ID FPRA_MYCLE Reviewed; 456 AA. AC O32886; DT 11-JUL-2002, integrated into UniProtKB/Swiss-Prot. DT 01-JAN-1998, sequence version 1. DT 16-JUN-2009, entry version 51. DE RecName: Full=NADPH-ferredoxin reductase fprA; DE Short=NFR; DE EC=1.18.1.2; GN Name=fprA; OrderedLocusNames=ML0666; ORFNames=MLCB1779.25; OS Mycobacterium leprae. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Mycobacteriaceae; Mycobacterium. OX NCBI_TaxID=1769; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=TN; RX MEDLINE=21128732; 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 -!- FUNCTION: May serve as electron transfer protein and supply CC electrons to P450 systems (By similarity). CC -!- CATALYTIC ACTIVITY: 2 reduced ferredoxin + NADP(+) + H(+) = 2 CC oxidized ferredoxin + NADPH. CC -!- COFACTOR: FAD (By similarity). CC -!- SUBUNIT: Monomer (By similarity). CC -!- SIMILARITY: Belongs to the ferredoxin--NADP reductase type 1 CC family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; Z98271; CAB11006.1; -; Genomic_DNA. DR EMBL; AL583919; CAC30175.1; -; Genomic_DNA. DR PIR; T45314; T45314. DR RefSeq; NP_301540.1; -. DR HSSP; O05783; 1LQT. DR SMR; O32886; 7-456. DR GeneID; 910559; -. DR GenomeReviews; AL450380_GR; ML0666. DR KEGG; mle:ML0666; -. DR NMPDR; fig|272631.1.peg.412; -. DR Leproma; ML0666; -. DR HOGENOM; O32886; -. DR OMA; O32886; YHAVLLT. DR BioCyc; MLEP272631:ML0666-MON; -. DR BRENDA; 1.18.1.2; 808. DR GO; GO:0009055; F:electron carrier activity; IEA:InterPro. DR GO; GO:0004324; F:ferredoxin-NADP+ reductase activity; IEA:EC. DR GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW. DR InterPro; IPR000759; Adrndx_reductase. DR InterPro; IPR013027; FAD_pyr_nucl-diS_OxRdtase. DR Pfam; PF07992; Pyr_redox_2; 1. DR PRINTS; PR00419; ADXRDTASE. PE 3: Inferred from homology; KW Complete proteome; FAD; Flavoprotein; NADP; Oxidoreductase. FT CHAIN 1 456 NADPH-ferredoxin reductase fprA. FT /FTId=PRO_0000087328. FT NP_BIND 158 161 NADP (By similarity). FT NP_BIND 202 203 NADP (By similarity). FT NP_BIND 369 371 FAD (By similarity). FT BINDING 17 17 FAD; via amide nitrogen (By similarity). FT BINDING 43 43 FAD (By similarity). FT BINDING 51 51 FAD; via amide nitrogen (By similarity). FT BINDING 87 87 FAD; via amide nitrogen and carbonyl FT oxygen (By similarity). FT BINDING 113 113 NADP (By similarity). FT BINDING 214 214 NADP (By similarity). FT BINDING 362 362 FAD; via amide nitrogen (By similarity). FT BINDING 369 369 NADP; via amide nitrogen (By similarity). SQ SEQUENCE 456 AA; 49630 MW; B3506A27B4B3AC79 CRC64; MRPHHIHHIA IVGSGPSGFF AAASVLKAAD ASDEINVAVD MLEMLPTPWG LVRSGVAPDH PKIKSISKQF EKTAEDPRFR FFGNVIVGKH IEPAELAERY DAVIYAVGAQ SDRALNIPGE DLPGSIAAVD FVGWYNAHPN FHERSPDLSG SRAVVIGNGN VALDVTRILI TDPDVLAFTD IADHALESLR PRGIEEVVIV GRRGPLQTAF TTLELRELAD IEGVDVLVDP AQLEGISDEN AAAAGKTTRQ NIKVLRDYTV RTPKPGHRRI VFRFLTSPIE IKGKGKVERI VLGQNELVTD DNGRVAAKDT GVREELPAQL IVRSIGYRGV PTPGLPFDDS SVTIPNTNGR VNGSRNEYVV GWIKRGPTGV IGTNKKDSQD TVDTLMENLA GANDTEKFGA DHADRLAEWL AERQPKLVTS AHWQAIDRFE RAAGEPHGRP RVKLPNLAEL LRIGHG //