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FENR_STAA3
ID   FENR_STAA3              Reviewed;         344 AA.
AC   Q2FEC4;
DT   03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2006, sequence version 1.
DT   03-AUG-2022, entry version 97.
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=SAUSA300_2319;
OS   Staphylococcus aureus (strain USA300).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=367830;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=USA300;
RX   PubMed=16517273; DOI=10.1016/s0140-6736(06)68231-7;
RA   Diep B.A., Gill S.R., Chang R.F., Phan T.H., Chen J.H., Davidson M.G.,
RA   Lin F., Lin J., Carleton H.A., Mongodin E.F., Sensabaugh G.F.,
RA   Perdreau-Remington F.;
RT   "Complete genome sequence of USA300, an epidemic clone of community-
RT   acquired meticillin-resistant Staphylococcus aureus.";
RL   Lancet 367:731-739(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; CP000255; ABD21289.1; -; Genomic_DNA.
DR   RefSeq; WP_000655971.1; NZ_CP027476.1.
DR   PDB; 5TWB; X-ray; 1.82 A; A=1-344.
DR   PDB; 5TWC; X-ray; 2.31 A; A=1-344.
DR   PDBsum; 5TWB; -.
DR   PDBsum; 5TWC; -.
DR   AlphaFoldDB; Q2FEC4; -.
DR   SMR; Q2FEC4; -.
DR   EnsemblBacteria; ABD21289; ABD21289; SAUSA300_2319.
DR   KEGG; saa:SAUSA300_2319; -.
DR   HOGENOM; CLU_031864_5_5_9; -.
DR   OMA; LEQCAPF; -.
DR   Proteomes; UP000001939; 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   1: Evidence at protein level;
KW   3D-structure; FAD; Flavoprotein; NADP; Oxidoreductase.
FT   CHAIN           1..344
FT                   /note="Ferredoxin--NADP reductase"
FT                   /id="PRO_0000364947"
FT   BINDING         12
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01685"
FT   BINDING         31
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         43
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01685"
FT   BINDING         83
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01685"
FT   BINDING         118
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01685"
FT   BINDING         285
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01685"
FT   BINDING         326
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01685"
FT   STRAND          2..7
FT                   /evidence="ECO:0007829|PDB:5TWB"
FT   HELIX           11..22
FT                   /evidence="ECO:0007829|PDB:5TWB"
FT   STRAND          27..30
FT                   /evidence="ECO:0007829|PDB:5TWB"
FT   STRAND          32..36
FT                   /evidence="ECO:0007829|PDB:5TWB"
FT   HELIX           38..42
FT                   /evidence="ECO:0007829|PDB:5TWB"
FT   STRAND          46..48
FT                   /evidence="ECO:0007829|PDB:5TWB"
FT   STRAND          56..58
FT                   /evidence="ECO:0007829|PDB:5TWB"
FT   HELIX           59..70
FT                   /evidence="ECO:0007829|PDB:5TWB"
FT   TURN            71..73
FT                   /evidence="ECO:0007829|PDB:5TWB"
FT   STRAND          76..78
FT                   /evidence="ECO:0007829|PDB:5TWB"
FT   STRAND          83..90
FT                   /evidence="ECO:0007829|PDB:5TWB"
FT   STRAND          93..98
FT                   /evidence="ECO:0007829|PDB:5TWB"
FT   STRAND          103..111
FT                   /evidence="ECO:0007829|PDB:5TWB"
FT   STRAND          117..120
FT                   /evidence="ECO:0007829|PDB:5TWB"
FT   STRAND          125..128
FT                   /evidence="ECO:0007829|PDB:5TWC"
FT   HELIX           131..133
FT                   /evidence="ECO:0007829|PDB:5TWB"
FT   STRAND          136..138
FT                   /evidence="ECO:0007829|PDB:5TWB"
FT   HELIX           144..146
FT                   /evidence="ECO:0007829|PDB:5TWB"
FT   STRAND          150..154
FT                   /evidence="ECO:0007829|PDB:5TWB"
FT   HELIX           158..168
FT                   /evidence="ECO:0007829|PDB:5TWB"
FT   STRAND          171..178
FT                   /evidence="ECO:0007829|PDB:5TWB"
FT   HELIX           180..182
FT                   /evidence="ECO:0007829|PDB:5TWB"
FT   HELIX           186..194
FT                   /evidence="ECO:0007829|PDB:5TWB"
FT   STRAND          198..202
FT                   /evidence="ECO:0007829|PDB:5TWB"
FT   STRAND          204..211
FT                   /evidence="ECO:0007829|PDB:5TWB"
FT   STRAND          215..225
FT                   /evidence="ECO:0007829|PDB:5TWB"
FT   TURN            226..228
FT                   /evidence="ECO:0007829|PDB:5TWB"
FT   STRAND          231..235
FT                   /evidence="ECO:0007829|PDB:5TWB"
FT   STRAND          237..241
FT                   /evidence="ECO:0007829|PDB:5TWB"
FT   STRAND          245..248
FT                   /evidence="ECO:0007829|PDB:5TWB"
FT   HELIX           251..254
FT                   /evidence="ECO:0007829|PDB:5TWB"
FT   STRAND          255..257
FT                   /evidence="ECO:0007829|PDB:5TWC"
FT   STRAND          261..265
FT                   /evidence="ECO:0007829|PDB:5TWB"
FT   STRAND          270..274
FT                   /evidence="ECO:0007829|PDB:5TWB"
FT   STRAND          280..282
FT                   /evidence="ECO:0007829|PDB:5TWB"
FT   HELIX           296..314
FT                   /evidence="ECO:0007829|PDB:5TWB"
FT   HELIX           325..327
FT                   /evidence="ECO:0007829|PDB:5TWB"
FT   HELIX           329..331
FT                   /evidence="ECO:0007829|PDB:5TWB"
FT   HELIX           332..342
FT                   /evidence="ECO:0007829|PDB:5TWB"
SQ   SEQUENCE   344 AA;  38230 MW;  46E1A319359751D3 CRC64;
     MKDVTIIGGG PSGLYASFYA GLRDMSVRLI DVQSELGGKM RIYPEKIIWD IGGIAPKPCH
     EILKDTIKQG LYFKPEVHLN ERVVDIRKKA ERHFEVETEA GEIYTSKAVI IAIGAGIINP
     KQLDVKGVER YQLTNLHYVV QSYRRFKDKD VLISGGGNTA LDWAHDIAKI AKSVTVVYRK
     EDVSGHEAMK TLVTDLNVKL CPKTRIKYLV GNDDETHISE VVLEHVESGD RHTVKFDDVI
     ISHGFDRCNT LLSETSSKLD MHDDCRVKGF GNTTTSIPGI YACGDIVYHD AKSHLIASAF
     SDGANAANLA KTYIQPDANA EGYVSSHHEV FKEANKTIVN KHLY
 
 
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