SPM_000295


  Uniprot: A0A037UPP1
Description: NADPH-dependent thioredoxin reductase
EC number: 1.18.1.2
Annotation score: 2 out of 5
Miscellaneous [CC]: 
Protein existence: Inferred from homology
Catalytic activity: CATALYTIC ACTIVITY: 2 reduced ferredoxin + NADP(+) + H(+) = 2 oxidized ferredoxin + NADPH. {ECO:0000256|HAMAP-Rule:MF_01685, ECO:0000256|SAAS:SAAS00541291}.
Cofactor: COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000256|HAMAP-Rule:MF_01685}; ; Note=Binds 1 FAD per subunit. {ECO:0000256|HAMAP-Rule:MF_01685}
Enzyme regulation: 
Function [CC]: 
Pathway: 
Active site: 
Binding site: BINDING 31 31 FAD. {ECO:0000256|HAMAP-Rule:MF_01685}.; BINDING 39 39 FAD. {ECO:0000256|HAMAP-Rule:MF_01685}.; BINDING 44 44 FAD. {ECO:0000256|HAMAP-Rule:MF_01685}.; BINDING 83 83 FAD; via amide nitrogen and carbonyl oxygen. {ECO:0000256|HAMAP-Rule:MF_01685}.; BINDING 120 120 FAD; via amide nitrogen. {ECO:0000256|HAMAP-Rule:MF_01685}.; BINDING 324 324 FAD. {ECO:0000256|HAMAP-Rule:MF_01685}.
Calcium binding: 
DNA binding: 
Metal binding: 
Nucleotide binding: 
Site: 
Gene names (primary): 
Gene names (synonym): 
Mass: 36,518
Subunit structure [CC]: SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01685, ECO:0000256|SAAS:SAAS00541287}.
Gene ontology (GO): ferredoxin-NADP+ reductase activity [GO:0004324]; flavin adenine dinucleotide binding [GO:0050660]; NADP binding [GO:0050661]
Gene ontology IDs: GO:0004324; GO:0050660; GO:0050661
Chain: 
Signal peptide: 
Domain [CC]: 
Sequence similarities: SIMILARITY: Belongs to the ferredoxin--NADP reductase type 2 family. {ECO:0000256|HAMAP-Rule:MF_01685, ECO:0000256|SAAS:SAAS00541289}.
Protein families: Ferredoxin--NADP reductase type 2 family
Coiled coil: 
Domain [FT]: DOMAIN 2 286 FAD/NAD-binding_dom. {ECO:0000259|Pfam:PF07992}.
Motif: 
Region: 
EMBL: AGBZ02000001
ProteinModelPortal: A0A037UPP1
MEROPS: 
EnsemblBacteria KO: KAI92556
UniPathway: 
CDD: 
Gene3D: 
HAMAP: 3.50.50.60
InterPro: MF_01685
PANTHER: IPR023753;IPR022890;IPR000103
PIRSF: 
PRINTS: 
PROSITE: PR00469
Pfam: 
ProDom: PF07992
SMART: 
SUPFAM: 
TIGRFAMs: SSF51905
57459-58446(+)

>nucleotide sequence
ATGAAAGATATTTTAATTATTGGGGCTGGTCCGGTTGGTTTATATGCCTGAAGTTGTGCT
GGTATGTTAGGGTTAAGCGGTTATATAATTGAAGGAAATGATACCCCTGGTGGACAACCA
TGAGAATTATATCCAGAAAAACCATTATATGATATGCCCGGGTTTGAAGAAATTAAAACT
AAAACATTTATTGAAAATTTAATTAAACAAGCTGAAAAAAATACAGGACAAATAACATAT
ATTGGGAAAACGAACATTAGTAATGTTCTTGAAACAACGGATGGATTTACTATTACTTTA
ACAACTAACGAAACACTTACGGTTAAAACAATTTTAATTACGAGTGGCAATGGTGTTTTT
ACTCCTATTCGTTTAGAACATCTTGATCCTCATCAAGAATATGAAAACTTATGATATGCT
GTTAAAAATCCAACCCTTTTAACACACAAGAAAATTGTTATTCTTGGTGGTGGTGATAGT
GCTGTTGATTGGGCAAATCATTTAATTGAAGATAACATTAGCAAAGATGTTACAATTATC
CATCGTCGTAGTTTGTACCGAGCTAAAGAAAGTAATGTCCAAAAATTACAGCAAAATAAA
GTCACGGAATTAAAACCTTATCATGTTAAAGCAGTTGATACGATTAATAATAAAATTACC
GCTTTAACATTAGTGCACGAAACAACGCATGCAACATTAACCATTCCAGCTGATCATTTT
ATTGTTCAATATGGTGCAAAAGTTGCACCAACAATCTTACAACAATTAACTTTAACAACA
ACCCCAATGCGAAAAATAATTATTGAACCAACTGGTCAAACAAATCATCCCCATATCTTT
GCCGCTGGAAATAGTGCTTATTATGCAGGAAAATATTATAATATGGTAACTGGGTTTGGA
GAAGCTATTAATGCGCTTTATAATATTACAAAAATTATTCATGGTCAAAAATACCACCCT
GGTTATTTAAGTGACATTAAAAAATAA


>protein sequence
MKDILIIGAGPVGLYAWSCAGMLGLSGYIIEGNDTPGGQPWELYPEKPLYDMPGFEEIKT
KTFIENLIKQAEKNTGQITYIGKTNISNVLETTDGFTITLTTNETLTVKTILITSGNGVF
TPIRLEHLDPHQEYENLWYAVKNPTLLTHKKIVILGGGDSAVDWANHLIEDNISKDVTII
HRRSLYRAKESNVQKLQQNKVTELKPYHVKAVDTINNKITALTLVHETTHATLTIPADHF
IVQYGAKVAPTILQQLTLTTTPMRKIIIEPTGQTNHPHIFAAGNSAYYAGKYYNMVTGFG
EAINALYNITKIIHGQKYHPGYLSDIKK






















© Fisunov Lab of Proteomics, 2016.