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 02-SEP-2026, entry version 117. 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; Bacillati; Actinomycetota; Actinomycetes; Mycobacteriales; OC Mycobacteriaceae; 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., Pryor M., RA Duthoy S., Grondin S., Lacroix C., Monsempe C., Simon S., Harris B., RA Atkin R., Doggett J., Mayes R., Keating L., Wheeler P.R., Parkhill J., RA 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 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 bovis RT AF2122/97."; RL Genome Announc. 5:E00157-E00157(2017). CC -!- CATALYTIC ACTIVITY: CC Reaction=2 reduced [2Fe-2S]-[ferredoxin] + NADP(+) + H(+) = 2 oxidized CC [2Fe-2S]-[ferredoxin] + NADPH; 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; LT708304; SIT99508.1; -; Genomic_DNA. DR RefSeq; WP_003404631.1; NC_002945.4. DR AlphaFoldDB; P65529; -. DR SMR; P65529; -. DR GeneID; 45424850; -. DR KEGG; mbo:BQ2027_MB0910; -. DR PATRIC; fig|233413.5.peg.990; -. DR Proteomes; UP000001419; Chromosome. DR GO; GO:0004324; F:ferredoxin-NADP+ reductase activity; IEA:UniProtKB-EC. DR CDD; cd04410; DMSOR_beta-like; 1. DR FunFam; 3.50.50.60:FF:000229; NADPH:adrenodoxin oxidoreductase, mitochondrial; 1. DR Gene3D; 3.30.70.20; -; 1. DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1. DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 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; IPR055275; Ferredox_Rdtase. DR PANTHER; PTHR48467; GLUTAMATE SYNTHASE 1 [NADH], CHLOROPLASTIC-LIKE; 1. DR PANTHER; PTHR48467:SF1; GLUTAMATE SYNTHASE 1 [NADH], CHLOROPLASTIC-LIKE; 1. DR Pfam; PF00037; Fer4; 1. DR Pfam; PF07992; Pyr_redox_2; 1. DR PRINTS; PR00419; ADXRDTASE. DR SUPFAM; SSF54862; 4Fe-4S ferredoxins; 1. DR SUPFAM; SSF51971; Nucleotide-binding domain; 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..575 FT /note="Probable ferredoxin/ferredoxin--NADP reductase" FT /id="PRO_0000167675" 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..575 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 456 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000250" FT BINDING 463..465 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000250" FT BINDING 463 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="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 //