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Database: UniProt
Entry: P65529
LinkDB: P65529
Original site: P65529 
ID   FPRB_MYCBO              Reviewed;         575 AA.
AC   P65529; A0A1R3XWP3; Q10547; X2BGE5;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   05-DEC-2018, entry version 93.
DE   RecName: Full=Probable ferredoxin/ferredoxin--NADP reductase;
DE            Short=FNR;
DE            EC=1.18.1.2;
GN   Name=fprB; OrderedLocusNames=BQ2027_MB0910;
OS   Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=233413;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-935 / AF2122/97;
RX   PubMed=12788972; DOI=10.1073/pnas.1130426100;
RA   Garnier T., Eiglmeier K., Camus J.-C., Medina N., Mansoor H.,
RA   Pryor M., Duthoy S., Grondin S., Lacroix C., Monsempe C., Simon S.,
RA   Harris B., Atkin R., Doggett J., Mayes R., Keating L., Wheeler P.R.,
RA   Parkhill J., Barrell B.G., Cole S.T., Gordon S.V., Hewinson R.G.;
RT   "The complete genome sequence of Mycobacterium bovis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:7877-7882(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME
RP   REANNOTATION.
RC   STRAIN=ATCC BAA-935 / AF2122/97;
RX   PubMed=28385856; DOI=10.1128/genomeA.00157-17;
RA   Malone K.M., Farrell D., Stuber T.P., Schubert O.T., Aebersold R.,
RA   Robbe-Austerman S., Gordon S.V.;
RT   "Updated reference genome sequence and annotation of Mycobacterium
RT   bovis AF2122/97.";
RL   Genome Announc. 5:E00157-E00157(2017).
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; LT708304; SIT99508.1; -; Genomic_DNA.
DR   RefSeq; NP_854567.1; NC_002945.3.
DR   RefSeq; WP_003404631.1; NC_002945.4.
DR   ProteinModelPortal; P65529; -.
DR   SMR; P65529; -.
DR   PRIDE; P65529; -.
DR   EnsemblBacteria; CDO42154; CDO42154; Mb0910.
DR   PATRIC; fig|233413.5.peg.990; -.
DR   HOGENOM; HOG000249250; -.
DR   OMA; VNCIHPS; -.
DR   BioCyc; MBOV233413:G1GT4-929-MONOMER; -.
DR   Proteomes; UP000001419; 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; Repeat;
KW   Transport.
FT   CHAIN         1    575       Probable ferredoxin/ferredoxin--NADP
FT                                reductase.
FT                                /FTId=PRO_0000167675.
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     463    465       FAD. {ECO:0000250}.
FT   REGION      115    575       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     456    456       FAD; via amide nitrogen. {ECO:0000250}.
FT   BINDING     463    463       NADP; via amide nitrogen. {ECO:0000250}.
SQ   SEQUENCE   575 AA;  61337 MW;  170C58599872A810 CRC64;
     MPHVITQSCC NDASCVFACP VNCIHPTPDE PGFATSEMLY IDPVACVDCG ACVTACPVSA
     IAPNTRLDFE QLPFVEINAS YYPKRPAGVK LAPTSKLAPV TPAAEVRVRR QPLTVAVVGS
     GPAAMYAADE LLVQQGVQVN VFEKLPTPYG LVRSGVAPDH QNTKRVTRLF DRIAGHRRFR
     FYLNVEIGKH LGHAELLAHH HAVLYAVGAP DDRRLTIDGM GLPGTGTATE LVAWLNGHPD
     FNDLPVDLSH ERVVIIGNGN VALDVARVLA ADPHELAATD IADHALSALR NSAVREVVVA
     ARRGPAHSAF TLPELIGLTA GADVVLDPGD HQRVLDDLAI VADPLTRNKL EILSTLGDGS
     APARRVGRPR IRLAYRLTPR RVLGQRRAGG VQFSVTGTDE LRQLDAGLVL TSIGYRGKPI
     PDLPFDEQAA LVPNDGGRVI DPGTGEPVPG AYVAGWIKRG PTGFIGTNKS CSMQTVQALV
     ADFNDGRLTD PVATPTALDQ LVQARQPQAI GCAGWRAIDA AEIARGSADG RVRNKFTDVA
     EMLAAATSAP KEPLRRRVLA RLRDLGQPIV LTVPL
//
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