FPRB_MYCLE
ID FPRB_MYCLE Reviewed; 555 AA.
AC O33064;
DT 05-DEC-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Probable ferredoxin/ferredoxin--NADP reductase;
DE Short=FNR;
DE EC=1.18.1.2;
GN Name=fprB; OrderedLocusNames=ML2134; ORFNames=MLCB57.39;
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 -!- 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=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Note=Binds 1 or 2 [4Fe-4S] clusters.;
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC -!- SIMILARITY: In the C-terminal section; belongs to the ferredoxin--NADP
CC reductase family. {ECO:0000305}.
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DR EMBL; Z99494; CAB16679.1; -; Genomic_DNA.
DR EMBL; AL583924; CAC31089.1; -; Genomic_DNA.
DR PIR; T45351; T45351.
DR RefSeq; NP_302407.1; NC_002677.1.
DR RefSeq; WP_010908727.1; NC_002677.1.
DR AlphaFoldDB; O33064; -.
DR SMR; O33064; -.
DR STRING; 272631.ML2134; -.
DR EnsemblBacteria; CAC31089; CAC31089; CAC31089.
DR KEGG; mle:ML2134; -.
DR PATRIC; fig|272631.5.peg.4036; -.
DR Leproma; ML2134; -.
DR eggNOG; COG0493; Bacteria.
DR eggNOG; COG1145; Bacteria.
DR HOGENOM; CLU_024722_4_1_11; -.
DR OMA; VNCIHPS; -.
DR Proteomes; UP000000806; Chromosome.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0004324; F:ferredoxin-NADP+ reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 3.50.50.60; -; 1.
DR InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR023753; FAD/NAD-binding_dom.
DR Pfam; PF00037; Fer4; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR PROSITE; PS00198; 4FE4S_FER_1; 1.
DR PROSITE; PS51379; 4FE4S_FER_2; 2.
PE 3: Inferred from homology;
KW 4Fe-4S; Electron transport; FAD; Flavoprotein; Iron; Iron-sulfur;
KW Metal-binding; NADP; Oxidoreductase; Reference proteome; Repeat; Transport.
FT CHAIN 1..555
FT /note="Probable ferredoxin/ferredoxin--NADP reductase"
FT /id="PRO_0000167674"
FT DOMAIN 2..29
FT /note="4Fe-4S ferredoxin-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT DOMAIN 37..66
FT /note="4Fe-4S ferredoxin-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT REGION 115..555
FT /note="Ferredoxin--NADP reductase"
FT BINDING 9
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 15
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 19
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 46
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 49
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 52
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 56
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 123
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 143
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 151
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 187
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 213
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 258..261
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 302..303
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 314
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 453
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 460..462
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 460
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
SQ SEQUENCE 555 AA; 59712 MW; 43C7292E6A2DFED9 CRC64;
MPYIITQSCC NDGSCVFACP VNCIHPTPDE PGFATSEMLY IDPVACVDCG ACVSACPVGA
IASDTRLAPK QLPFIEINAS YYPARPIDLK LPPTSKLAPV IPAAQVHVRR RPLTVAIVGS
GPAAMYAADE LLTQPGVWVN VFEKLPTPYG LVRAGLAPDH QNTKKVTELF DRVAEHRRFR
FFLNVEIGRH LSHDELLAHH HAVLYAVGAP DDRRLNIDGM GIPGTGTATE LVAWINAHPD
FAYLPVDLSH ERVVVIGNGN VALDVARLLT ADPDNLARTD ISEFALHVLG GSAVREVVVA
ARRGPAHSAF TLPELIGLKA TSEVVLDAGD RKLVEGDFAT VSDSLTRKKL EVLSSLVDSS
KPTSRRRIRL AYQLTPKRVL GNQRATGVEF SVTGTEESRR FDAGLVLTSV GYRGKRIRDL
PFDEEAAVIP NDGGRVVDPS RGRPMPGAYV AGWIKRGPTG FIGTNKLCSV QTVQAVVADF
NAGWLTDPVA EPAELAKLVH ARQPDTVDSV GWRAIDAAEI AQGSTEGRPR RKFTDVADML
AVAAGAPPLR LRALS
