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DESVH:FLAV
Contents
Species (Taxon ID) | Desulfovibrio vulgaris (strain Hildenborough / ATCC 29579 / NCIMB8303). (882) | |
Gene Name(s) | No Information Provided. | |
Protein Name(s) | Flavodoxin | |
External Links | ||
UniProt | P00323 | |
EMBL | J04033 AE017285 | |
PIR | A31991 | |
RefSeq | WP_010939949.1 YP_011892.1 | |
PDB | 1AKQ 1AKR 1AKT 1AKU 1AKV 1AKW 1AZL 1BU5 1C7E 1C7F 1F4P 1FX1 1I1O 1J8Q 1J9E 1J9G 1WSB 1WSW 1XT6 1XYV 1XYY 2FX2 3FX2 4FX2 5FX2 | |
PDBsum | 1AKQ 1AKR 1AKT 1AKU 1AKV 1AKW 1AZL 1BU5 1C7E 1C7F 1F4P 1FX1 1I1O 1J8Q 1J9E 1J9G 1WSB 1WSW 1XT6 1XYV 1XYY 2FX2 3FX2 4FX2 5FX2 | |
ProteinModelPortal | P00323 | |
SMR | P00323 | |
STRING | 882.DVU2680 | |
PaxDb | P00323 | |
EnsemblBacteria | AAS97152 | |
GeneID | 2795051 | |
KEGG | dvu:DVU2680 | |
PATRIC | 32064950 | |
eggNOG | ENOG41082EJ COG0716 | |
OMA | TACFGSG | |
OrthoDB | EOG6RG039 | |
PhylomeDB | P00323 | |
BioCyc | DVUL882:GJIL-2748-MONOMER | |
EvolutionaryTrace | P00323 | |
Proteomes | UP000002194 | |
GO | GO:0009055 GO:0010181 GO:0005506 GO:0055114 | |
Gene3D | 3.40.50.360 | |
InterPro | IPR010087 IPR001094 IPR008254 IPR001226 IPR029039 | |
Pfam | PF00258 | |
PRINTS | PR00369 | |
SUPFAM | SSF52218 | |
TIGRFAMs | TIGR01753 | |
PROSITE | PS00201 PS50902 |
Annotations
Qualifier | GO ID | GO term name | Reference | ECO ID | ECO term name | with/from | Aspect | Extension | Notes | Status |
---|---|---|---|---|---|---|---|---|---|---|
GO:0009055 |
electron carrier activity |
other:GO_REF:0000100 |
ECO:0000247 |
|
F |
The transfer annotation HHpred hits had an E-value of 4.8E-28, a similarity of 100%, and a query coverage of 99.32% which serves as the evidence. |
complete | |||
GO:0009055 |
electron carrier activity |
ECO:0000314 |
F |
Figure 4 of the article shows a stereo view of supercomposition held between the apoflavodoxin flavin-binding site in the FMN and the riboflavin complexes. The similar structures provide evidence of flavodoxin found in D. vulgaris. Additionally, figure 5 in the article provides a schematic representation of how hydrogen bonding takes place at both the flavin-binding site of apoflavodoxin and the riboflavin complex. The structures have a similar core but are only reversed at the Tyr-100 site, providing further evidence of the presnce of flavodoxin. Page 367 in the article further provides evidence by stating that "the interactions of the 90-loop in the structure of the apoflavodoxin-riboflavin complex are essentially identical to those in native flavodoxin, differing only in the orientation of the isoalloxazine and the interactions with Y98." |
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:0009055 |
electron transfer activity |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
enables |
GO:0010181 |
FMN binding |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
InterPro:IPR001094 |
F |
Seeded From UniProt |
complete | ||
involved_in |
GO:0055114 |
oxidation-reduction process |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
P |
Seeded From UniProt |
complete | |||
involved_in |
GO:0055114 |
oxidation-reduction process |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
P |
Seeded From UniProt |
complete | |||
Notes
References
See Help:References for how to manage references in GONUTS.
- ↑ Helms, LR et al. (1990) Identification, sequence determination, and expression of the flavodoxin gene from Desulfovibrio salexigens. Biochem. Biophys. Res. Commun. 168 809-17 PubMed GONUTS page
- ↑ Walsh, MA et al. (1998) X-ray crystal structure of the Desulfovibrio vulgaris (Hildenborough) apoflavodoxin-riboflavin complex. Eur. J. Biochem. 258 362-71 PubMed GONUTS page