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9CAUD:A0A0K2CZZ1

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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

GO_REF:0000100

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
CACAO 11463

GO:0003824

catalytic activity

PMID:17519237[2]

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
CACAO 11583

GO:0004604

phosphoadenylyl-sulfate reductase (thioredoxin) activity

PMID:7588765[1]

ECO:0000250

UniProtKB:R8CUT3


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
CACAO 11610

enables

GO:0003824

catalytic activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR002500

F

Seeded From UniProt

complete

Notes

References

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

  1. 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
  2. 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