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P50970 (DLDH_ZYMMO) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 101. 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
E3 component of pyruvate and 2-oxoglutarate dehydrogenases complexes
Gene names
Name:lpd
Ordered Locus Names:ZMO0512
OrganismZymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4) [Complete proteome] [HAMAP]
Taxonomic identifier264203 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Alphaproteobacteria › Sphingomonadales › Sphingomonadaceae › Zymomonas ›

Protein attributes

Sequence length466 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Lipoamide dehydrogenase is a component of the alpha-ketoacid dehydrogenase complexes By similarity.

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.

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 processGlycolysis
   Cellular componentCytoplasm
   DomainRedox-active center
   LigandFAD
Flavoprotein
NAD
   Molecular functionOxidoreductase
   PTMDisulfide bond
   Technical termComplete proteome
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: 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 – 466466Dihydrolipoyl dehydrogenase
PRO_0000068054

Regions

Nucleotide binding34 – 429FAD By similarity
Nucleotide binding180 – 1845NAD By similarity
Nucleotide binding269 – 2724NAD By similarity

Sites

Active site4451Proton acceptor By similarity
Binding site511FAD By similarity
Binding site1141FAD; via amide nitrogen and carbonyl oxygen By similarity
Binding site2031NAD By similarity
Binding site3111FAD By similarity
Binding site3191FAD; via amide nitrogen By similarity

Amino acid modifications

Disulfide bond42 ↔ 47Redox-active By similarity

Experimental info

Sequence conflict921T → A Ref.1
Sequence conflict921T → A Ref.2
Sequence conflict1231L → R Ref.1
Sequence conflict1231L → R Ref.2
Sequence conflict1911F → L Ref.1
Sequence conflict1911F → L Ref.2
Sequence conflict3321A → D Ref.1
Sequence conflict3321A → D Ref.2
Sequence conflict4231Q → H Ref.1
Sequence conflict4231Q → H Ref.2

Sequences

Sequence LengthMass (Da)Tools
P50970 [UniParc].

Last modified February 15, 2005. Version 3.
Checksum: CDAB257276BBD319

FASTA46649,746
        10         20         30         40         50         60 
MADHFDLIVL GGGPGGYVAA IRAAQLNLKV ALVERVHLGG ICLNWGCIPT KSLLRSAEVY 

        70         80         90        100        110        120 
HEMQNAEAYG LTSFKPDFDL DKIIARSREV ATRLASGVKT LLRKNKVEVI SGVGQLTGNQ 

       130        140        150        160        170        180 
QMLVETTEGE EKILEAKDII IATGARARQL PNVHSDGKHI WTYHHALKPP AMPKKLLVIG 

       190        200        210        220        230        240 
SGAIGIEFAS FYADFGAEVS IVEHAPQILP MEDAEVSAYV AKAFKKRGIR ILTQSALQNL 

       250        260        270        280        290        300 
TPDDEGVTAE IAGADGKVTK ERFSHAIVAI GVVANVENIG LDKLGIKLDR GFIAVDGFGR 

       310        320        330        340        350        360 
TNVDHVWAIG DVAGAPCLAH KASHQGVIAA EAIAGCDHVH PLNTQNIPGC TYARPQVASV 

       370        380        390        400        410        420 
GLTEEKARQQ GYNVKIGNFP FIANGKAIAQ GATDGFVKTV FDADSGALLG AHMVGAEVTE 

       430        440        450        460 
MIQGYTVART LETTEAEIME TIFPHPTLSE AMHESVLAAY GRALHF

« Hide

References

« Hide 'large scale' references
[1]"Cloning, sequencing and expression of the Zymomonas mobilis dihydrolipoamide dehydrogenase gene (lpd) in Escherichia coli."
Bringer-Meyer S., Neveling U., Klasen R., Sahm H.
(In) Bisswanger H., Schellenberger A. (eds.); Biochemistry and physiology of thiamin diphosphate enzymes, pp.382-389, Intemann, Germany (1996)
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 29191 / DSM 3580 / NBRC 13756 / NCIMB 11199 / NRRL B-4490 / ZM6.
[2]"Purification of the pyruvate dehydrogenase multienzyme complex of Zymomonas mobilis and identification and sequence analysis of the corresponding genes."
Neveling U., Klasen R., Bringer-Meyer S., Sahm H.
J. Bacteriol. 180:1540-1548(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 29191 / DSM 3580 / NBRC 13756 / NCIMB 11199 / NRRL B-4490 / ZM6.
[3]"The genome sequence of the ethanologenic bacterium Zymomonas mobilis ZM4."
Seo J.-S., Chong H., Park H.S., Yoon K.-O., Jung C., Kim J.J., Hong J.H., Kim H., Kim J.-H., Kil J.-I., Park C.J., Oh H.-M., Lee J.-S., Jin S.-J., Um H.-W., Lee H.-J., Oh S.-J., Kim J.Y. expand/collapse author list , Kang H.L., Lee S.Y., Lee K.J., Kang H.S.
Nat. Biotechnol. 23:63-68(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 31821 / ZM4 / CP4.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		X82291 Genomic DNA. Translation: CAA57734.1.
X93605 Genomic DNA. Translation: CAA63810.1.
AE008692 Genomic DNA. Translation: AAV89136.1.
PIRS57635.
RefSeqYP_162247.1. NC_006526.2.

3D structure databases

ProteinModelPortalP50970.
ModBaseSearch...

Protein-protein interaction databases

STRING264203.ZMO0512.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAV89136; AAV89136; ZMO0512.
GeneID3189435.
KEGGzmo:ZMO0512.
PATRIC32566346. VBIZymMob102260_0483.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1249.
HOGENOMHOG000276708.
KOK00382.
OMAFKPDGKQ.
ProtClustDBCLSK2524602.

Family and domain databases

Gene3D3.30.390.30. 1 hit.
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]
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_ZYMMO
AccessionPrimary (citable) accession number: P50970
Secondary accession number(s): P96191, Q5NQ69
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: February 15, 2005
Last modified: May 1, 2013
This is version 101 of the entry and version 3 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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