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CLOAB:Q9ANR5
Contents
Species (Taxon ID) | Clostridium acetobutylicum. (1488) | |
Gene Name(s) | adhE2 (ECO:0000313 with EMBL:AAK09379.1) | |
Protein Name(s) | Aldehyde-alcohol dehydrogenase (ECO:0000256 with PIRNR:PIRNR000111) | |
External Links | ||
UniProt | Q9ANR5 | |
EMBL | AF321779 | |
RefSeq | NP_149199.1 YP_009076789.1 | |
ProteinModelPortal | Q9ANR5 | |
STRING | 272562.CA_P0035 | |
GeneID | 1116040 | |
KEGG | cac:CA_P0035 | |
PATRIC | 32033950 | |
HOGENOM | HOG000025256 | |
KO | K04072 | |
OrthoDB | EOG6TFCQS | |
BioCyc | MetaCyc:MONOMER-15847 | |
GO | GO:0008774 GO:0004022 GO:0004029 GO:0046872 GO:0071271 GO:0015976 | |
Gene3D | 3.40.309.10 3.40.605.10 | |
InterPro | IPR001670 IPR018211 IPR016161 IPR016163 IPR016162 IPR015590 IPR012079 | |
Pfam | PF00171 PF00465 | |
PIRSF | PIRSF000111 | |
SUPFAM | SSF53720 | |
PROSITE | PS00913 PS00060 |
Annotations
Qualifier | GO ID | GO term name | Reference | ECO ID | ECO term name | with/from | Aspect | Extension | Notes | Status |
---|---|---|---|---|---|---|---|---|---|---|
involved_in |
GO:0071271 |
1-butanol biosynthetic process |
ECO:0000314 |
direct assay evidence used in manual assertion |
P |
Seeded From UniProt |
complete | |||
enables |
GO:0004029 |
aldehyde dehydrogenase (NAD) activity |
ECO:0000314 |
direct assay evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
enables |
GO:0004022 |
alcohol dehydrogenase (NAD) activity |
ECO:0000314 |
direct assay evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
enables |
GO:0004022 |
alcohol dehydrogenase (NAD) activity |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
involved_in |
GO:0006066 |
alcohol metabolic process |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
P |
Seeded From UniProt |
complete | |||
enables |
GO:0008774 |
acetaldehyde dehydrogenase (acetylating) activity |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
involved_in |
GO:0015976 |
carbon utilization |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
P |
Seeded From UniProt |
complete | |||
enables |
GO:0016491 |
oxidoreductase activity |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
InterPro:IPR001670 |
F |
Seeded From UniProt |
complete | ||
enables |
GO:0016620 |
oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
GO:0004022 |
alcohol dehydrogenase (NAD) activity |
ECO:0000314 |
F |
See figures 1, 2, 5. The adhE2 gene of Clostridium acetobutylicum ATCC 824, coding for an aldehyde/alcohol dehydrogenase (AADH), was characterized from molecular and biochemical points of view. The 2,577-bp adhE2 codes for a 94.4-kDa protein. adhE2 is expressed, as a monocistronic operon, in alcohologenic cultures and not in solventogenic cultures. Primer extension analysis identified two transcriptional start sites 160 and 215 bp upstream of the adhE2 start codon. The expression of adhE2 from a plasmid in the DG1 mutant of C. acetobutylicum, a mutant cured of the pSOL1 megaplasmid, restored butanol production and provided elevated activities of NADH-dependent butyraldehyde and butanol dehydrogenases. The recombinant AdhE2 protein expressed in E. coli as a Strep-tag fusion protein and purified to homogeneity also demonstrated NADH-dependent butyraldehyde and butanol dehydrogenase activities. This is the second AADH identified in C. acetobutylicum ATCC 824, and to our knowledge this is the first example of a bacterium with two AADHs. It is noteworthy that the two corresponding genes, adhE and adhE2, are carried by the pSOL1 megaplasmid of C. acetobutylicum ATCC 824. |
complete | |||||
enables |
GO:0046872 |
metal ion 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:IPR001670 |
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 | |||
involved_in |
GO:0055114 |
oxidation-reduction process |
ECO:0000323 |
imported automatically asserted information used in automatic assertion |
P |
Seeded From UniProt |
complete | |||
enables |
GO:0004022 |
alcohol dehydrogenase (NAD) activity |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
UniRule:UR000132767 |
F |
Seeded From UniProt |
complete | ||
enables |
GO:0008774 |
acetaldehyde dehydrogenase (acetylating) activity |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
UniRule:UR000132767 |
F |
Seeded From UniProt |
complete | ||
Notes
References
See Help:References for how to manage references in GONUTS.
- ↑ 1.0 1.1 1.2 1.3 Fontaine, L et al. (2002) Molecular characterization and transcriptional analysis of adhE2, the gene encoding the NADH-dependent aldehyde/alcohol dehydrogenase responsible for butanol production in alcohologenic cultures of Clostridium acetobutylicum ATCC 824. J. Bacteriol. 184 821-30 PubMed GONUTS page
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