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Database: UniProt
Entry: K2JFQ9_9GAMM
LinkDB: K2JFQ9_9GAMM
Original site: K2JFQ9_9GAMM 
ID   K2JFQ9_9GAMM            Unreviewed;       245 AA.
AC   K2JFQ9;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   24-JAN-2024, entry version 44.
DE   RecName: Full=Flavodoxin/ferredoxin--NADP reductase {ECO:0000256|ARBA:ARBA00020327};
DE            EC=1.18.1.2 {ECO:0000256|ARBA:ARBA00013223};
DE            EC=1.19.1.1 {ECO:0000256|ARBA:ARBA00012872};
DE   AltName: Full=Ferredoxin (flavodoxin):NADP(+) oxidoreductase {ECO:0000256|ARBA:ARBA00030173};
DE   AltName: Full=Ferredoxin--NADP reductase {ECO:0000256|ARBA:ARBA00029856};
DE   AltName: Full=Flavodoxin--NADP reductase {ECO:0000256|ARBA:ARBA00030000};
GN   ORFNames=B3C1_15322 {ECO:0000313|EMBL:EKE69494.1};
OS   Gallaecimonas xiamenensis 3-C-1.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Gallaecimonas.
OX   NCBI_TaxID=745411 {ECO:0000313|EMBL:EKE69494.1, ECO:0000313|Proteomes:UP000006755};
RN   [1] {ECO:0000313|EMBL:EKE69494.1, ECO:0000313|Proteomes:UP000006755}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=3-C-1 {ECO:0000313|EMBL:EKE69494.1,
RC   ECO:0000313|Proteomes:UP000006755};
RX   PubMed=23209203; DOI=10.1128/JB.01854-12;
RA   Lai Q., Wang L., Wang W., Shao Z.;
RT   "Genome Sequence of Gallaecimonas xiamenensis Type Strain 3-C-1.";
RL   J. Bacteriol. 194:6937-6937(2012).
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   -!- CATALYTIC ACTIVITY:
CC       Reaction=NADP(+) + reduced [flavodoxin] = 2 H(+) + NADPH + oxidized
CC         [flavodoxin]; Xref=Rhea:RHEA:50756, Rhea:RHEA-COMP:10622, Rhea:RHEA-
CC         COMP:10623, ChEBI:CHEBI:15378, ChEBI:CHEBI:57618, ChEBI:CHEBI:57783,
CC         ChEBI:CHEBI:58210, ChEBI:CHEBI:58349; EC=1.19.1.1;
CC         Evidence={ECO:0000256|ARBA:ARBA00000579};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC   -!- SIMILARITY: Belongs to the ferredoxin--NADP reductase type 1 family.
CC       {ECO:0000256|ARBA:ARBA00008312}.
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:EKE69494.1}.
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DR   EMBL; AMRI01000024; EKE69494.1; -; Genomic_DNA.
DR   RefSeq; WP_008485941.1; NZ_AMRI01000024.1.
DR   AlphaFoldDB; K2JFQ9; -.
DR   STRING; 745411.B3C1_15322; -.
DR   PATRIC; fig|745411.4.peg.3013; -.
DR   eggNOG; COG1018; Bacteria.
DR   OrthoDB; 9784483at2; -.
DR   Proteomes; UP000006755; 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:SF2; FLAVODOXIN/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   PRINTS; PR00410; PHEHYDRXLASE.
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   3: Inferred from homology;
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006755}.
FT   DOMAIN          2..100
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51384"
SQ   SEQUENCE   245 AA;  27185 MW;  9B9B159269692E46 CRC64;
     MAQWLSAKVV ENHQWNPTLF SLRVETPPFD FVAGQFVRLA LEGPQGRAQR AYSLVNSPGS
     PYLDFLVTPV PQGKLSPQLH LLKAGDSLEV SQPASGFFVL DEVPDGKSLW LLATGTGLGP
     YLSMLGTEVP WRRFERIHLV HGVRWQQDLA YKDQIEALVH QHPQLRYQPV ITREAVPGAL
     GGRLPALIAS GELEAALGDQ LNIESQLMLC GNPDMIRDSL ATLAQKGLNK NLRRQPGHVT
     VEQYW
//
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