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FENR_BACCR
ID   FENR_BACCR              Reviewed;         331 AA.
AC   Q816D9;
DT   03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 111.
DE   RecName: Full=Ferredoxin--NADP reductase {ECO:0000255|HAMAP-Rule:MF_01685};
DE            Short=FNR {ECO:0000255|HAMAP-Rule:MF_01685};
DE            Short=Fd-NADP(+) reductase {ECO:0000255|HAMAP-Rule:MF_01685};
DE            EC=1.18.1.2 {ECO:0000255|HAMAP-Rule:MF_01685};
GN   OrderedLocusNames=BC_4926;
OS   Bacillus cereus (strain ATCC 14579 / DSM 31 / CCUG 7414 / JCM 2152 / NBRC
OS   15305 / NCIMB 9373 / NCTC 2599 / NRRL B-3711).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=226900;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 14579 / DSM 31 / CCUG 7414 / JCM 2152 / NBRC 15305 / NCIMB 9373
RC   / NCTC 2599 / NRRL B-3711;
RX   PubMed=12721630; DOI=10.1038/nature01582;
RA   Ivanova N., Sorokin A., Anderson I., Galleron N., Candelon B., Kapatral V.,
RA   Bhattacharyya A., Reznik G., Mikhailova N., Lapidus A., Chu L., Mazur M.,
RA   Goltsman E., Larsen N., D'Souza M., Walunas T., Grechkin Y., Pusch G.,
RA   Haselkorn R., Fonstein M., Ehrlich S.D., Overbeek R., Kyrpides N.C.;
RT   "Genome sequence of Bacillus cereus and comparative analysis with Bacillus
RT   anthracis.";
RL   Nature 423:87-91(2003).
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; AE016877; AAP11799.1; -; Genomic_DNA.
DR   RefSeq; NP_834598.1; NC_004722.1.
DR   PDB; 6GAS; X-ray; 2.40 A; A/B/C/D=1-331.
DR   PDBsum; 6GAS; -.
DR   AlphaFoldDB; Q816D9; -.
DR   SMR; Q816D9; -.
DR   STRING; 226900.BC_4926; -.
DR   EnsemblBacteria; AAP11799; AAP11799; BC_4926.
DR   KEGG; bce:BC4926; -.
DR   PATRIC; fig|226900.8.peg.5078; -.
DR   HOGENOM; CLU_031864_5_5_9; -.
DR   OMA; PEKVIYD; -.
DR   Proteomes; UP000001417; 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   GO; GO:0004791; F:thioredoxin-disulfide reductase activity; IBA:GO_Central.
DR   GO; GO:0045454; P:cell redox homeostasis; IBA:GO_Central.
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   1: Evidence at protein level;
KW   3D-structure; FAD; Flavoprotein; NADP; Oxidoreductase; Reference proteome.
