(data stored in ACNUC7421 zone)

SWISSPROT: A0A0F6BIX1_GEOS0

ID   A0A0F6BIX1_GEOS0        Unreviewed;       330 AA.
AC   A0A0F6BIX1;
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_0540 {ECO:0000313|EMBL:ADP73372.1};
OS   Geobacillus sp. (strain Y4.1MC1).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus.
OX   NCBI_TaxID=581103 {ECO:0000313|EMBL:ADP73372.1, ECO:0000313|Proteomes:UP000002034};
RN   [1] {ECO:0000313|EMBL:ADP73372.1, ECO:0000313|Proteomes:UP000002034}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Y4.1MC1 {ECO:0000313|EMBL:ADP73372.1,
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; ADP73372.1; -; Genomic_DNA.
DR   RefSeq; WP_003248321.1; NC_014650.1.
DR   EnsemblBacteria; ADP73372; ADP73372; GY4MC1_0540.
DR   GeneID; 29236806; -.
DR   KEGG; gmc:GY4MC1_0540; -.
DR   KO; K21567; -.
DR   OMA; CGFHEAT; -.
DR   OrthoDB; 692968at2; -.
DR   BioCyc; GSP581103:G1GOQ-590-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; A0A0F6BIX1.
DR   SWISS-2DPAGE; A0A0F6BIX1.
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        8    297       Pyr_redox_2. {ECO:0000259|Pfam:PF07992}.
FT   BINDING      18     18       FAD. {ECO:0000256|HAMAP-Rule:MF_01685}.
FT   BINDING      37     37       FAD. {ECO:0000256|HAMAP-Rule:MF_01685}.
FT   BINDING      45     45       FAD. {ECO:0000256|HAMAP-Rule:MF_01685}.
FT   BINDING      50     50       FAD. {ECO:0000256|HAMAP-Rule:MF_01685}.
FT   BINDING      90     90       FAD; via amide nitrogen and carbonyl
FT                                oxygen. {ECO:0000256|HAMAP-Rule:
FT                                MF_01685}.
FT   BINDING     124    124       FAD; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01685}.
FT   BINDING     286    286       FAD. {ECO:0000256|HAMAP-Rule:MF_01685}.
FT   BINDING     327    327       FAD. {ECO:0000256|HAMAP-Rule:MF_01685}.
SQ   SEQUENCE   330 AA;  36504 MW;  B4280667CC39116D CRC64;
     MKEDPKIYDV TIIGGGPTGL FAAFYGGLRQ MSVKIIESLP QLGGQLSALY PEKYIYDIAG
     FPKIRAQELI NNLKEQMEQF APTVCLEQSV EKLEKLENGT LKLTTNKEIH YSKTVVITAG
     NGAFQPRRLE LETAAQYEGK NLYYFINDLN QFKGQKVLVC GGGDSAVDWS LMLEPIAEKV
     TIVHRRDKFR AHEHSVETLL NSTVNVKTPF VPVELIGDEN GIRQVVIEHV KDGSRETIDI
     DALIVNYGFI SSLGPIKNWG LEIEKNSIKV NSKMETNIPG VYAAGDICTY EGKIKLIACG
     FGEAPIAISS AKTYIDPTAR MQPAHSTSLF
//

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