ID   FPRA_MYCLE              Reviewed;         456 AA.
AC   O32886;
DT   11-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 117.
DE   RecName: Full=NADPH-ferredoxin reductase FprA;
DE            Short=NFR;
DE            EC=1.18.1.2;
GN   Name=fprA; OrderedLocusNames=ML0666; ORFNames=MLCB1779.25;
OS   Mycobacterium leprae (strain TN).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=272631;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TN;
RX   PubMed=11234002; DOI=10.1038/35059006;
RA   Cole S.T., Eiglmeier K., Parkhill J., James K.D., Thomson N.R.,
RA   Wheeler P.R., Honore N., Garnier T., Churcher C.M., Harris D.E.,
RA   Mungall K.L., Basham D., Brown D., Chillingworth T., Connor R.,
RA   Davies R.M., Devlin K., Duthoy S., Feltwell T., Fraser A., Hamlin N.,
RA   Holroyd S., Hornsby T., Jagels K., Lacroix C., Maclean J., Moule S.,
RA   Murphy L.D., Oliver K., Quail M.A., Rajandream M.A., Rutherford K.M.,
RA   Rutter S., Seeger K., Simon S., Simmonds M., Skelton J., Squares R.,
RA   Squares S., Stevens K., Taylor K., Whitehead S., Woodward J.R.,
RA   Barrell B.G.;
RT   "Massive gene decay in the leprosy bacillus.";
RL   Nature 409:1007-1011(2001).
CC   -!- FUNCTION: May serve as electron transfer protein and supply electrons
CC       to P450 systems. {ECO:0000250}.
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:0000250};
CC   -!- SUBUNIT: Monomer. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the ferredoxin--NADP reductase type 1 family.
CC       {ECO:0000305}.
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DR   EMBL; Z98271; CAB11006.1; -; Genomic_DNA.
DR   EMBL; AL583919; CAC30175.1; -; Genomic_DNA.
DR   PIR; T45314; T45314.
DR   RefSeq; NP_301540.1; NC_002677.1.
DR   RefSeq; WP_010907864.1; NC_002677.1.
DR   AlphaFoldDB; O32886; -.
DR   SMR; O32886; -.
DR   STRING; 272631.ML0666; -.
DR   EnsemblBacteria; CAC30175; CAC30175; CAC30175.
DR   KEGG; mle:ML0666; -.
DR   PATRIC; fig|272631.5.peg.1186; -.
DR   Leproma; ML0666; -.
DR   eggNOG; COG0493; Bacteria.
DR   HOGENOM; CLU_024722_3_0_11; -.
DR   OMA; MRPYHVA; -.
DR   Proteomes; UP000000806; Chromosome.
DR   GO; GO:0004324; F:ferredoxin-NADP+ reductase activity; IEA:UniProtKB-EC.
DR   Gene3D; 3.50.50.60; -; 1.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR023753; FAD/NAD-binding_dom.
DR   InterPro; IPR021163; Ferredox_Rdtase_adrenod.
DR   Pfam; PF07992; Pyr_redox_2; 1.
DR   PIRSF; PIRSF000362; FNR; 1.
PE   3: Inferred from homology;
KW   FAD; Flavoprotein; NADP; Oxidoreductase; Reference proteome.
FT   CHAIN           1..456
FT                   /note="NADPH-ferredoxin reductase FprA"
FT                   /id="PRO_0000087328"
FT   BINDING         17
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         43
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         51
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         87
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         113
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         158..161
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         202..203
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         214
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         362
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         369..371
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         369
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   456 AA;  49630 MW;  B3506A27B4B3AC79 CRC64;
     MRPHHIHHIA IVGSGPSGFF AAASVLKAAD ASDEINVAVD MLEMLPTPWG LVRSGVAPDH
     PKIKSISKQF EKTAEDPRFR FFGNVIVGKH IEPAELAERY DAVIYAVGAQ SDRALNIPGE
     DLPGSIAAVD FVGWYNAHPN FHERSPDLSG SRAVVIGNGN VALDVTRILI TDPDVLAFTD
     IADHALESLR PRGIEEVVIV GRRGPLQTAF TTLELRELAD IEGVDVLVDP AQLEGISDEN
     AAAAGKTTRQ NIKVLRDYTV RTPKPGHRRI VFRFLTSPIE IKGKGKVERI VLGQNELVTD
     DNGRVAAKDT GVREELPAQL IVRSIGYRGV PTPGLPFDDS SVTIPNTNGR VNGSRNEYVV
     GWIKRGPTGV IGTNKKDSQD TVDTLMENLA GANDTEKFGA DHADRLAEWL AERQPKLVTS
     AHWQAIDRFE RAAGEPHGRP RVKLPNLAEL LRIGHG