FENR1_BACSU
ID FENR1_BACSU Reviewed; 336 AA.
AC O31475; P94397;
DT 03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Ferredoxin--NADP reductase 1 {ECO:0000255|HAMAP-Rule:MF_01685};
DE Short=FNR 1 {ECO:0000255|HAMAP-Rule:MF_01685};
DE Short=Fd-NADP(+) reductase 1 {ECO:0000255|HAMAP-Rule:MF_01685};
DE EC=1.18.1.2 {ECO:0000255|HAMAP-Rule:MF_01685};
GN Name=ycgT; OrderedLocusNames=BSU03270;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=8969502; DOI=10.1099/13500872-142-11-3047;
RA Yamane K., Kumano M., Kurita K.;
RT "The 25 degrees-36 degrees region of the Bacillus subtilis chromosome:
RT determination of the sequence of a 146 kb segment and identification of 113
RT genes.";
RL Microbiology 142:3047-3056(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA08961.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; D50453; BAA08961.1; ALT_FRAME; Genomic_DNA.
DR EMBL; AL009126; CAB12121.1; -; Genomic_DNA.
DR PIR; G69759; G69759.
DR RefSeq; NP_388209.1; NC_000964.3.
DR RefSeq; WP_003234643.1; NZ_JNCM01000030.1.
DR PDB; 5XHU; X-ray; 2.10 A; A=6-334.
DR PDBsum; 5XHU; -.
DR AlphaFoldDB; O31475; -.
DR SMR; O31475; -.
DR STRING; 224308.BSU03270; -.
DR PaxDb; O31475; -.
DR PRIDE; O31475; -.
DR EnsemblBacteria; CAB12121; CAB12121; BSU_03270.
DR GeneID; 938327; -.
DR KEGG; bsu:BSU03270; -.
DR PATRIC; fig|224308.179.peg.341; -.
DR eggNOG; COG0492; Bacteria.
DR InParanoid; O31475; -.
DR OMA; FYSGMRD; -.
DR PhylomeDB; O31475; -.
DR BioCyc; BSUB:BSU03270-MON; -.
DR Proteomes; UP000001570; 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 GO; GO:0071281; P:cellular response to iron ion; IDA:CollecTF.
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..336
FT /note="Ferredoxin--NADP reductase 1"
FT /id="PRO_0000364801"
FT BINDING 37
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01685"
FT BINDING 45
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01685"
FT BINDING 50
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01685"
FT BINDING 90
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01685"
FT BINDING 125
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 7..13
FT /evidence="ECO:0007829|PDB:5XHU"
FT HELIX 17..28
FT /evidence="ECO:0007829|PDB:5XHU"
FT STRAND 33..36
FT /evidence="ECO:0007829|PDB:5XHU"
FT STRAND 38..42
FT /evidence="ECO:0007829|PDB:5XHU"
FT HELIX 44..49
FT /evidence="ECO:0007829|PDB:5XHU"
FT STRAND 53..55
FT /evidence="ECO:0007829|PDB:5XHU"
FT HELIX 66..78
FT /evidence="ECO:0007829|PDB:5XHU"
FT STRAND 83..85
FT /evidence="ECO:0007829|PDB:5XHU"
FT STRAND 90..95
FT /evidence="ECO:0007829|PDB:5XHU"
FT STRAND 101..105
FT /evidence="ECO:0007829|PDB:5XHU"
FT STRAND 110..118
FT /evidence="ECO:0007829|PDB:5XHU"
FT HELIX 132..138
FT /evidence="ECO:0007829|PDB:5XHU"
FT TURN 139..142
FT /evidence="ECO:0007829|PDB:5XHU"
FT STRAND 143..146
FT /evidence="ECO:0007829|PDB:5XHU"
FT HELIX 150..153
FT /evidence="ECO:0007829|PDB:5XHU"
FT STRAND 157..161
FT /evidence="ECO:0007829|PDB:5XHU"
FT HELIX 165..174
FT /evidence="ECO:0007829|PDB:5XHU"
FT TURN 175..177
FT /evidence="ECO:0007829|PDB:5XHU"
FT STRAND 178..184
FT /evidence="ECO:0007829|PDB:5XHU"
FT STRAND 186..188
FT /evidence="ECO:0007829|PDB:5XHU"
FT HELIX 194..202
FT /evidence="ECO:0007829|PDB:5XHU"
FT STRAND 206..208
FT /evidence="ECO:0007829|PDB:5XHU"
FT STRAND 211..218
FT /evidence="ECO:0007829|PDB:5XHU"
FT STRAND 223..230
FT /evidence="ECO:0007829|PDB:5XHU"
FT TURN 231..233
FT /evidence="ECO:0007829|PDB:5XHU"
FT STRAND 236..240
FT /evidence="ECO:0007829|PDB:5XHU"
FT STRAND 242..246
FT /evidence="ECO:0007829|PDB:5XHU"
FT HELIX 255..259
FT /evidence="ECO:0007829|PDB:5XHU"
FT STRAND 268..270
FT /evidence="ECO:0007829|PDB:5XHU"
FT STRAND 282..284
FT /evidence="ECO:0007829|PDB:5XHU"
FT HELIX 286..288
FT /evidence="ECO:0007829|PDB:5XHU"
FT HELIX 298..316
FT /evidence="ECO:0007829|PDB:5XHU"
FT HELIX 327..329
FT /evidence="ECO:0007829|PDB:5XHU"
FT TURN 331..333
FT /evidence="ECO:0007829|PDB:5XHU"
SQ SEQUENCE 336 AA; 36967 MW; BF7F1617376AD742 CRC64;
MAENQEVYDV TIIGGGPIGL FTAFYCGMRE LKTKVIEFLP KLGGKVSLFF PEKIIRDIGG
IPGIAGKQLI EQLKEQAATF DPDIVLNQRV TGFERLDDGT IVLTGSEGKK HYTRTVILAC
GMGTLEVNEF DSEDAARYAG KNLHYGVEKL DAFKGKRVVI SGGGDTAVDW ANELEPIAAS
VTVVHRREEF GGMESSVTKM KQSSVRVLTP YRLEQLNGDE EGIKSVTVCH TESGQRKDIE
IDELIINHGF KIDLGPMMEW GLEIEEGRVK ADRHMRTNLP GVFVAGDAAF YESKLRLIAG
GFTEGPTAVN SAKAYLDPKA ENMAMYSTHH KKLVHK
