UMBC Phage Hunters Spring 2015
My Annotations
| Status | Page | Date/Time | GO Term (Aspect) | Reference | Evidence | Notes | Links |
|---|
| unacceptable | 9CAUD:S5Y026 | 2015-03-31 15:40:16 CDT | GO:0009055 electron carrier activity (F) | PMID:8694750 | ECO:0000247 sequence alignment evidence used in manual assertion | HHPred shows a match with flavodoxin in the Bacterium Desulfovibrio desulfuricans with probability 100.0, e-value 3.5E-29, p value 1E-33.
Flavodoxins are proteins that bind flavin mononucleotide(FMN) and are used in electron transfer pathways and redox potentials. PMID:8694750.
Blastp showed the presence of conserved regions in the Flavodoxin family of proteins. Given the conservation of the protein and the match with several other proteins, it can be inferred that the protein has a similar structure and function to flavodoxin found in other organisms.
| challenge |
| unacceptable | DESDE:FLAV | 2015-03-31 15:08:23 CDT | GO:0009055 electron carrier activity (F) | GO_REF:0000100 | ECO:0000247 sequence alignment evidence used in manual assertion | Blastp to azotobacter vinelandii has e value of 2e-11. Compositional matrix adjustment. 32% identity, 50% positives
PMID:8694750: The article describes the function of a flavodoxin protein in Azotobacter vinelandii as an electron carrier and donor in redox pathways. The article experimentally determined that the protein contains acid-labile iron and
sulphide and molybdenum pterin cofactor (Moco)redox centers.
GO:0009457 is obsolete because it represents a class of gene products. It was replaced by GO:0009055.
| challenge |
| unacceptable | DESDE:FLAV | 2015-04-01 10:39:45 CDT | GO:0043873 pyruvate-flavodoxin oxidoreductase activity (F) | GO_REF:0000100 | ECO:0000247 sequence alignment evidence used in manual assertion | Blastp to azotobacter vinelandii shows e value of 2e-11. Compositional matrix adjustment. 32% identity, 50% positives.
linked Pubmed article describes the redox potential determined by experimental evidence. The molecule is able to donate electrons to Nitrogen and can accept electrons from pyruvate.
| challenge |
| unacceptable | 9CAUD:S5Y026 | 2015-04-01 10:44:38 CDT | GO:0043873 pyruvate-flavodoxin oxidoreductase activity (F) | GO_REF:0000100 | ECO:0000247 sequence alignment evidence used in manual assertion | HHPred shows a match with flavodoxin in the Bacterium Desulfovibrio desulfuricans with probability 100.0, e-value 3.5E-29, p value 1E-33. The structure was determined in PMID:19465766, and linked to the family of flavodoxin proteins. The function of these was determined in PMID:8694750
Flavodoxins are proteins that accept electrons from pyruvate and donate electrons to nitrogen in oxidation reduction pathways. PMID:8694750.
Blastp showed the presence of conserved regions in the Flavodoxin family of proteins. Given the conservation of the protein and the match with several other proteins, it can be inferred that the protein has a similar structure and function to flavodoxin found in other organisms.
| challenge |
| unacceptable | AZOVI:M9YPU5 | 2015-04-08 07:32:27 CDT | GO:0043873 pyruvate-flavodoxin oxidoreductase activity (F) | PMID:8694750 | ECO:0000314 direct assay evidence used in manual assertion | Pubmed article describes the redox potential determined by experimental evidence. The molecule is able to donate electrons to Nitrogen and can accept electrons from pyruvate.
| challenge |
acceptable:0
unacceptable:5
requires_changes:0
flagged:0
Annotations challenged by Yhassaan
| Status | Author,Group | Page | GO Term (Aspect) | Reference | Evidence | Links | Page history |
|---|
0 annotations fixed by Yhassaan
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