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P85207 (DLDH_THESS) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 32. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Dihydrolipoyl dehydrogenase
EC=1.8.1.4
Alternative name(s):
Dihydrolipoamide dehydrogenase
Gene names
Name:lpd
Synonyms:lpdA1
Ordered Locus Names:TSC_c02350
OrganismThermus scotoductus (strain ATCC 700910 / SA-01) [Complete proteome] [HAMAP]
Taxonomic identifier743525 [NCBI]
Taxonomic lineageBacteria › Deinococcus-Thermus › Deinococci › Thermales › Thermaceae › Thermus

Protein attributes

Sequence length461 AA.
Sequence statusComplete.
Protein existenceEvidence 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

Sequence caution

The sequence CAO77701.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
   Biological processGlycolysis
   Cellular componentMembrane
   DomainRedox-active center
   LigandFAD
Flavoprotein
NAD
   Molecular functionOxidoreductase
   PTMDisulfide bond
   Technical termComplete proteome
Direct protein sequencing
Gene Ontology (GO)
   Biological processcell redox homeostasis

Inferred from electronic annotation. Source: InterPro

glycolysis

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: InterPro

membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functiondihydrolipoyl 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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 461461Dihydrolipoyl dehydrogenase
PRO_0000315941

Regions

Nucleotide binding33 – 419FAD By similarity UniProtKB P11959
Nucleotide binding173 – 1775NAD By similarity
Nucleotide binding263 – 2664NAD By similarity

Sites

Active site4371Proton acceptor By similarity UniProtKB P11959
Binding site501FAD By similarity
Binding site1121FAD; via amide nitrogen and carbonyl oxygen By similarity
Binding site1961NAD By similarity
Binding site3061FAD By similarity
Binding site3141FAD; via amide nitrogen By similarity

Amino acid modifications

Disulfide bond41 ↔ 46Redox-active By similarity UniProtKB P11959

Sequences

Sequence LengthMass (Da)Tools
P85207 [UniParc].

Last modified February 26, 2008. Version 2.
Checksum: 3B4A1719A22BF200

FASTA46148,505
        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

« Hide

References

« Hide 'large scale' 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.
[2]"The genome sequence of Thermus scotoductus SA-01."
Gounder K., Liesegang H., Brzuszkiewicz E., Wollherr A., Daniel R., Gottschalk G., van Heerden E., Litthauer D.
Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 700910 / SA-01.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AM749392 Genomic DNA. Translation: CAO77701.1. Different initiation.
CP001962 Genomic DNA. Translation: ADW20875.1.
RefSeqYP_004201424.1. NC_014974.1.

3D structure databases

ProteinModelPortalP85207.
SMRP85207. Positions 1-460.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID10176356.
GenomeReviewsGene locus TSC_c02350 in contig CP001962_GR.
KEGGtsc:TSC_c02350.
PATRIC47043314. VBITheSco147128_0221.

Organism-specific databases

CMRSearch...

Family and domain databases

InterProIPR016156. 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]
Gene3DG3DSA:3.30.390.30. Pyr_redox_dim. 1 hit.
KOK00382.
PANTHERPTHR22912:SF20. Lipoamide_DH. 1 hit.
PfamPF00070. Pyr_redox. 1 hit.
PF07992. Pyr_redox_2. 1 hit.
PF02852. Pyr_redox_dim. 1 hit.
[Graphical view]
PRINTSPR00368. FADPNR.
SUPFAMSSF55424. FAD/NAD-linked_reductase_dimer. 1 hit.
TIGRFAMsTIGR01350. Lipoamide_DH. 1 hit.
PROSITEPS00076. PYRIDINE_REDOX_1. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameDLDH_THESS
AccessionPrimary (citable) accession number: P85207
Secondary accession number(s): A9JPS7, E8PKA3
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: February 26, 2008
Last modified: January 25, 2012
This is version 32 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

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