FT   CHAIN           1..331
FT                   /note="Ferredoxin--NADP reductase"
FT                   /id="PRO_0000364790"
FT   BINDING         20
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01685"
FT   BINDING         39
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01685"
FT   BINDING         47
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01685"
FT   BINDING         52
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01685"
FT   BINDING         92
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01685"
FT   BINDING         126
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01685"
FT   BINDING         287
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01685"
FT   BINDING         328
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01685"
FT   STRAND          9..15
FT                   /evidence="ECO:0007829|PDB:6GAS"
FT   HELIX           19..30
FT                   /evidence="ECO:0007829|PDB:6GAS"
FT   STRAND          35..38
FT                   /evidence="ECO:0007829|PDB:6GAS"
FT   STRAND          40..44
FT                   /evidence="ECO:0007829|PDB:6GAS"
FT   HELIX           46..51
FT                   /evidence="ECO:0007829|PDB:6GAS"
FT   STRAND          55..57
FT                   /evidence="ECO:0007829|PDB:6GAS"
FT   STRAND          64..67
FT                   /evidence="ECO:0007829|PDB:6GAS"
FT   HELIX           68..79
FT                   /evidence="ECO:0007829|PDB:6GAS"
FT   HELIX           80..82
FT                   /evidence="ECO:0007829|PDB:6GAS"
FT   STRAND          85..87
FT                   /evidence="ECO:0007829|PDB:6GAS"
FT   STRAND          94..97
FT                   /evidence="ECO:0007829|PDB:6GAS"
FT   STRAND          103..106
FT                   /evidence="ECO:0007829|PDB:6GAS"
FT   STRAND          111..119
FT                   /evidence="ECO:0007829|PDB:6GAS"
FT   STRAND          124..128
FT                   /evidence="ECO:0007829|PDB:6GAS"
FT   HELIX           136..139
FT                   /evidence="ECO:0007829|PDB:6GAS"
FT   TURN            140..143
FT                   /evidence="ECO:0007829|PDB:6GAS"
FT   STRAND          144..146
FT                   /evidence="ECO:0007829|PDB:6GAS"
FT   HELIX           151..154
FT                   /evidence="ECO:0007829|PDB:6GAS"
FT   STRAND          158..162
FT                   /evidence="ECO:0007829|PDB:6GAS"
FT   HELIX           166..175
FT                   /evidence="ECO:0007829|PDB:6GAS"
FT   TURN            176..178
FT                   /evidence="ECO:0007829|PDB:6GAS"
FT   STRAND          179..185
FT                   /evidence="ECO:0007829|PDB:6GAS"
FT   STRAND          187..190
FT                   /evidence="ECO:0007829|PDB:6GAS"
FT   HELIX           195..202
FT                   /evidence="ECO:0007829|PDB:6GAS"
FT   TURN            203..205
FT                   /evidence="ECO:0007829|PDB:6GAS"
FT   STRAND          207..209
FT                   /evidence="ECO:0007829|PDB:6GAS"
FT   STRAND          212..218
FT                   /evidence="ECO:0007829|PDB:6GAS"
FT   STRAND          220..222
FT                   /evidence="ECO:0007829|PDB:6GAS"
FT   STRAND          225..230
FT                   /evidence="ECO:0007829|PDB:6GAS"
FT   TURN            231..233
FT                   /evidence="ECO:0007829|PDB:6GAS"
FT   STRAND          236..240
FT                   /evidence="ECO:0007829|PDB:6GAS"
FT   STRAND          242..246
FT                   /evidence="ECO:0007829|PDB:6GAS"
FT   STRAND          250..253
FT                   /evidence="ECO:0007829|PDB:6GAS"
FT   HELIX           255..259
FT                   /evidence="ECO:0007829|PDB:6GAS"
FT   STRAND          268..270
FT                   /evidence="ECO:0007829|PDB:6GAS"
FT   STRAND          282..284
FT                   /evidence="ECO:0007829|PDB:6GAS"
FT   HELIX           298..316
FT                   /evidence="ECO:0007829|PDB:6GAS"
FT   HELIX           327..329
FT                   /evidence="ECO:0007829|PDB:6GAS"
SQ   SEQUENCE   331 AA;  36748 MW;  3D910538F9E38649 CRC64;
     MKVAENQKVY DITIIGGGPT GLFTAFYGGM RQASVKIIES LPQLGGQLSA LYPEKYIYDV
     AGFPKVRAQE LVDNLKEQMK KFDPTVCLEE AVDTLEKQAD GIFKLVTNKQ THYSKSVIIT
     AGNGAFQPRR LELEGTAKYE KKNLHYFVDD MNKFAGKRVV VFGGGDSAVD WTMMLEPIAE
     KVTIVHRRDK FRAHEHSVEN LMNSRAEVST PYVPVELIGD DKIEQVVLQH VKTEEKVIID
     VDDVIVNYGF VSSLGPIKNW GLDIQKNSIL VNSKMETNIP GIYAAGDICT YEGKVKLIAC
     GFGEAPTAVN NAKAYFDPNA KLQPMHSSSM F
 
 
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