lpd:Gene Product(s)

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Nomenclature Function Interactions Localization Sequence Domains Structure Resources Accessions Links References Suggestions

Nomenclature

See Help:Product_nomenclature for help entering or editing information in this section of EcoliWiki.

Standard name

Lpd

Synonyms

lipoamide dehydrogenase, E3 component is part of three enzyme complexes[1], B0116[2][1], Lpd[2][1], Dhl[2][1], LpdA[2][1] , dhl, ECK0115, JW0112, lpdA, b0116

Product description

E3[2][3];

Component of E3-CPLX[2]; lipoamide dehydrogenase[3]; 2-oxoglutarate dehydrogenase complex[2][3]; gcv system[2][3]; pyruvate dehydrogenase multienzyme complex[2][3]

Lipoamide dehydrogenase, NADH-dependent; E3 component of pyruvate and 2-oxoglutarate dehydrogenase complexes; also functions as glycine cleavage system L protein; binds Zn(II)[4]

EC number (for enzymes)
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Notes

Function

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<protect> Gene Ontology
See Help:Gene_ontology for help entering or editing GO terms and GO annotations in EcoliWiki.

Qualifier GO ID GO term name Reference Evidence Code with/from Aspect Notes Status
GO:0004148

dihydrolipoyl dehydrogenase activity

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR006258

F

Seeded from EcoCyc (v14.0)

complete

GO:0004148

dihydrolipoyl dehydrogenase activity

GOA:spec
GO_REF:0000003

IEA: Inferred from Electronic Annotation

EC:1.8.1.4

F

Seeded from EcoCyc (v14.0)

complete

GO:0005829

cytosol

PMID:16858726[5]

IDA: Inferred from Direct Assay

C

Seeded from EcoCyc (v14.0)

complete

GO:0005886

plasma membrane

GOA:spkw
SP_KW:GO_REF:0000004

IEA: Inferred from Electronic Annotation

SP_KW:KW-0997

C

Seeded from EcoCyc (v14.0)

complete

GO:0005886

plasma membrane

GOA:spkw
SP_KW:GO_REF:0000004

IEA: Inferred from Electronic Annotation

SP_KW:KW-1003

C

Seeded from EcoCyc (v14.0)

complete

GO:0006096

glycolysis

GOA:spkw
SP_KW:GO_REF:0000004

IEA: Inferred from Electronic Annotation

SP_KW:KW-0324

P

Seeded from EcoCyc (v14.0)

complete

GO:0016020

membrane

GOA:spkw
SP_KW:GO_REF:0000004

IEA: Inferred from Electronic Annotation

SP_KW:KW-0472

C

Seeded from EcoCyc (v14.0)

complete

GO:0016020

membrane

PMID:16858726[5]

IDA: Inferred from Direct Assay

C

Seeded from EcoCyc (v14.0)

complete

GO:0019898

extrinsic to membrane

GO_REF:0000023

IEA: Inferred from Electronic Annotation

SP_SL:SL-9903

C

Seeded from EcoCyc (v14.0)

complete

GO:0045454

cell redox homeostasis

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR004099

P

Seeded from EcoCyc (v14.0)

complete

GO:0050660

FAD binding

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR000815

F

Seeded from EcoCyc (v14.0)

complete

GO:0050660

FAD binding

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR001327

F

Seeded from EcoCyc (v14.0)

complete

GO:0050660

FAD binding

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR004099

F

Seeded from EcoCyc (v14.0)

complete

GO:0050660

FAD binding

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR006258

F

Seeded from EcoCyc (v14.0)

complete

GO:0050660

FAD binding

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR016156

F

Seeded from EcoCyc (v14.0)

complete

GO:0055114

oxidation reduction

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR000815

P

Seeded from EcoCyc (v14.0)

complete

GO:0055114

oxidation reduction

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR001327

P

Seeded from EcoCyc (v14.0)

complete

GO:0055114

oxidation reduction

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR004099

P

Seeded from EcoCyc (v14.0)

complete

GO:0055114

oxidation reduction

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR006258

P

Seeded from EcoCyc (v14.0)

complete

GO:0055114

oxidation reduction

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR016156

P

Seeded from EcoCyc (v14.0)

complete

GO:0055114

oxidation reduction

GOA:spkw
SP_KW:GO_REF:0000004

IEA: Inferred from Electronic Annotation

SP_KW:KW-0560

P

Seeded from EcoCyc (v14.0)

complete

GO:0004148

dihydrolipoyl dehydrogenase activity

PMID:3066354[6]

