ID H0A925_9PROT Unreviewed; 321 AA.
AC H0A925;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=ferredoxin--NADP(+) reductase {ECO:0000256|ARBA:ARBA00013223};
DE EC=1.18.1.2 {ECO:0000256|ARBA:ARBA00013223};
DE Flags: Fragment;
GN ORFNames=HMPREF9946_05336 {ECO:0000313|EMBL:EHL95102.1};
OS Acetobacteraceae bacterium AT-5844.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae.
OX NCBI_TaxID=1054213 {ECO:0000313|EMBL:EHL95102.1, ECO:0000313|Proteomes:UP000003292};
RN [1] {ECO:0000313|EMBL:EHL95102.1, ECO:0000313|Proteomes:UP000003292}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AT-5844 {ECO:0000313|Proteomes:UP000003292};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Hou S., Chen J., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Zhang X., Suruliraj S., Warren W.,
RA Chinwalla A., Mardis E.R., Wilson R.K.;
RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EHL95102.1}.
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DR EMBL; AGEZ01000243; EHL95102.1; -; Genomic_DNA.
DR AlphaFoldDB; H0A925; -.
DR STRING; 1054213.HMPREF9946_05336; -.
DR PATRIC; fig|1054213.3.peg.4854; -.
DR eggNOG; COG0543; Bacteria.
DR HOGENOM; CLU_864653_0_0_5; -.
DR Proteomes; UP000003292; Unassembled WGS sequence.
DR GO; GO:0004324; F:ferredoxin-NADP+ reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR CDD; cd06195; FNR1; 1.
DR Gene3D; 3.40.50.80; Nucleotide-binding domain of ferredoxin-NADP reductase (FNR) module; 1.
DR Gene3D; 2.40.30.10; Translation factors; 1.
DR InterPro; IPR008333; Cbr1-like_FAD-bd_dom.
DR InterPro; IPR017927; FAD-bd_FR_type.
DR InterPro; IPR001709; Flavoprot_Pyr_Nucl_cyt_Rdtase.
DR InterPro; IPR033892; FNR_bac.
DR InterPro; IPR039261; FNR_nucleotide-bd.
DR InterPro; IPR001433; OxRdtase_FAD/NAD-bd.
DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR PANTHER; PTHR47878:SF1; FERREDOXIN--NADP(+) REDUCTASE; 1.
DR PANTHER; PTHR47878; OXIDOREDUCTASE FAD/NAD(P)-BINDING DOMAIN PROTEIN; 1.
DR Pfam; PF00970; FAD_binding_6; 1.
DR Pfam; PF00175; NAD_binding_1; 1.
DR PRINTS; PR00371; FPNCR.
DR SUPFAM; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1.
DR SUPFAM; SSF63380; Riboflavin synthase domain-like; 1.
DR PROSITE; PS51384; FAD_FR; 1.
PE 4: Predicted;
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000003292}.
FT DOMAIN 66..166
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:EHL95102.1"
SQ SEQUENCE 321 AA; 35486 MW; 4EF8700C504F50AC CRC64;
GGAAVAGAGV ALEGVLMIAK GHRNRGRMQA VPCPCLMSTH LARHVEEDHL PLMNAETRPP
LKSAHAAYFT ETVETVHHWT DRLFSFRCTR QPGLRFTAGQ FVMIGLIVEG KPLVRAYSVA
SAPYDEHLEF LSIKVQDGPL TSRLQHIRPG DEILVGKKAV GTLVPDALLP GRTLWLYGTG
TGLAPFMSLI REPEVYDRFD KVVLLHGVRE VKELAYSSYI ENELPADELL GEMVAPKLVY
YPTVTREPFR NQGRVTDLIR SGKLFTDLGL PAFTPEHDRI MLCGSPEMLA ETKGLLEGMG
FEEGANSRPG HYVIEKAFVE K
//
