FENR_THET8
ID FENR_THET8 Reviewed; 335 AA.
AC Q5SL28;
DT 03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Ferredoxin--NADP reductase;
DE Short=FNR;
DE Short=Fd-NADP(+) reductase;
DE EC=1.18.1.2;
GN OrderedLocusNames=TTHA0465;
OS Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8).
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=300852;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27634 / DSM 579 / HB8;
RA Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T.,
RA Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.;
RT "Complete genome sequence of Thermus thermophilus HB8.";
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN COMPLEX WITH FAD, COFACTOR, AND
RP SUBUNIT.
RG RIKEN structural genomics initiative (RSGI);
RT "Crystal structure of thioredoxin reductase-like protein from Thermus
RT thermophilus HB8.";
RL Submitted (NOV-2007) to the PDB data bank.
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;
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000269|Ref.2};
CC Note=Binds 1 FAD per subunit. {ECO:0000269|Ref.2};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|Ref.2}.
CC -!- SIMILARITY: Belongs to the ferredoxin--NADP reductase type 2 family.
CC {ECO:0000305}.
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DR EMBL; AP008226; BAD70288.1; -; Genomic_DNA.
DR RefSeq; WP_011227955.1; NC_006461.1.
DR RefSeq; YP_143731.1; NC_006461.1.
DR PDB; 2ZBW; X-ray; 2.10 A; A/B=1-335.
DR PDBsum; 2ZBW; -.
DR AlphaFoldDB; Q5SL28; -.
DR SMR; Q5SL28; -.
DR STRING; 300852.55771847; -.
DR EnsemblBacteria; BAD70288; BAD70288; BAD70288.
DR GeneID; 3169949; -.
DR KEGG; ttj:TTHA0465; -.
DR PATRIC; fig|300852.9.peg.464; -.
DR eggNOG; COG0492; Bacteria.
DR HOGENOM; CLU_031864_5_5_0; -.
DR OMA; PEKVIYD; -.
DR PhylomeDB; Q5SL28; -.
DR EvolutionaryTrace; Q5SL28; -.
DR Proteomes; UP000000532; 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; Reference proteome.
FT CHAIN 1..335
FT /note="Ferredoxin--NADP reductase"
FT /id="PRO_0000364981"
FT BINDING 16
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|Ref.2"
FT BINDING 35
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|Ref.2"
FT BINDING 43
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|Ref.2"
FT BINDING 48
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|Ref.2"
FT BINDING 88
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|Ref.2"
FT BINDING 122
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|Ref.2"
FT BINDING 287
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|Ref.2"
FT BINDING 328
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|Ref.2"
FT STRAND 5..11
FT /evidence="ECO:0007829|PDB:2ZBW"
FT HELIX 15..26
FT /evidence="ECO:0007829|PDB:2ZBW"
FT STRAND 31..40
FT /evidence="ECO:0007829|PDB:2ZBW"
FT HELIX 42..46
FT /evidence="ECO:0007829|PDB:2ZBW"
FT STRAND 51..53
FT /evidence="ECO:0007829|PDB:2ZBW"
FT STRAND 60..63
FT /evidence="ECO:0007829|PDB:2ZBW"
FT HELIX 64..75
FT /evidence="ECO:0007829|PDB:2ZBW"
FT HELIX 76..78
FT /evidence="ECO:0007829|PDB:2ZBW"
FT STRAND 81..85
FT /evidence="ECO:0007829|PDB:2ZBW"
FT STRAND 88..94
FT /evidence="ECO:0007829|PDB:2ZBW"
FT STRAND 97..102
FT /evidence="ECO:0007829|PDB:2ZBW"
FT STRAND 107..115
FT /evidence="ECO:0007829|PDB:2ZBW"
FT STRAND 120..124
FT /evidence="ECO:0007829|PDB:2ZBW"
FT TURN 130..135
FT /evidence="ECO:0007829|PDB:2ZBW"
FT TURN 137..139
FT /evidence="ECO:0007829|PDB:2ZBW"
FT STRAND 140..143
FT /evidence="ECO:0007829|PDB:2ZBW"
FT HELIX 147..150
FT /evidence="ECO:0007829|PDB:2ZBW"
FT STRAND 154..158
FT /evidence="ECO:0007829|PDB:2ZBW"
FT HELIX 162..170
FT /evidence="ECO:0007829|PDB:2ZBW"
FT TURN 171..174
FT /evidence="ECO:0007829|PDB:2ZBW"
FT STRAND 175..181
FT /evidence="ECO:0007829|PDB:2ZBW"
FT STRAND 183..186
FT /evidence="ECO:0007829|PDB:2ZBW"
FT HELIX 191..202
FT /evidence="ECO:0007829|PDB:2ZBW"
FT STRAND 205..209
FT /evidence="ECO:0007829|PDB:2ZBW"
FT STRAND 212..230
FT /evidence="ECO:0007829|PDB:2ZBW"
FT TURN 231..233
FT /evidence="ECO:0007829|PDB:2ZBW"
FT STRAND 236..240
FT /evidence="ECO:0007829|PDB:2ZBW"
FT STRAND 242..246
FT /evidence="ECO:0007829|PDB:2ZBW"
FT STRAND 250..253
FT /evidence="ECO:0007829|PDB:2ZBW"
FT HELIX 255..259
FT /evidence="ECO:0007829|PDB:2ZBW"
FT STRAND 268..270
FT /evidence="ECO:0007829|PDB:2ZBW"
FT STRAND 282..284
FT /evidence="ECO:0007829|PDB:2ZBW"
FT HELIX 298..316
FT /evidence="ECO:0007829|PDB:2ZBW"
FT HELIX 327..329
FT /evidence="ECO:0007829|PDB:2ZBW"
SQ SEQUENCE 335 AA; 36207 MW; F0C4631F805520C0 CRC64;
MAADHTDVLI VGAGPTGLFA GFYVGMRGLS FRFVDPLPEP GGQLTALYPE KYIYDVAGFP
KVYAKDLVKG LVEQVAPFNP VYSLGERAET LEREGDLFKV TTSQGNAYTA KAVIIAAGVG
AFEPRRIGAP GEREFEGRGV YYAVKSKAEF QGKRVLIVGG GDSAVDWALN LLDTARRITL
IHRRPQFRAH EASVKELMKA HEEGRLEVLT PYELRRVEGD ERVRWAVVFH NQTQEELALE
VDAVLILAGY ITKLGPLANW GLALEKNKIK VDTTMATSIP GVYACGDIVT YPGKLPLIVL
GFGEAAIAAN HAAAYANPAL KVNPGHSSEK AAPGT
