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PELCA:Q60154

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Species (Taxon ID) Pelobacter carbinolicus. (19)
Gene Name(s) acoL (ECO:0000313 with EMBL:AAA91879.1)
Protein Name(s) Dihydrolipoyl dehydrogenase (ECO:0000256 with RuleBase:RU003692)
External Links
UniProt Q60154
EMBL U01100
L24124
PIR F36953
RefSeq YP_006716019.1
ProteinModelPortal Q60154
GeneID 3723480
KEGG pca:Pcar_0347
PATRIC 22886616
KO K00382
OrthoDB EOG6QCD6D
GO GO:0004148
GO:0050660
GO:0045454
Gene3D 3.30.390.30
InterPro IPR016156
IPR013027
IPR006258
IPR004099
IPR023753
IPR012999
IPR001327
Pfam PF00070
PF07992
PF02852
PRINTS PR00368
SUPFAM SSF55424
TIGRFAMs TIGR01350
PROSITE PS00076

Annotations

Qualifier GO ID GO term name Reference ECO ID ECO term name with/from Aspect Extension Notes Status
GO:0004148

dihydrolipoyl dehydrogenase activity

PMID:1898934[1]

ECO:0000021

F

Codes for a subunit(dihydrolipoamide dehydrogenase)that dimerizes to become the E3 subunit dihydrolipoamide dehydrogenase (DHLDH) in the acetoin dehydrogenase complex that catalyzes the conversion of acetoin to acetyl-CoA and acetaldehyde. Table 6 indicates DHLDH is only present in high activity in acetoin utilizing cultures. Fig. 4 illustrates growth of P. carbinolicus in double immunodiffusion tests that gave strong cross-reactions only between organisms capable of utilizing and degrading acetoin

Missing: with/from
CACAO 4081

part_of

GO:0005623

cell

GO_REF:0000108

ECO:0000366

evidence based on logical inference from automatic annotation used in automatic assertion

GO:0045454

C

Seeded From UniProt

complete

involved_in

GO:0022900

electron transport chain

GO_REF:0000108

ECO:0000366

evidence based on logical inference from automatic annotation used in automatic assertion

GO:0009055

P

Seeded From UniProt

complete

enables

GO:0004148

dihydrolipoyl dehydrogenase activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR006258

F

Seeded From UniProt

complete

enables

GO:0009055

electron transfer activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR001100

F

Seeded From UniProt

complete

enables

GO:0016491

oxidoreductase activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR001100
InterPro:IPR016156
InterPro:IPR023753

F

Seeded From UniProt

complete

enables

GO:0016668

oxidoreductase activity, acting on a sulfur group of donors, NAD(P) as acceptor

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR012999

F

Seeded From UniProt

complete

involved_in

GO:0045454

cell redox homeostasis

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR004099

P

Seeded From UniProt

complete

enables

GO:0050660

flavin adenine dinucleotide binding

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR006258
InterPro:IPR016156

F

Seeded From UniProt

complete

involved_in

GO:0055114

oxidation-reduction process

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR004099
InterPro:IPR006258
InterPro:IPR012999
InterPro:IPR016156
InterPro:IPR023753

P

Seeded From UniProt

complete

enables

GO:0004148

dihydrolipoyl dehydrogenase activity

GO_REF:0000003

ECO:0000501

evidence used in automatic assertion

EC:1.8.1.4

F

Seeded From UniProt

complete

involved_in

GO:0055114

oxidation-reduction process

GO_REF:0000038

ECO:0000323

imported automatically asserted information used in automatic assertion

UniProtKB-KW:KW-0560

P

Seeded From UniProt

complete

enables

GO:0016491

oxidoreductase activity

GO_REF:0000038

ECO:0000323

imported automatically asserted information used in automatic assertion

UniProtKB-KW:KW-0560

F

Seeded From UniProt

complete

Notes

References

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

  1. Oppermann, FB et al. (1991) Purification and characterization of acetoin:2,6-dichlorophenolindophenol oxidoreductase, dihydrolipoamide dehydrogenase, and dihydrolipoamide acetyltransferase of the Pelobacter carbinolicus acetoin dehydrogenase enzyme system. J. Bacteriol. 173 757-67 PubMed GONUTS page