(data stored in SCRATCH zone)

SWISSPROT: A0A0F6BHY7_GEOS0

ID   A0A0F6BHY7_GEOS0        Unreviewed;       349 AA.
AC   A0A0F6BHY7;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   08-MAY-2019, entry version 26.
DE   RecName: Full=Ferredoxin--NADP reductase {ECO:0000256|HAMAP-Rule:MF_01685};
DE            Short=FNR {ECO:0000256|HAMAP-Rule:MF_01685};
DE            Short=Fd-NADP(+) reductase {ECO:0000256|HAMAP-Rule:MF_01685};
DE            EC=1.18.1.2 {ECO:0000256|HAMAP-Rule:MF_01685};
GN   OrderedLocusNames=GY4MC1_0186 {ECO:0000313|EMBL:ADP73038.1};
OS   Geobacillus sp. (strain Y4.1MC1).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus.
OX   NCBI_TaxID=581103 {ECO:0000313|EMBL:ADP73038.1, ECO:0000313|Proteomes:UP000002034};
RN   [1] {ECO:0000313|EMBL:ADP73038.1, ECO:0000313|Proteomes:UP000002034}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Y4.1MC1 {ECO:0000313|EMBL:ADP73038.1,
RC   ECO:0000313|Proteomes:UP000002034};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., Chertkov O., Zhang X., Detter J.C., Han C., Tapia R.,
RA   Land M., Hauser L., Jeffries C., Kyrpides N., Ivanova N.,
RA   Ovchinnikova G., Brumm P., Mead D., Woyke T.;
RT   "Complete sequence of chromosome of Geobacillus sp. Y4.1MC1.";
RL   Submitted (OCT-2010) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+) + NADP(+) + 2 reduced [2Fe-2S]-[ferredoxin] = NADPH
CC         + 2 oxidized [2Fe-2S]-[ferredoxin]; Xref=Rhea:RHEA:20125,
CC         Rhea:RHEA-COMP:10000, Rhea:RHEA-COMP:10001, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:33737, ChEBI:CHEBI:33738, ChEBI:CHEBI:57783,
CC         ChEBI:CHEBI:58349; EC=1.18.1.2; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01685, ECO:0000256|SAAS:SAAS01118367};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01685};
CC       Note=Binds 1 FAD per subunit. {ECO:0000256|HAMAP-Rule:MF_01685};
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01685,
CC       ECO:0000256|SAAS:SAAS00541287}.
CC   -!- SIMILARITY: Belongs to the ferredoxin--NADP reductase type 2
CC       family. {ECO:0000256|HAMAP-Rule:MF_01685,
CC       ECO:0000256|SAAS:SAAS00541289}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|HAMAP-Rule:MF_01685}.
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DR   EMBL; CP002293; ADP73038.1; -; Genomic_DNA.
DR   RefSeq; WP_013399856.1; NC_014650.1.
DR   EnsemblBacteria; ADP73038; ADP73038; GY4MC1_0186.
DR   KEGG; gmc:GY4MC1_0186; -.
DR   KO; K21567; -.
DR   OMA; AFQCGMN; -.
DR   OrthoDB; 692968at2; -.
DR   BioCyc; GSP581103:G1GOQ-226-MONOMER; -.
DR   Proteomes; UP000002034; Chromosome.
DR   GO; GO:0004324; F:ferredoxin-NADP+ reductase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0050661; F:NADP binding; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.50.50.60; -; 2.
DR   HAMAP; MF_01685; FENR2; 1.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR023753; FAD/NAD-binding_dom.
DR   InterPro; IPR022890; Fd--NADP_Rdtase_type_2.
DR   Pfam; PF07992; Pyr_redox_2; 1.
DR   SUPFAM; SSF51905; SSF51905; 1.
PE   3: Inferred from homology;
DR   PRODOM; A0A0F6BHY7.
DR   SWISS-2DPAGE; A0A0F6BHY7.
KW   Complete proteome {ECO:0000313|Proteomes:UP000002034};
KW   FAD {ECO:0000256|HAMAP-Rule:MF_01685, ECO:0000256|SAAS:SAAS00541298};
KW   Flavoprotein {ECO:0000256|HAMAP-Rule:MF_01685,
KW   ECO:0000256|SAAS:SAAS00541285};
KW   NADP {ECO:0000256|HAMAP-Rule:MF_01685, ECO:0000256|SAAS:SAAS00541286};
KW   Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_01685,
KW   ECO:0000256|SAAS:SAAS00541294}.
FT   DOMAIN        7    307       Pyr_redox_2. {ECO:0000259|Pfam:PF07992}.
FT   BINDING      36     36       FAD. {ECO:0000256|HAMAP-Rule:MF_01685}.
FT   BINDING      44     44       FAD. {ECO:0000256|HAMAP-Rule:MF_01685}.
FT   BINDING      48     48       FAD. {ECO:0000256|HAMAP-Rule:MF_01685}.
FT   BINDING      88     88       FAD; via amide nitrogen and carbonyl
FT                                oxygen. {ECO:0000256|HAMAP-Rule:
FT                                MF_01685}.
FT   BINDING     123    123       FAD; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01685}.
FT   BINDING     290    290       FAD. {ECO:0000256|HAMAP-Rule:MF_01685}.
FT   BINDING     331    331       FAD. {ECO:0000256|HAMAP-Rule:MF_01685}.
SQ   SEQUENCE   349 AA;  38663 MW;  01046F1D70D592CD CRC64;
     MEREELYDVT IIGGGPAGLY AAFYSGLRKM KTKLIECQPQ LGGKLHVYPE KIIWDVGGHA
     PITGEQLMKQ LVKQGLTFHP TVILNEKVVS MKRQNDGIFV LSTASGQQHF SKTVIVAVGS
     GILKPKKLEI EGAEKFEVTN LHYTVKSLKR FKDKTVIISG GGNSAIDWAN ELVPIAKKVY
     LTYRNEELKG HESQVTQLLN SSAVCYFNTS ITKLIASANH EIIDRVELTN HETGEVIYLP
     VDEVIVNHGY ERDTSLLENS ELDIKMVDND YIAGNANCES SVPGLYAAGD ILKYDGKLNL
     IIGAFQDAAN AVNSAKRFIE PAADPFGMVS SHNEIFKKQN QEFIKQMMK
//

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