FENR2_BACSU
ID FENR2_BACSU Reviewed; 332 AA.
AC O05268; Q795K8;
DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-2009, sequence version 2.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Ferredoxin--NADP reductase 2;
DE Short=FNR 2;
DE Short=Fd-NADP(+) reductase 2;
DE EC=1.18.1.2;
GN Name=yumC; OrderedLocusNames=BSU32110;
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;
RA Oudega B., Koningsteyn G., Ramon-De Haan M., Rodrigues L.;
RT "Bacillus genome sequence project: sequence of yumA to pai; a segment of
RT the bacillus genome at about 284 degrees.";
RL Submitted (APR-1997) to the EMBL/GenBank/DDBJ databases.
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).
RN [3]
RP SEQUENCE REVISION TO 105-116.
RX PubMed=19383706; DOI=10.1099/mic.0.027839-0;
RA Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A.,
RA Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.;
RT "From a consortium sequence to a unified sequence: the Bacillus subtilis
RT 168 reference genome a decade later.";
RL Microbiology 155:1758-1775(2009).
RN [4]
RP PROTEIN SEQUENCE OF 1-17, BIOPHYSICOCHEMICAL PROPERTIES, CATALYTIC
RP ACTIVITY, SUBUNIT, AND COFACTOR.
RX PubMed=15252706; DOI=10.1007/s00203-004-0701-5;
RA Seo D., Kamino K., Inoue K., Sakurai H.;
RT "Purification and characterization of ferredoxin-NADP+ reductase encoded by
RT Bacillus subtilis yumC.";
RL Arch. Microbiol. 182:80-89(2004).
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:15252706};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000269|PubMed:15252706};
CC Note=Binds 1 FAD per subunit. {ECO:0000269|PubMed:15252706};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.54 uM for NADPH (at 24 degrees Celsius and pH 7.0)
CC {ECO:0000269|PubMed:15252706};
CC Note=KM for NADH is < 0.1 uM.;
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:15252706}.
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; Z93939; CAB07954.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB15201.2; -; Genomic_DNA.
DR PIR; B70015; B70015.
DR RefSeq; NP_391091.2; NC_000964.3.
DR RefSeq; WP_003220618.1; NZ_JNCM01000033.1.
DR PDB; 3LZW; X-ray; 1.80 A; A=1-332.
DR PDB; 3LZX; X-ray; 1.90 A; A/B=1-332.
DR PDBsum; 3LZW; -.
DR PDBsum; 3LZX; -.
DR AlphaFoldDB; O05268; -.
DR SMR; O05268; -.
DR IntAct; O05268; 1.
DR MINT; O05268; -.
DR STRING; 224308.BSU32110; -.
DR jPOST; O05268; -.
DR PaxDb; O05268; -.
DR PRIDE; O05268; -.
DR EnsemblBacteria; CAB15201; CAB15201; BSU_32110.
DR GeneID; 64304956; -.
DR GeneID; 936577; -.
DR KEGG; bsu:BSU32110; -.
DR PATRIC; fig|224308.179.peg.3477; -.
DR eggNOG; COG0492; Bacteria.
DR InParanoid; O05268; -.
DR OMA; PEKVIYD; -.
DR PhylomeDB; O05268; -.
DR BioCyc; BSUB:BSU32110-MON; -.
DR BRENDA; 1.14.14.47; 9933.
DR BRENDA; 1.18.1.2; 658.
DR BRENDA; 1.19.1.1; 658.
DR SABIO-RK; O05268; -.
DR EvolutionaryTrace; O05268; -.
DR PRO; PR:O05268; -.
