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PELCA:Q60154
Contents
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 |
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 | |||||
part_of |
GO:0005623 |
cell |
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 |
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 |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
enables |
GO:0009055 |
electron transfer activity |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
enables |
GO:0016491 |
oxidoreductase activity |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
enables |
GO:0016668 |
oxidoreductase activity, acting on a sulfur group of donors, NAD(P) as acceptor |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
involved_in |
GO:0045454 |
cell redox homeostasis |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
P |
Seeded From UniProt |
complete | |||
enables |
GO:0050660 |
flavin adenine dinucleotide binding |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
involved_in |
GO:0055114 |
oxidation-reduction process |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
InterPro:IPR004099 |
P |
Seeded From UniProt |
complete | ||
enables |
GO:0004148 |
dihydrolipoyl dehydrogenase activity |
ECO:0000501 |
evidence used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
involved_in |
GO:0055114 |
oxidation-reduction process |
ECO:0000323 |
imported automatically asserted information used in automatic assertion |
P |
Seeded From UniProt |
complete | |||
enables |
GO:0016491 |
oxidoreductase activity |
ECO:0000323 |
imported automatically asserted information used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
Notes
References
See Help:References for how to manage references in GONUTS.
- ↑ 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