IDA: Inferred from Direct Assay

F

complete

GO:0055114

oxidation reduction

PMID:3066354[6]

IDA: Inferred from Direct Assay

P

complete

GO:0006103

2-oxoglutarate metabolic process

PMID:4197899[7]

IMP: Inferred from Mutant Phenotype

P

complete

GO:0008270

zinc ion binding

PMID:11985624[8]

IDA: Inferred from Direct Assay

F

complete

GO:0006090

pyruvate metabolic process

PMID:4197899[7]

IMP: Inferred from Mutant Phenotype

P

complete

GO:0006103

2-oxoglutarate metabolic process

PMID:6311808[9]

IGI: Inferred from Genetic Interaction

EcoliWiki:sucA|EcoliWiki:sucB

P

complete

GO:0006090

pyruvate metabolic process

PMID:6311808[9]

IDA: Inferred from Direct Assay

P

complete

GO:0050660

FAD binding

PMID:4863745[10]

IDA: Inferred from Direct Assay

F

complete

GO:0015036

disulfide oxidoreductase activity

PMID:4863745[10]

IDA: Inferred from Direct Assay

F

complete

GO:0005737

cytoplasm

PMID:4863745[10]

IDA: Inferred from Direct Assay

C

complete

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Interactions See Help:Product_interactions for help entering or editing information about gene product interactions in this section of EcoliWiki.

Partner Type Partner Notes References Evidence

Protein

Subunits of E3-CPLX

could be indirect

Protein

iscS

PMID:16606699[11]

Experiment(s):EBI-1135611

Protein

aceE

PMID:16606699[11]

Experiment(s):EBI-1135611

Protein

ribB

PMID:16606699[11]

Experiment(s):EBI-1135611

Protein

Subunits of 2-oxoglutarate dehydrogenase complex

could be indirect

Protein

Subunits of gcv system

could be indirect

Protein

Subunits of pyruvate dehydrogenase multienzyme complex

could be indirect


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Notes

Localization

See Help:Product_localization for how to add or edit information in this section of EcoliWiki.

Compartment Description Evidence Reference/Source Notes

Cytoplasm

PMID:9298646[12], PMID:6352260[13]

EchoLocation:lpd


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Notes

Structure and Physical Properties

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<protect> Physical Properties See Help:Product_physical_properties for help entering or editing information about the physical properties of this gene product.

Name
Sequence

at EcoCyc 

MSTEIKTQVV VLGAGPAGYS AAFRCADLGL ETVIVERYNT LGGVCLNVGC IPSKALLHVA
KVIEEAKALA EHGIVFGEPK TDIDKIRTWK EKVINQLTGG LAGMAKGRKV KVVNGLGKFT
GANTLEVEGE NGKTVINFDN AIIAAGSRPI QLPFIPHEDP RIWDSTDALE LKEVPERLLV
MGGGIIGLEM GTVYHALGSQ IDVVEMFDQV IPAADKDIVK VFTKRISKKF NLMLETKVTA
VEAKEDGIYV TMEGKKAPAE PQRYDAVLVA IGRVPNGKNL DAGKAGVEVD DRGFIRVDKQ
LRTNVPHIFA IGDIVGQPML AHKGVHEGHV AAEVIAGKKH YFDPKVIPSI AYTEPEVAWV
GLTEKEAKEK GISYETATFP WAASGRAIAS DCADGMTKLI FDKESHRVIG GAIVGTNGGE
LLGEIGLAIE MGCDAEDIAL TIHAHPTLHE SVGLAAEVFE GSITDLPNPK AKKK
Length

474

Mol. Wt

50.688 kDa

pI

6.1 (calculated)

Extinction coefficient

33,920 - 34,545 (calc based on 8 Y, 4 W, and 5 C residues)

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Domains/Motifs/Modification Sites

See Help:Product_domains_motifs for help entering or editing information in this section of EcoliWiki.

Type Residues Description Notes References

Initiator Methionine

1

Removed

UniProt:P0A9P0

Domain

177..257

PF00070 Pyridine nucleotide-disulphide oxidoreductase

PMID:19920124[14]

Domain

347..456

PF02852 Pyridine nucleotide-disulphide oxidoreductase, dimerisation domain

PMID:19920124[14]

Domain

8..319

PF07992 Pyridine nucleotide-disulphide oxidoreductase

PMID:19920124[14]

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<motif_map/>

Structure
See Help:Product_structure for help entering or editing information in this section of EcoliWiki.

