ID I4M4S3_GARVA Unreviewed; 498 AA.
AC I4M4S3;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 24-JAN-2024, entry version 42.
DE RecName: Full=ferredoxin--NADP(+) reductase {ECO:0000256|ARBA:ARBA00013223};
DE EC=1.18.1.2 {ECO:0000256|ARBA:ARBA00013223};
GN ORFNames=CGSMWGv1500E_00730 {ECO:0000313|EMBL:EIK84213.1};
OS Gardnerella vaginalis 1500E.
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Gardnerella.
OX NCBI_TaxID=698957 {ECO:0000313|EMBL:EIK84213.1, ECO:0000313|Proteomes:UP000032875};
RN [1] {ECO:0000313|EMBL:EIK84213.1, ECO:0000313|Proteomes:UP000032875}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1500E {ECO:0000313|EMBL:EIK84213.1,
RC ECO:0000313|Proteomes:UP000032875};
RX PubMed=22609915; DOI=10.1128/JB.00056-12;
RA Ahmed A., Earl J., Retchless A., Hillier S., Rabe L., Cherpes T.,
RA Powell E., Janto B., Eutsey R., Hiller N.L., Boissy R., Dahlgreen M.,
RA Hall B., Costerton J., Post J.C., Hu F., Ehrlich G.;
RT "Comparative Genomic Analyses of 17 Clinical Isolates of Gardnerella
RT vaginalis Provide Evidence of Multiple Genetically Isolated Clades
RT Consistent with Subspeciation into Genovars.";
RL J. Bacteriol. 194:3922-3937(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 -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974,
CC ECO:0000256|PIRSR:PIRSR000362-1};
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:EIK84213.1}.
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DR EMBL; ADES01000001; EIK84213.1; -; Genomic_DNA.
DR RefSeq; WP_004126661.1; NZ_ADES01000001.1.
DR AlphaFoldDB; I4M4S3; -.
DR PATRIC; fig|698957.3.peg.144; -.
DR Proteomes; UP000032875; Unassembled WGS sequence.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR023753; FAD/NAD-binding_dom.
DR InterPro; IPR021163; Ferredox_Rdtase_adrenod.
DR PANTHER; PTHR11938; FAD NADPH DEHYDROGENASE/OXIDOREDUCTASE; 1.
DR PANTHER; PTHR11938:SF91; NADPH:ADRENODOXIN OXIDOREDUCTASE, MITOCHONDRIAL; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR PIRSF; PIRSF000362; FNR; 1.
DR PRINTS; PR00419; ADXRDTASE.
DR SUPFAM; SSF51971; Nucleotide-binding domain; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|PIRSR:PIRSR000362-1};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW NADP {ECO:0000256|ARBA:ARBA00022857, ECO:0000256|PIRSR:PIRSR000362-2};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT DOMAIN 29..194
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT BINDING 38
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000362-1"
FT BINDING 69
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000362-1"
FT BINDING 77
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000362-1"
FT BINDING 228..229
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR000362-2"
FT BINDING 240
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR000362-2"
FT BINDING 405
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000362-1"
FT BINDING 412..414
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000362-1"
FT BINDING 412
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR000362-2"
SQ SEQUENCE 498 AA; 55023 MW; E690957355453473 CRC64;
MKKNNLIENV APETSQASEI SKVHAPEVRI AVIGAGPAGV YSSDIFLRQL AKRGEELGLG
TSARIDLFEK LPVPFGLVRY GVAPDHPSIK FIADALEKTL DNPNIHLYAN VEFGKDITLE
DLLARYDAVL FATGAVEDRP LRVPGADLDG VYGAAKFVEW YDGYPTSKRT WPLEAKEVAV
IGGGNVAMDV ARELLRDPDY LRAHTDIPDD VYEGLQKNQT QTLHLFIRRG VAQAKFSVQE
LREMEKLAGV QIVINEDDFE LDDETIEVAG NDKLTRQMVE ELFAIRDMAE DMEDGGNVDF
EGNPANRRYV IHFNSAPVEI LGEDGRVKAI RVERTVTSAD GTMSRTGEFE DYAVQAVYHA
IGYHPAEVAG IAYDEKRTLL ANNDGRIVTS AENGEVRERL YATGWAKRGP VGLIGSTKSD
ALLIVDRMLE DLAKSGLIAE DRNEKSIDEL LKSRGVKAID YAGWKRVDEY EREAGAKEQR
ARKKVVSSAD LIAIALDC
//
