DESAD:FLAV

Species (Taxon ID)	Desulfovibrio salexigens (strain ATCC 14822 / DSM 2638 / NCIB 8403 /VKM B-1763). (526222)
Gene Name(s)	No Information Provided.
Protein Name(s)	Flavodoxin
External Links
UniProt	P18086
EMBL	M35475 CP001649
PIR	A34640
RefSeq	WP_015850690.1
ProteinModelPortal	P18086
SMR	P18086
STRING	526222.Desal_0805
EnsemblBacteria	ACS78871
KEGG	dsa:Desal_0805
PATRIC	21757061
eggNOG	ENOG41082EJ COG0716
HOGENOM	HOG000030540
OMA	TACFGSG
OrthoDB	EOG6RG039
BioCyc	DSAL526222:GHES-815-MONOMER
Proteomes	UP000002601
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	PMID:2334437	ECO:0000247		UniProtKB:P00323	F		Matched 100% with Flavodoxin; electron transport (4HEQ - the crystal structure of flavodoxin from Desulfovibrio gigas) with an E-value of 7.6E-30. Figure 4 of the PubMed article compares the flavodoxin protein sequences found in D. vulgaris and D. salexigens. Most protein sequences compared between the two were found to be identical (marked with a ";") or conservative (marked with a ":"), showing much similarity between what was found between the two. This provides evidence that flavodoxin appears in D. salexigens as it does in D. vulgaris. Additionally, Page 814 of the article adds more evidence to the fact that when the X-ray structure of the DVF was compared, all homologous regions were confined to areas in which were in the immediate vicinity of the flavin mononucleotide cofactor binding site. It was stated that all known flavodoxin structures provided highly conserved sequences near an amino terminus which surrounds the hydrogen bonds of the cofactor. This additionally shows evidence of the presence of flavodoxin in D. salexigens as it appears in D. vulgaris.	complete CACAO 11885
involved_in	GO:0022900	electron transport chain	GO_REF:0000108	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	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR001226	F		Seeded From UniProt	complete
enables	GO:0010181	FMN binding	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR001094 InterPro:IPR001226 InterPro:IPR008254 InterPro:IPR010087	F		Seeded From UniProt	complete
involved_in	GO:0055114	oxidation-reduction process	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR001094	P		Seeded From UniProt	complete
involved_in	GO:0055114	oxidation-reduction process	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0249	P		Seeded From UniProt	complete
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References

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