FENR_CHLTE
ID FENR_CHLTE Reviewed; 360 AA.
AC Q8KCB2;
DT 03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Ferredoxin--NADP reductase;
DE Short=FNR;
DE Short=Fd-NADP(+) reductase;
DE EC=1.18.1.2;
GN OrderedLocusNames=CT1512;
OS Chlorobaculum tepidum (strain ATCC 49652 / DSM 12025 / NBRC 103806 / TLS)
OS (Chlorobium tepidum).
OC Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae; Chlorobaculum.
OX NCBI_TaxID=194439;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49652 / DSM 12025 / NBRC 103806 / TLS;
RX PubMed=12093901; DOI=10.1073/pnas.132181499;
RA Eisen J.A., Nelson K.E., Paulsen I.T., Heidelberg J.F., Wu M., Dodson R.J.,
RA DeBoy R.T., Gwinn M.L., Nelson W.C., Haft D.H., Hickey E.K., Peterson J.D.,
RA Durkin A.S., Kolonay J.F., Yang F., Holt I.E., Umayam L.A., Mason T.M.,
RA Brenner M., Shea T.P., Parksey D.S., Nierman W.C., Feldblyum T.V.,
RA Hansen C.L., Craven M.B., Radune D., Vamathevan J.J., Khouri H.M.,
RA White O., Gruber T.M., Ketchum K.A., Venter J.C., Tettelin H., Bryant D.A.,
RA Fraser C.M.;
RT "The complete genome sequence of Chlorobium tepidum TLS, a photosynthetic,
RT anaerobic, green-sulfur bacterium.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:9509-9514(2002).
RN [2]
RP PROTEIN SEQUENCE OF 1-25, CATALYTIC ACTIVITY, SUBUNIT, AND COFACTOR.
RX PubMed=12009411; DOI=10.1016/s0167-4838(02)00269-8;
RA Seo D., Sakurai H.;
RT "Purification and characterization of ferredoxin-NAD(P)(+) reductase from
RT the green sulfur bacterium Chlorobium tepidum.";
RL Biochim. Biophys. Acta 1597:123-132(2002).
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 Evidence={ECO:0000269|PubMed:12009411};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000269|PubMed:12009411};
CC Note=Binds 1 FAD per subunit. {ECO:0000269|PubMed:12009411};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:12009411}.
CC -!- SIMILARITY: Belongs to the ferredoxin--NADP reductase type 2 family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE006470; AAM72739.1; -; Genomic_DNA.
DR RefSeq; NP_662397.1; NC_002932.3.
DR RefSeq; WP_010933178.1; NC_002932.3.
DR PDB; 3AB1; X-ray; 2.39 A; A/B=1-360.
DR PDBsum; 3AB1; -.
DR AlphaFoldDB; Q8KCB2; -.
DR SMR; Q8KCB2; -.
DR STRING; 194439.CT1512; -.
DR EnsemblBacteria; AAM72739; AAM72739; CT1512.
DR KEGG; cte:CT1512; -.
DR PATRIC; fig|194439.7.peg.1372; -.
DR eggNOG; COG0492; Bacteria.
DR HOGENOM; CLU_031864_5_5_10; -.
DR OMA; LEQCAPF; -.
DR OrthoDB; 692968at2; -.
DR BRENDA; 1.18.1.2; 1345.
DR Proteomes; UP000001007; 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; Direct protein sequencing; FAD; Flavoprotein; NADP;
KW Oxidoreductase; Reference proteome.
FT CHAIN 1..360
FT /note="Ferredoxin--NADP reductase"
FT /id="PRO_0000364821"
FT BINDING 25
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 44
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 52
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 57
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 97
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 132
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 298
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 339
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT STRAND 15..20
FT /evidence="ECO:0007829|PDB:3AB1"
FT HELIX 24..35
FT /evidence="ECO:0007829|PDB:3AB1"
FT STRAND 40..43
FT /evidence="ECO:0007829|PDB:3AB1"
FT STRAND 45..49
FT /evidence="ECO:0007829|PDB:3AB1"
FT HELIX 51..55
FT /evidence="ECO:0007829|PDB:3AB1"
FT STRAND 60..62
FT /evidence="ECO:0007829|PDB:3AB1"
FT STRAND 69..72
FT /evidence="ECO:0007829|PDB:3AB1"
FT HELIX 73..85
FT /evidence="ECO:0007829|PDB:3AB1"
FT STRAND 90..92
FT /evidence="ECO:0007829|PDB:3AB1"
FT STRAND 97..102
FT /evidence="ECO:0007829|PDB:3AB1"
FT STRAND 108..112
FT /evidence="ECO:0007829|PDB:3AB1"
FT STRAND 117..125
FT /evidence="ECO:0007829|PDB:3AB1"
FT HELIX 138..140
FT /evidence="ECO:0007829|PDB:3AB1"
FT TURN 144..146
FT /evidence="ECO:0007829|PDB:3AB1"
FT TURN 148..150
FT /evidence="ECO:0007829|PDB:3AB1"
FT STRAND 151..154
FT /evidence="ECO:0007829|PDB:3AB1"
FT HELIX 158..161
FT /evidence="ECO:0007829|PDB:3AB1"
FT STRAND 165..169
FT /evidence="ECO:0007829|PDB:3AB1"
FT HELIX 173..181
FT /evidence="ECO:0007829|PDB:3AB1"
FT TURN 182..185
FT /evidence="ECO:0007829|PDB:3AB1"
FT STRAND 186..192
FT /evidence="ECO:0007829|PDB:3AB1"
FT STRAND 194..197
FT /evidence="ECO:0007829|PDB:3AB1"
FT HELIX 203..206
FT /evidence="ECO:0007829|PDB:3AB1"
FT HELIX 209..213
FT /evidence="ECO:0007829|PDB:3AB1"
FT STRAND 216..231
FT /evidence="ECO:0007829|PDB:3AB1"
FT STRAND 234..242
FT /evidence="ECO:0007829|PDB:3AB1"
FT STRAND 247..251
FT /evidence="ECO:0007829|PDB:3AB1"
FT STRAND 253..257
FT /evidence="ECO:0007829|PDB:3AB1"
FT HELIX 266..270
FT /evidence="ECO:0007829|PDB:3AB1"
FT STRAND 279..281
FT /evidence="ECO:0007829|PDB:3AB1"
FT STRAND 293..295
FT /evidence="ECO:0007829|PDB:3AB1"
FT HELIX 309..327
FT /evidence="ECO:0007829|PDB:3AB1"
FT HELIX 338..347
FT /evidence="ECO:0007829|PDB:3AB1"
SQ SEQUENCE 360 AA; 39240 MW; F016A6B0602475B1 CRC64;
MLDIHNPATD HHDMRDLTII GGGPTGIFAA FQCGMNNISC RIIESMPQLG GQLAALYPEK
HIYDVAGFPE VPAIDLVESL WAQAERYNPD VVLNETVTKY TKLDDGTFET RTNTGNVYRS
RAVLIAAGLG AFEPRKLPQL GNIDHLTGSS VYYAVKSVED FKGKRVVIVG GGDSALDWTV
GLIKNAASVT LVHRGHEFQG HGKTAHEVER ARANGTIDVY LETEVASIEE SNGVLTRVHL
RSSDGSKWTV EADRLLILIG FKSNLGPLAR WDLELYENAL VVDSHMKTSV DGLYAAGDIA
YYPGKLKIIQ TGLSEATMAV RHSLSYIKPG EKIRNVFSSV KMAKEKKAAE AGNATENKAE
