26, 2008. Version 2. Checksum: 3B4A1719A22BF200	FASTA	461	48,505
	10 20 30 40 50 60 MKTYDLIVIG TGPGGYPAAI RGAQLGLKVL AVEAAEVGGV CLNVGCIPTK ALLHAAETVH 70 80 90 100 110 120 HLKGAEGFGL KAKPELDLKK LGAWRDGVVK KLTGGVAGLL KGNKVELLRG FARFKGPREI 130 140 150 160 170 180 EVNGETYGAQ SFIIATGSEP MPLKGFPFGE DVWDSTRALR VEEGIPKRLL VIGGGAVGLE 190 200 210 220 230 240 LGQIYHRLGS EVTLIEYMPE ILPAGDRETA ALLRKALEKE GLKVRTGTKA VGYEKKQDGL 250 260 270 280 290 300 HVLLEAAQGG SQEEIVVDKI LVAVGRRPRT EGLGLEKAGV KVDERGFIQV NARMETSAPG 310 320 330 340 350 360 VYAIGDVARP PLLAHKAMKE GLVAAENAAG KNALFDFQVP SVVYTGPEWA GVGLTEEEAR 370 380 390 400 410 420 KAGYNVKVGK FPFSASGRAL TLGGAEGLIK VVGDAETDLL LGVFVVGPQA GELIAEATLA 430 440 450 460 LEMGATVSDL GLTIHPHPTL SEGLMEAAEA LHKQAIHILN R

References

[1]

"A membrane-associated protein with Cr(VI)-reducing activity from Thermus scotoductus SA-01." Opperman D.J., van Heerden E. FEMS Microbiol. Lett. 280:210-218(2008) [PubMed: 18218019] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-14, FUNCTION, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION. Strain: ATCC 700910 / SA-01.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AM749392 Genomic DNA. Translation: CAO77701.1. Different initiation.
3D structure databases
SMR	P85207. Positions 1-460.
ModBase	Search...
Enzyme and pathway databases
BRENDA	1.8.1.4. 1133.
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

DLDH_THESC

Accession

Primary (citable) accession number: P85207
Secondary accession number(s): A9JPS7

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 15, 2008
Last sequence update:	February 26, 2008
Last modified:	February 9, 2010
This is version 20 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)