(data stored in ACNUC7421 zone)

SWISSPROT: C4KJF4_SULIK

ID   C4KJF4_SULIK            Unreviewed;       332 AA.
AC   C4KJF4;
DT   07-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   07-JUL-2009, sequence version 1.
DT   07-JUN-2017, entry version 51.
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=M164_0038 {ECO:0000313|EMBL:ACR40674.1};
OS   Sulfolobus islandicus (strain M.16.4 / Kamchatka #3).
OC   Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Sulfolobus.
OX   NCBI_TaxID=426118 {ECO:0000313|EMBL:ACR40674.1, ECO:0000313|Proteomes:UP000001479};
RN   [1] {ECO:0000313|EMBL:ACR40674.1, ECO:0000313|Proteomes:UP000001479}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M.16.4 / Kamchatka #3 {ECO:0000313|Proteomes:UP000001479};
RX   PubMed=19435847; DOI=10.1073/pnas.0808945106;
RA   Reno M.L., Held N.L., Fields C.J., Burke P.V., Whitaker R.J.;
RT   "Biogeography of the Sulfolobus islandicus pan-genome.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:8605-8610(2009).
CC   -!- CATALYTIC ACTIVITY: 2 reduced ferredoxin + NADP(+) + H(+) = 2
CC       oxidized ferredoxin + NADPH. {ECO:0000256|HAMAP-Rule:MF_01685}.
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   -!- SIMILARITY: Belongs to the ferredoxin--NADP reductase type 2
CC       family. {ECO:0000256|HAMAP-Rule:MF_01685}.
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; CP001402; ACR40674.1; -; Genomic_DNA.
DR   RefSeq; WP_012710217.1; NC_012726.1.
DR   ProteinModelPortal; C4KJF4; -.
DR   EnsemblBacteria; ACR40674; ACR40674; M164_0038.
DR   GeneID; 8759877; -.
DR   KEGG; sid:M164_0038; -.
DR   HOGENOM; HOG000072909; -.
DR   KO; K00384; -.
DR   OMA; CGFHEAT; -.
DR   OrthoDB; POG093Z053C; -.
DR   BioCyc; SISL426118:GI01-38-MONOMER; -.
DR   Proteomes; UP000001479; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004324; F:ferredoxin-NADP+ reductase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0050661; F:NADP binding; IEA:UniProtKB-HAMAP.
DR   Gene3D; 3.50.50.60; -; 2.
DR   HAMAP; MF_01685; FENR2; 1.
DR   InterPro; IPR023753; FAD/NAD-binding_dom.
DR   InterPro; IPR022890; Fd--NADP_Rdtase_type_2.
DR   InterPro; IPR000103; Pyridine_nuc-diS_OxRdtase_2.
DR   Pfam; PF07992; Pyr_redox_2; 1.
DR   PRINTS; PR00469; PNDRDTASEII.
DR   SUPFAM; SSF51905; SSF51905; 1.
PE   3: Inferred from homology;
DR   PRODOM; C4KJF4.
DR   SWISS-2DPAGE; C4KJF4.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001479};
KW   FAD {ECO:0000256|HAMAP-Rule:MF_01685};
KW   Flavoprotein {ECO:0000256|HAMAP-Rule:MF_01685};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   NADP {ECO:0000256|HAMAP-Rule:MF_01685};
KW   Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_01685};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM      6     24       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN        4    296       FAD/NAD-binding_dom. {ECO:0000259|Pfam:
FT                                PF07992}.
FT   BINDING      33     33       FAD. {ECO:0000256|HAMAP-Rule:MF_01685}.
FT   BINDING      41     41       FAD. {ECO:0000256|HAMAP-Rule:MF_01685}.
FT   BINDING      46     46       FAD. {ECO:0000256|HAMAP-Rule:MF_01685}.
FT   BINDING      86     86       FAD; via amide nitrogen and carbonyl
FT                                oxygen. {ECO:0000256|HAMAP-Rule:
FT                                MF_01685}.
FT   BINDING     120    120       FAD; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01685}.
FT   BINDING     281    281       FAD. {ECO:0000256|HAMAP-Rule:MF_01685}.
FT   BINDING     324    324       FAD. {ECO:0000256|HAMAP-Rule:MF_01685}.
SQ   SEQUENCE   332 AA;  36527 MW;  556E84B6CC919487 CRC64;
     MNEYDMVIIG GGPVGLFGTF YAGLRDMKAL LIDAQDELGG QLVSLYPEKI VYDVGGLAGI
     QAYELAQRLI EQAKMFGPDI RVNEWADMIE KTSDNMWIVK TDKGSYKTKT IFIAAGIGKI
     VPSRLGAKGE IEYENKGVYY TVRRKKDFEG KRILVVGGGD SAVDWALNLA PVAKSVTLIH
     RRDQFRAHER SVKELFRVAN VYVWHELKEI KGDGNKVTQA IIFDNRTKEE KVLNVDSVII
     SIGYKGDLGN IPKWGVNMKG RDIVVNGKME TNLPGVYAGG DIVQLEGSPK LALIAVGFAH
     AAIAISVAKK YVEPSASLFA GHSSEMDKFK PK
//

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