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Database: UniProt
Entry: N9T6P1_9GAMM
LinkDB: N9T6P1_9GAMM
Original site: N9T6P1_9GAMM 
ID   N9T6P1_9GAMM            Unreviewed;       259 AA.
AC   N9T6P1;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   24-JAN-2024, entry version 34.
DE   RecName: Full=ferredoxin--NADP(+) reductase {ECO:0000256|ARBA:ARBA00013223};
DE            EC=1.18.1.2 {ECO:0000256|ARBA:ARBA00013223};
GN   ORFNames=F884_02252 {ECO:0000313|EMBL:ENX62786.1};
OS   Acinetobacter sp. CIP 102143.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Acinetobacter.
OX   NCBI_TaxID=1144666 {ECO:0000313|EMBL:ENX62786.1, ECO:0000313|Proteomes:UP000018424};
RN   [1] {ECO:0000313|EMBL:ENX62786.1, ECO:0000313|Proteomes:UP000018424}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CIP 102143 {ECO:0000313|EMBL:ENX62786.1,
RC   ECO:0000313|Proteomes:UP000018424};
RG   The Broad Institute Genome Sequencing Platform;
RG   The Broad Institute Genome Sequencing Center for Infectious Disease;
RA   Cerqueira G., Feldgarden M., Courvalin P., Perichon B.,
RA   Grillot-Courvalin C., Clermont D., Rocha E., Yoon E.-J., Nemec A.,
RA   Walker B., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA   Abouelleil A., Alvarado L., Arachchi H.M., Berlin A.M., Chapman S.B.,
RA   Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C.,
RA   Imamovic A., Larimer J., McCowan C., Murphy C., Neiman D., Pearson M.,
RA   Priest M., Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J.,
RA   Nusbaum C., Birren B.;
RT   "The Genome Sequence of Acinetobacter sp. CIP 102143.";
RL   Submitted (FEB-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+) + NADP(+) + 2 reduced [2Fe-2S]-[ferredoxin] = NADPH + 2
CC         oxidized [2Fe-2S]-[ferredoxin]; 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         Evidence={ECO:0000256|ARBA:ARBA00001005};
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:ENX62786.1}.
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DR   EMBL; APSE01000080; ENX62786.1; -; Genomic_DNA.
DR   RefSeq; WP_004679719.1; NZ_KB850238.1.
DR   AlphaFoldDB; N9T6P1; -.
DR   PATRIC; fig|1144666.3.peg.2211; -.
DR   HOGENOM; CLU_003827_3_0_6; -.
DR   Proteomes; UP000018424; 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}.
FT   DOMAIN          1..102
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51384"
SQ   SEQUENCE   259 AA;  29397 MW;  D9EF9A138E3E7E77 CRC64;
     MAAFNVERIT HVHHWNDTLF SFKTTRDTSL RFKNGQFVMI GLEVNGKPLM RAYSIASANY
     EEELEFFSIK VQDGPLTSIL QKVQVGDEIL ISKKPTGTLV HDDLLPGKNL YLLSSGTGLA
     PFLSLLRDPE TYEKFEKVIM VHGTRYVSEL AYQDLILNEL PNNEFFEELG IKDKLVYYPT
     VTREPFHTQG RVTTAIETGE LFEKIGLPRF NRETDRAMLC GSPAFLKDVA ALLDQHGLVE
     SPRMGVMGDY VIERAFVEK
//
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