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Database: UniProt
Entry: B8GPY9_THISH
LinkDB: B8GPY9_THISH
Original site: B8GPY9_THISH 
ID   B8GPY9_THISH            Unreviewed;       246 AA.
AC   B8GPY9;
DT   03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   03-MAR-2009, sequence version 1.
DT   27-MAR-2024, entry version 73.
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   OrderedLocusNames=Tgr7_3067 {ECO:0000313|EMBL:ACL74136.1};
OS   Thioalkalivibrio sulfidiphilus (strain HL-EbGR7).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales;
OC   Ectothiorhodospiraceae; Thioalkalivibrio.
OX   NCBI_TaxID=396588 {ECO:0000313|EMBL:ACL74136.1, ECO:0000313|Proteomes:UP000002383};
RN   [1] {ECO:0000313|EMBL:ACL74136.1, ECO:0000313|Proteomes:UP000002383}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HL-EbGR7 {ECO:0000313|EMBL:ACL74136.1,
RC   ECO:0000313|Proteomes:UP000002383};
RX   PubMed=21475584;
RA   Muyzer G., Sorokin D.Y., Mavromatis K., Lapidus A., Clum A., Ivanova N.,
RA   Pati A., d'Haeseleer P., Woyke T., Kyrpides N.C.;
RT   "Complete genome sequence of 'Thioalkalivibrio sulfidophilus' HL-EbGr7.";
RL   Stand. Genomic Sci. 4:23-35(2011).
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}.
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DR   EMBL; CP001339; ACL74136.1; -; Genomic_DNA.
DR   RefSeq; WP_012639598.1; NC_011901.1.
DR   AlphaFoldDB; B8GPY9; -.
DR   STRING; 396588.Tgr7_3067; -.
DR   KEGG; tgr:Tgr7_3067; -.
DR   eggNOG; COG1018; Bacteria.
DR   HOGENOM; CLU_003827_3_0_6; -.
DR   OrthoDB; 9784483at2; -.
DR   Proteomes; UP000002383; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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; 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   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   FAD {ECO:0000256|ARBA:ARBA00022827};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   NADP {ECO:0000256|ARBA:ARBA00022857};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002383}.
FT   DOMAIN          2..101
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51384"
FT   REGION          227..246
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   246 AA;  27934 MW;  07BE92DE885C2C51 CRC64;
     MAAWLEGTVV ERKRWTERLH SLRLEAPVEP FQAGQFNRLA LDIDGERVGR PYSYVNAPGQ
     SPLDFYFITV PDGPLSNRLA ALNPGDRVQL MSRAQGFFTL SELPDAHILW LMATGTAIGP
     YLSMLRTETP WQRFERIVLI HAVRQAEELT YRDVIDGFRD FGRQFQFVPF VSRERHPGAM
     SGRVPAAIGD GSLERRVDLP LSADAAQVML CGNPDMVRDT TEALKARGMK KNRRREPGHI
     TTEHYW
//
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