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 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..332
FT /note="Ferredoxin--NADP reductase 2"
FT /id="PRO_0000360548"
FT BINDING 37
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 45
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 50
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 90
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 124
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 285
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 326
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT CONFLICT 105..116
FT /note="TNEETHYSKTVI -> QMKKPTTLKRSC (in Ref. 1; CAB07954)"
FT /evidence="ECO:0000305"
FT STRAND 2..13
FT /evidence="ECO:0007829|PDB:3LZW"
FT HELIX 17..28
FT /evidence="ECO:0007829|PDB:3LZW"
FT STRAND 33..36
FT /evidence="ECO:0007829|PDB:3LZW"
FT STRAND 38..42
FT /evidence="ECO:0007829|PDB:3LZW"
FT HELIX 44..49
FT /evidence="ECO:0007829|PDB:3LZW"
FT STRAND 53..55
FT /evidence="ECO:0007829|PDB:3LZW"
FT STRAND 62..65
FT /evidence="ECO:0007829|PDB:3LZW"
FT HELIX 66..77
FT /evidence="ECO:0007829|PDB:3LZW"
FT STRAND 83..85
FT /evidence="ECO:0007829|PDB:3LZW"
FT STRAND 90..95
FT /evidence="ECO:0007829|PDB:3LZW"
FT STRAND 101..117
FT /evidence="ECO:0007829|PDB:3LZW"
FT STRAND 122..126
FT /evidence="ECO:0007829|PDB:3LZX"
FT HELIX 134..137
FT /evidence="ECO:0007829|PDB:3LZW"
FT TURN 139..141
FT /evidence="ECO:0007829|PDB:3LZW"
FT STRAND 142..145
FT /evidence="ECO:0007829|PDB:3LZW"
FT HELIX 149..152
FT /evidence="ECO:0007829|PDB:3LZW"
FT STRAND 156..160
FT /evidence="ECO:0007829|PDB:3LZW"
FT HELIX 164..173
FT /evidence="ECO:0007829|PDB:3LZW"
FT TURN 174..176
FT /evidence="ECO:0007829|PDB:3LZW"
FT STRAND 177..183
FT /evidence="ECO:0007829|PDB:3LZW"
FT STRAND 185..188
FT /evidence="ECO:0007829|PDB:3LZW"
FT HELIX 193..201
FT /evidence="ECO:0007829|PDB:3LZW"
FT STRAND 205..207
FT /evidence="ECO:0007829|PDB:3LZW"
FT STRAND 210..216
FT /evidence="ECO:0007829|PDB:3LZW"
FT STRAND 218..220
FT /evidence="ECO:0007829|PDB:3LZW"
FT STRAND 223..228
FT /evidence="ECO:0007829|PDB:3LZW"
FT STRAND 234..238
FT /evidence="ECO:0007829|PDB:3LZW"
FT STRAND 240..244
FT /evidence="ECO:0007829|PDB:3LZW"
FT STRAND 248..251
FT /evidence="ECO:0007829|PDB:3LZX"
FT HELIX 253..257
FT /evidence="ECO:0007829|PDB:3LZW"
FT STRAND 266..268
FT /evidence="ECO:0007829|PDB:3LZW"
FT STRAND 280..282
FT /evidence="ECO:0007829|PDB:3LZW"
FT HELIX 284..286
FT /evidence="ECO:0007829|PDB:3LZW"
FT HELIX 296..314
FT /evidence="ECO:0007829|PDB:3LZW"
FT HELIX 325..328
FT /evidence="ECO:0007829|PDB:3LZW"
SQ SEQUENCE 332 AA; 36841 MW; E84835A1861A1529 CRC64;
MREDTKVYDI TIIGGGPVGL FTAFYGGMRQ ASVKIIESLP QLGGQLSALY PEKYIYDVAG
FPKIRAQELI NNLKEQMAKF DQTICLEQAV ESVEKQADGV FKLVTNEETH YSKTVIITAG
NGAFKPRKLE LENAEQYEGK NLHYFVDDLQ KFAGRRVAIL GGGDSAVDWA LMLEPIAKEV
SIIHRRDKFR AHEHSVENLH ASKVNVLTPF VPAELIGEDK IEQLVLEEVK GDRKEILEID
DLIVNYGFVS SLGPIKNWGL DIEKNSIVVK STMETNIEGF FAAGDICTYE GKVNLIASGF
GEAPTAVNNA KAYMDPKARV QPLHSTSLFE NK
