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 GGTATGTTAGGGTTAAGCGGTTATATAATTGAAGGAAATGATACCCCTGGTGGACAACCA TGAGAATTATATCCAGAAAAACCATTATATGATATGCCCGGGTTTGAAGAAATTAAAACT AAAACATTTATTGAAAATTTAATTAAACAAGCTGAAAAAAATACAGGACAAATAACATAT ATTGGGAAAACGAACATTAGTAATGTTCTTGAAACAACGGATGGATTTACTATTACTTTA ACAACTAACGAAACACTTACGGTTAAAACAATTTTAATTACGAGTGGCAATGGTGTTTTT ACTCCTATTCGTTTAGAACATCTTGATCCTCATCAAGAATATGAAAACTTATGATATGCT GTTAAAAATCCAACCCTTTTAACACACAAGAAAATTGTTATTCTTGGTGGTGGTGATAGT GCTGTTGATTGGGCAAATCATTTAATTGAAGATAACATTAGCAAAGATGTTACAATTATC CATCGTCGTAGTTTGTACCGAGCTAAAGAAAGTAATGTCCAAAAATTACAGCAAAATAAA GTCACGGAATTAAAACCTTATCATGTTAAAGCAGTTGATACGATTAATAATAAAATTACC GCTTTAACATTAGTGCACGAAACAACGCATGCAACATTAACCATTCCAGCTGATCATTTT ATTGTTCAATATGGTGCAAAAGTTGCACCAACAATCTTACAACAATTAACTTTAACAACA ACCCCAATGCGAAAAATAATTATTGAACCAACTGGTCAAACAAATCATCCCCATATCTTT GCCGCTGGAAATAGTGCTTATTATGCAGGAAAATATTATAATATGGTAACTGGGTTTGGA GAAGCTATTAATGCGCTTTATAATATTACAAAAATTATTCATGGTCAAAAATACCACCCT GGTTATTTAAGTGACATTAAAAAATAA >protein sequence KTFIENLIKQAEKNTGQITYIGKTNISNVLETTDGFTITLTTNETLTVKTILITSGNGVF TPIRLEHLDPHQEYENLWYAVKNPTLLTHKKIVILGGGDSAVDWANHLIEDNISKDVTII HRRSLYRAKESNVQKLQQNKVTELKPYHVKAVDTINNKITALTLVHETTHATLTIPADHF IVQYGAKVAPTILQQLTLTTTPMRKIIIEPTGQTNHPHIFAAGNSAYYAGKYYNMVTGFG EAINALYNITKIIHGQKYHPGYLSDIKK |
© Fisunov Lab of Proteomics, 2016.