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Database: UniProt
Entry: O33064
LinkDB: O33064
Original site: O33064 
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   16-JAN-2019, entry version 120.
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
CC         + 2 oxidized [2Fe-2S]-[ferredoxin]; Xref=Rhea:RHEA:20125,
CC         Rhea:RHEA-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--
CC       NADP reductase family. {ECO:0000305}.
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   ProteinModelPortal; O33064; -.
DR   SMR; O33064; -.
DR   STRING; 272631.ML2134; -.
DR   EnsemblBacteria; CAC31089; CAC31089; CAC31089.
DR   GeneID; 909093; -.
DR   KEGG; mle:ML2134; -.
DR   PATRIC; fig|272631.5.peg.4036; -.
DR   Leproma; ML2134; -.
DR   eggNOG; ENOG4105EQH; Bacteria.
DR   eggNOG; COG0493; LUCA.
DR   eggNOG; COG1146; LUCA.
DR   HOGENOM; HOG000249250; -.
DR   KO; K00528; -.
DR   OMA; VNCIHPS; -.
DR   BioCyc; MLEP272631:G1GT5-2337-MONOMER; -.
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   InterPro; IPR021163; Ferredox_Rdtase_adrenod.
DR   Pfam; PF00037; Fer4; 1.
DR   Pfam; PF07992; Pyr_redox_2; 1.
DR   PIRSF; PIRSF000362; FNR; 1.
DR   PROSITE; PS00198; 4FE4S_FER_1; 1.
DR   PROSITE; PS51379; 4FE4S_FER_2; 2.
PE   3: Inferred from homology;
KW   4Fe-4S; Complete proteome; Electron transport; FAD; Flavoprotein;
KW   Iron; Iron-sulfur; Metal-binding; NADP; Oxidoreductase;
KW   Reference proteome; Repeat; Transport.
FT   CHAIN         1    555       Probable ferredoxin/ferredoxin--NADP
FT                                reductase.
FT                                /FTId=PRO_0000167674.
FT   DOMAIN        2     29       4Fe-4S ferredoxin-type 1.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   DOMAIN       37     66       4Fe-4S ferredoxin-type 2.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   NP_BIND     258    261       NADP. {ECO:0000250}.
FT   NP_BIND     302    303       NADP. {ECO:0000250}.
FT   NP_BIND     460    462       FAD. {ECO:0000250}.
FT   REGION      115    555       Ferredoxin--NADP reductase.
FT   METAL         9      9       Iron-sulfur 1. {ECO:0000250}.
FT   METAL        15     15       Iron-sulfur 1. {ECO:0000250}.
FT   METAL        19     19       Iron-sulfur 2 (4Fe-4S). {ECO:0000250}.
FT   METAL        46     46       Iron-sulfur 2 (4Fe-4S). {ECO:0000250}.
FT   METAL        49     49       Iron-sulfur 2 (4Fe-4S). {ECO:0000250}.
FT   METAL        52     52       Iron-sulfur 2 (4Fe-4S). {ECO:0000250}.
FT   METAL        56     56       Iron-sulfur 1. {ECO:0000250}.
FT   BINDING     123    123       FAD; via amide nitrogen. {ECO:0000250}.
FT   BINDING     143    143       FAD. {ECO:0000250}.
FT   BINDING     151    151       FAD; via amide nitrogen. {ECO:0000250}.
FT   BINDING     187    187       FAD; via amide nitrogen and carbonyl
FT                                oxygen. {ECO:0000250}.
FT   BINDING     213    213       NADP. {ECO:0000250}.
FT   BINDING     314    314       NADP. {ECO:0000250}.
FT   BINDING     453    453       FAD; via amide nitrogen. {ECO:0000250}.
FT   BINDING     460    460       NADP; via amide nitrogen. {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
//
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