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9CAUD:A0A0K2CZZ1
Contents
Species (Taxon ID) | Bacillus phage TsarBomba. (1690456) | |
Gene Name(s) | No Information Provided. | |
Protein Name(s) | Putative phosphoadenosine phosphosulfate reductase (ECO:0000313 with EMBL:ALA13134.1) | |
External Links | ||
UniProt | A0A0K2CZZ1 | |
EMBL | KT224359 | |
RefSeq | YP_009206853.1 | |
GeneID | 26633344 | |
GO | GO:0003824 | |
Gene3D | 3.40.50.620 | |
InterPro | IPR002500 IPR014729 | |
Pfam | PF01507 |
Annotations
Qualifier | GO ID | GO term name | Reference | ECO ID | ECO term name | with/from | Aspect | Extension | Notes | Status |
---|---|---|---|---|---|---|---|---|---|---|
GO:0004604 |
phosphoadenylyl-sulfate reductase (thioredoxin) activity |
ECO:0000250 |
PMID:7588765[1] UniProtKB:WP_001466333.1
|
F |
BlastP shows that the protein is a homolog of phosphoadenosine phosphosulfate reductase (WP_001466333.1 coded by E.coli). The conserved binding domains and sequence similarity provide support for the claim that this protein provides reductase enzymatic activity |
complete | ||||
GO:0003824 |
catalytic activity |
ECO:0000315 |
F |
Figure 2 shows the aligned using ClustaIW and subjected to phylogenetic analysis. Both Analyses resulted in trees of the same topology. |
complete | |||||
GO:0004604 |
phosphoadenylyl-sulfate reductase (thioredoxin) activity |
ECO:0000250 |
|
F |
Sequence alignment via BlastP gave an E value of 1 E-12 and 68 % query cover. This gene can be homolog to phosphoadenylyl-sulfate reductase domain |
complete | ||||
enables |
GO:0003824 |
catalytic activity |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
Notes
References
See Help:References for how to manage references in GONUTS.
- ↑ 1.0 1.1 Berendt, U et al. (1995) Reaction mechanism of thioredoxin: 3'-phospho-adenylylsulfate reductase investigated by site-directed mutagenesis. Eur. J. Biochem. 233 347-56 PubMed GONUTS page
- ↑ Kopriva, S et al. (2007) The putative moss 3'-phosphoadenosine-5'-phosphosulfate reductase is a novel form of adenosine-5'-phosphosulfate reductase without an iron-sulfur cluster. J. Biol. Chem. 282 22930-8 PubMed GONUTS page