ID   FPRA_MYCTO              Reviewed;         456 AA.
AC   P9WIQ2; L0TBK5; O05783;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   03-AUG-2022, entry version 40.
DE   RecName: Full=NADPH-ferredoxin reductase FprA;
DE            Short=NFR;
DE            EC=1.18.1.2;
GN   Name=fprA; OrderedLocusNames=MT3189;
OS   Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83331;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC 1551 / Oshkosh;
RX   PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA   Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA   Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA   Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA   Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA   Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT   "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT   laboratory strains.";
RL   J. Bacteriol. 184:5479-5490(2002).
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; AE000516; AAK47528.1; -; Genomic_DNA.
DR   PIR; A70920; A70920.
DR   RefSeq; WP_003900632.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WIQ2; -.
DR   SMR; P9WIQ2; -.
DR   EnsemblBacteria; AAK47528; AAK47528; MT3189.
DR   KEGG; mtc:MT3189; -.
DR   PATRIC; fig|83331.31.peg.3439; -.
DR   HOGENOM; CLU_024722_3_0_11; -.
DR   Proteomes; UP000001020; 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.
FT   CHAIN           1..456
FT                   /note="NADPH-ferredoxin reductase FprA"
FT                   /id="PRO_0000427965"
FT   BINDING         14
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         40
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         48
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         84
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         110
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         155..158
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         199..200
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         211
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         359
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         366..368
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         366
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   456 AA;  49341 MW;  74D91282BD78BFB9 CRC64;
     MRPYYIAIVG SGPSAFFAAA SLLKAADTTE DLDMAVDMLE MLPTPWGLVR SGVAPDHPKI
     KSISKQFEKT AEDPRFRFFG NVVVGEHVQP GELSERYDAV IYAVGAQSDR MLNIPGEDLP
     GSIAAVDFVG WYNAHPHFEQ VSPDLSGARA VVIGNGNVAL DVARILLTDP DVLARTDIAD
     HALESLRPRG IQEVVIVGRR GPLQAAFTTL ELRELADLDG VDVVIDPAEL DGITDEDAAA
     VGKVCKQNIK VLRGYADREP RPGHRRMVFR FLTSPIEIKG KRKVERIVLG RNELVSDGSG
     RVAAKDTGER EELPAQLVVR SVGYRGVPTP GLPFDDQSGT IPNVGGRING SPNEYVVGWI
     KRGPTGVIGT NKKDAQDTVD TLIKNLGNAK EGAECKSFPE DHADQVADWL AARQPKLVTS
     AHWQVIDAFE RAAGEPHGRP RVKLASLAEL LRIGLG