Structures

<beststructure> gene=lpd taxon=562,83333 </beststructure>

Models

View models at:

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Structure figures

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Notes

Gene Product Resources

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See Help:Product_resources for help with entering or editing information in this section of EcoliWiki.

Resource type Source Notes/Reference
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Notes

Accessions in Other Databases

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See Help:Gene_accessions for help with entering information into the Gene Accessions table.

Database Accession Notes

NCBI (Protein) (EcoliWiki Page)

GI:16128109

Escherichia coli str. K-12 substr. MG1655

NCBI (Protein) (EcoliWiki Page)

GeneID:944854

Escherichia coli str. K-12 substr. MG1655

ASAP

ASAP:ABE-0000404

Escherichia coli str. K-12 substr. MG1655

UniProt (EcoliWiki Page)

UniProtKB/Swiss-Prot:P0A9P0

Escherichia coli str. K-12 substr. MG1655

EcoCyc

EcoCyc:EG10543

Escherichia coli str. K-12 substr. MG1655

EcoGene

EcoGene:EG10543

Escherichia coli str. K-12 substr. MG1655

NCBI (Gene) (EcoliWiki Page)

GeneID:944854

Escherichia coli str. K-12 substr. MG1655

RegulonDB

RegulonDB:ECK120000536

Escherichia coli str. K-12 substr. MG1655

EchoBASE

EchoBASE:EB0538

Escherichia coli str. K-12 substr. MG1655

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Notes

Links

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References

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See Help:References for how to manage references in EcoliWiki.

  1. ↑ 1.0 1.1 1.2 1.3 1.4 1.5 Riley, M. et al. (2006) Nucleic Acids Res 34:1-6 (corrected supplemental data from B. Wanner)
  2. ↑ 2.0 2.1 2.2 2.3 2.4 2.5 2.6 2.7 2.8 EcoCyc (release 10.6; 2007) Keseler, IM et al. (2005) Nucleic Acids Res. 33(Database issue):D334-7
  3. ↑ 3.0 3.1 3.2 3.3 3.4 EcoCyc (release 11.1; 2007) Keseler, IM et al. (2005) Nucleic Acids Res. 33(Database issue):D334-7
  4. ↑ EcoGene: Rudd, KE (2000) EcoGene: a genome sequence database for Escherichia coli K-12. Nucleic Acids Res 28:60-4.
  5. ↑ 5.0 5.1 Lasserre, JP et al. (2006) A complexomic study of Escherichia coli using two-dimensional blue native/SDS polyacrylamide gel electrophoresis. Electrophoresis 27 3306-21 PubMed
  6. ↑ 6.0 6.1 Allison, N et al. (1988) Overexpression and mutagenesis of the lipoamide dehydrogenase of Escherichia coli. Biochem. J. 256 741-9 PubMed
  7. ↑ 7.0 7.1 Alwine, JC et al. (1973) Characterization of an Escherichia coli mutant deficient in dihydrolipoyl dehydrogenase activity. J. Bacteriol. 115 1-8 PubMed
  8. ↑ Katayama, A et al. (2002) Systematic search for zinc-binding proteins in Escherichia coli. Eur. J. Biochem. 269 2403-13 PubMed
  9. ↑ 9.0 9.1 Smith, MW & Neidhardt, FC (1983) 2-Oxoacid dehydrogenase complexes of Escherichia coli: cellular amounts and patterns of synthesis. J. Bacteriol. 156 81-8 PubMed
  10. ↑ 10.0 10.1 10.2 Williams, CH Jr et al. (1967) Lipoamide dehydrogenase, glutathione reductase, thioredoxin reductase, and thioredoxin. J. Biol. Chem. 242 5226-31 PubMed
  11. ↑ 11.0 11.1 11.2 Arifuzzaman, M et al. (2006) Large-scale identification of protein-protein interaction of Escherichia coli K-12. Genome Res. 16 686-91 PubMed
  12. ↑ Link, AJ et al. (1997) Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12. Electrophoresis 18 1259-313 PubMed
  13. ↑ Stephens, PE et al. (1983) Nucleotide sequence of the lipoamide dehydrogenase gene of Escherichia coli K12. Eur. J. Biochem. 135 519-27 PubMed
  14. ↑ 14.0 14.1 14.2 Finn, RD et al. (2010) The Pfam protein families database. Nucleic Acids Res. 38 D211-22 PubMed

Categories

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