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FENR2_CUPNH
ID   FENR2_CUPNH             Reviewed;         369 AA.
AC   Q0K8J6;
DT   03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   03-OCT-2006, sequence version 1.
DT   03-AUG-2022, entry version 95.
DE   RecName: Full=Ferredoxin--NADP reductase 2 {ECO:0000255|HAMAP-Rule:MF_01685};
DE            Short=FNR 2 {ECO:0000255|HAMAP-Rule:MF_01685};
DE            Short=Fd-NADP(+) reductase 2 {ECO:0000255|HAMAP-Rule:MF_01685};
DE            EC=1.18.1.2 {ECO:0000255|HAMAP-Rule:MF_01685};
GN   OrderedLocusNames=H16_A2592;
OS   Cupriavidus necator (strain ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442
OS   / H16 / Stanier 337) (Ralstonia eutropha).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Cupriavidus.
OX   NCBI_TaxID=381666;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442 / H16 / Stanier 337;
RX   PubMed=16964242; DOI=10.1038/nbt1244;
RA   Pohlmann A., Fricke W.F., Reinecke F., Kusian B., Liesegang H., Cramm R.,
RA   Eitinger T., Ewering C., Poetter M., Schwartz E., Strittmatter A., Voss I.,
RA   Gottschalk G., Steinbuechel A., Friedrich B., Bowien B.;
RT   "Genome sequence of the bioplastic-producing 'Knallgas' bacterium Ralstonia
RT   eutropha H16.";
RL   Nat. Biotechnol. 24:1257-1262(2006).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+) + NADP(+) + 2 reduced [2Fe-2S]-[ferredoxin] = NADPH + 2
CC         oxidized [2Fe-2S]-[ferredoxin]; Xref=Rhea:RHEA:20125, Rhea:RHEA-
CC         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:0000255|HAMAP-
CC         Rule:MF_01685};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01685};
CC       Note=Binds 1 FAD per subunit. {ECO:0000255|HAMAP-Rule:MF_01685};
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01685}.
CC   -!- SIMILARITY: Belongs to the ferredoxin--NADP reductase type 2 family.
CC       {ECO:0000255|HAMAP-Rule:MF_01685}.
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DR   EMBL; AM260479; CAJ93675.1; -; Genomic_DNA.
DR   RefSeq; WP_010814655.1; NC_008313.1.
DR   AlphaFoldDB; Q0K8J6; -.
DR   SMR; Q0K8J6; -.
DR   STRING; 381666.H16_A2592; -.
DR   EnsemblBacteria; CAJ93675; CAJ93675; H16_A2592.
DR   GeneID; 57644716; -.
DR   KEGG; reh:H16_A2592; -.
DR   eggNOG; COG0492; Bacteria.
DR   HOGENOM; CLU_031864_5_5_4; -.
DR   OMA; PEKVIYD; -.
DR   OrthoDB; 692968at2; -.
DR   Proteomes; UP000008210; Chromosome 1.
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; IPR022890; Fd--NADP_Rdtase_type_2.
DR   SUPFAM; SSF51905; SSF51905; 2.
PE   3: Inferred from homology;
KW   FAD; Flavoprotein; NADP; Oxidoreductase; Reference proteome.
FT   CHAIN           1..369
FT                   /note="Ferredoxin--NADP reductase 2"
FT                   /id="PRO_0000364904"
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         58
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01685"
FT   BINDING         66
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01685"
FT   BINDING         71
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01685"
FT   BINDING         111
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01685"
FT   BINDING         146
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01685"
FT   BINDING         311
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01685"
FT   BINDING         352
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01685"
SQ   SEQUENCE   369 AA;  40324 MW;  F6398C2ECCC01733 CRC64;
     MDLSIPNPVA DTTKQVDGGS PAGGQPQEID ALIVGAGPVG LFQVFELGLL EIKAHVIDSL
     KVVGGQCVEL YPDKPIYDIP AVPICTGQEL TDNLLKQIEP FEPTFHLGQE VAVVERREDG
     RFFVETSLGT RFITKTIFIA AGVGSFQPRT LKVEGIDKFD GKQLFYRVKD PSRFHGRNLV
     IIGGGDSALD WTLDLVGKAE SVVMIHRRDG FRAAPASVAK MKELCEQMEM QFLVGQVGGY
     EEKDGVLTEI KVTGADGVTR RLPVDDLLVF FGLSPKLGPI AEWGLDLERK QIKVDTEKFE
     TNIPGIFAVG DINTYPGKKK LILSGFHEAA LAAFGAAPYI FPEKKIHMQY TTTSPKLHKI
     LGVDSPVFD
 
 
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