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FAD-binding family protein FTT_1328c
microbial protein found in Francisella tularensis subsp. tularensis SCHU S4
FTT_1328C
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Statements
instance of
protein
1 reference
stated in
UniProt
retrieved
5 December 2018
UniProt protein ID
W0TYL4
subclass of
protein
1 reference
stated in
UniProt
language of work or name
English
UniProt protein ID
W0TYL4
retrieved
16 January 2017
part of
FAD-linked oxidase-like, C-terminal
1 reference
stated in
InterPro Release 71.0
reference URL
http://www.ebi.ac.uk/interpro/protein/W0TYL4
Alpha-helical ferredoxin
1 reference
stated in
InterPro Release 71.0
reference URL
http://www.ebi.ac.uk/interpro/protein/W0TYL4
FAD-binding, type PCMH-like superfamily
1 reference
stated in
InterPro Release 71.0
reference URL
http://www.ebi.ac.uk/interpro/protein/W0TYL4
FAD-oxidase
1 reference
based on heuristic
inferred from protein domain or family
FAD-linked oxidase, C-terminal domain, protein family
1 reference
based on heuristic
inferred from protein domain or family
FAD-binding domain, PCMH-type, protein family
1 reference
based on heuristic
inferred from protein domain or family
4Fe-4S ferredoxin-type, iron-sulphur binding domain, protein family
1 reference
based on heuristic
inferred from protein domain or family
4Fe-4S ferredoxin, iron-sulphur binding, conserved site, protein family
1 reference
based on heuristic
inferred from protein domain or family
found in taxon
Francisella tularensis subsp. tularensis SCHU S4
1 reference
stated in
UniProt
retrieved
5 December 2018
UniProt protein ID
W0TYL4
encoded by
FAD-binding family protein FTT_1328c
1 reference
stated in
UniProt
retrieved
5 December 2018
UniProt protein ID
W0TYL4
molecular function
catalytic activity
determination method
IEA
1 reference
retrieved
14 February 2019
stated in
GOA
curator
InterPro
reference URL
http://www.ebi.ac.uk/QuickGO/annotations?geneProductId=UniProtKB:W0TYL4
determination method
IEA
oxidoreductase activity
determination method
IEA
1 reference
retrieved
14 February 2019
stated in
GOA
curator
InterPro
reference URL
http://www.ebi.ac.uk/QuickGO/annotations?geneProductId=UniProtKB:W0TYL4
determination method
IEA
oxidoreductase activity, acting on CH-OH group of donors
determination method
IEA
1 reference
retrieved
27 March 2018
stated in
GOA
curator
InterPro
reference URL
http://www.ebi.ac.uk/QuickGO/annotations?protein=W0TYL4&geneProductId=UniProtKB:W0TYL4
determination method
IEA
flavin adenine dinucleotide binding
determination method
IEA
1 reference
retrieved
14 February 2019
stated in
GOA
curator
InterPro
reference URL
http://www.ebi.ac.uk/QuickGO/annotations?geneProductId=UniProtKB:W0TYL4
determination method
IEA
iron-sulfur cluster binding
determination method
IEA
1 reference
retrieved
14 February 2019
stated in
GOA
curator
InterPro
reference URL
http://www.ebi.ac.uk/QuickGO/annotations?geneProductId=UniProtKB:W0TYL4
determination method
IEA
FAD binding
determination method
IEA
1 reference
retrieved
14 February 2019
stated in
GOA
curator
InterPro
reference URL
http://www.ebi.ac.uk/QuickGO/annotations?geneProductId=UniProtKB:W0TYL4
determination method
IEA
has part(s)
4Fe-4S ferredoxin, iron-sulphur binding, conserved site
1 reference
stated in
InterPro Release 71.0
reference URL
http://www.ebi.ac.uk/interpro/protein/W0TYL4
FAD-binding domain, PCMH-type
1 reference
stated in
InterPro Release 71.0
reference URL
http://www.ebi.ac.uk/interpro/protein/W0TYL4
FAD-linked oxidase, C-terminal
1 reference
stated in
InterPro Release 71.0
reference URL
http://www.ebi.ac.uk/interpro/protein/W0TYL4
4Fe-4S ferredoxin-type, iron-sulphur binding domain
1 reference
stated in
InterPro Release 71.0
reference URL
http://www.ebi.ac.uk/interpro/protein/W0TYL4
FAD linked oxidase, N-terminal
1 reference
stated in
InterPro Release 71.0
reference URL
http://www.ebi.ac.uk/interpro/protein/W0TYL4
Identifiers
RefSeq protein ID
YP_003097805
1 reference
stated in
NCBI Gene
retrieved
7 December 2018
Entrez Gene ID
3191121
UniProt protein ID
W0TYL4
1 reference
stated in
UniProt
retrieved
5 December 2018
UniProt protein ID
W0TYL4
Sitelinks
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Multilingual sites
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