(data stored in SCRATCH zone)

SWISSPROT: 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   11-DEC-2019, entry version 117.
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};
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   SMR; O31475; -.
DR   STRING; 224308.BSU03270; -.
DR   PaxDb; O31475; -.
DR   PRIDE; O31475; -.
DR   EnsemblBacteria; CAB12121; CAB12121; BSU03270.
DR   GeneID; 938327; -.
DR   KEGG; bsu:BSU03270; -.
DR   PATRIC; fig|224308.179.peg.341; -.
DR   eggNOG; COG0492; LUCA.
DR   HOGENOM; HOG000072909; -.
DR   InParanoid; O31475; -.
DR   KO; K21567; -.
DR   OMA; FYSGMRD; -.
DR   PhylomeDB; O31475; -.
DR   BioCyc; BSUB:BSU03270-MONOMER; -.
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: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;
DR   PRODOM; O31475.
DR   SWISS-2DPAGE; O31475.
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                   /note="FAD"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01685"
FT   BINDING         45
FT                   /note="FAD"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01685"
FT   BINDING         50
FT                   /note="FAD"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01685"
FT   BINDING         90
FT                   /note="FAD; via amide nitrogen and carbonyl oxygen"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01685"
FT   BINDING         125
FT                   /note="FAD; via amide nitrogen"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01685"
FT   BINDING         287
FT                   /note="FAD"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01685"
FT   BINDING         328
FT                   /note="FAD"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01685"
FT   STRAND          7..13
FT                   /evidence="ECO:0000244|PDB:5XHU"
FT   HELIX           17..28
FT                   /evidence="ECO:0000244|PDB:5XHU"
FT   STRAND          33..36
FT                   /evidence="ECO:0000244|PDB:5XHU"
FT   STRAND          38..42
FT                   /evidence="ECO:0000244|PDB:5XHU"
FT   HELIX           44..49
FT                   /evidence="ECO:0000244|PDB:5XHU"
FT   STRAND          53..55
FT                   /evidence="ECO:0000244|PDB:5XHU"
FT   HELIX           66..78
FT                   /evidence="ECO:0000244|PDB:5XHU"
FT   STRAND          83..85
FT                   /evidence="ECO:0000244|PDB:5XHU"
FT   STRAND          90..95
FT                   /evidence="ECO:0000244|PDB:5XHU"
FT   STRAND          101..105
FT                   /evidence="ECO:0000244|PDB:5XHU"
FT   STRAND          110..118
FT                   /evidence="ECO:0000244|PDB:5XHU"
FT   HELIX           132..138
FT                   /evidence="ECO:0000244|PDB:5XHU"
FT   TURN            139..142
FT                   /evidence="ECO:0000244|PDB:5XHU"
FT   STRAND          143..146
FT                   /evidence="ECO:0000244|PDB:5XHU"
FT   HELIX           150..153
FT                   /evidence="ECO:0000244|PDB:5XHU"
FT   STRAND          157..161
FT                   /evidence="ECO:0000244|PDB:5XHU"
FT   HELIX           165..174
FT                   /evidence="ECO:0000244|PDB:5XHU"
FT   TURN            175..177
FT                   /evidence="ECO:0000244|PDB:5XHU"
FT   STRAND          178..184
FT                   /evidence="ECO:0000244|PDB:5XHU"
FT   STRAND          186..188
FT                   /evidence="ECO:0000244|PDB:5XHU"
FT   HELIX           194..202
FT                   /evidence="ECO:0000244|PDB:5XHU"
FT   STRAND          206..208
FT                   /evidence="ECO:0000244|PDB:5XHU"
FT   STRAND          211..218
FT                   /evidence="ECO:0000244|PDB:5XHU"
FT   STRAND          223..230
FT                   /evidence="ECO:0000244|PDB:5XHU"
FT   TURN            231..233
FT                   /evidence="ECO:0000244|PDB:5XHU"
FT   STRAND          236..240
FT                   /evidence="ECO:0000244|PDB:5XHU"
FT   STRAND          242..246
FT                   /evidence="ECO:0000244|PDB:5XHU"
FT   HELIX           255..259
FT                   /evidence="ECO:0000244|PDB:5XHU"
FT   STRAND          268..270
FT                   /evidence="ECO:0000244|PDB:5XHU"
FT   STRAND          282..284
FT                   /evidence="ECO:0000244|PDB:5XHU"
FT   HELIX           286..288
FT                   /evidence="ECO:0000244|PDB:5XHU"
FT   HELIX           298..316
FT                   /evidence="ECO:0000244|PDB:5XHU"
FT   HELIX           327..329
FT                   /evidence="ECO:0000244|PDB:5XHU"
FT   TURN            331..333
FT                   /evidence="ECO:0000244|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
//

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