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Database: UniProt
Entry: A0A0Q6RGA7_9MICO
LinkDB: A0A0Q6RGA7_9MICO
Original site: A0A0Q6RGA7_9MICO 
ID   A0A0Q6RGA7_9MICO        Unreviewed;       449 AA.
AC   A0A0Q6RGA7;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 28.
DE   RecName: Full=ferredoxin--NADP(+) reductase {ECO:0000256|ARBA:ARBA00013223};
DE            EC=1.18.1.2 {ECO:0000256|ARBA:ARBA00013223};
GN   ORFNames=ASC54_01565 {ECO:0000313|EMBL:KQV25708.1};
OS   Yonghaparkia sp. Root332.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Microcella.
OX   NCBI_TaxID=1736516 {ECO:0000313|EMBL:KQV25708.1, ECO:0000313|Proteomes:UP000051768};
RN   [1] {ECO:0000313|EMBL:KQV25708.1, ECO:0000313|Proteomes:UP000051768}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root332 {ECO:0000313|EMBL:KQV25708.1,
RC   ECO:0000313|Proteomes:UP000051768};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQV25708.1, ECO:0000313|Proteomes:UP000051768}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root332 {ECO:0000313|EMBL:KQV25708.1,
RC   ECO:0000313|Proteomes:UP000051768};
RA   Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-2015) 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         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:KQV25708.1}.
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DR   EMBL; LMCX01000001; KQV25708.1; -; Genomic_DNA.
DR   RefSeq; WP_055896275.1; NZ_LMCX01000001.1.
DR   AlphaFoldDB; A0A0Q6RGA7; -.
DR   STRING; 1736516.ASC54_01565; -.
DR   OrthoDB; 289202at2; -.
DR   Proteomes; UP000051768; 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; 2.
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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000051768}.
FT   DOMAIN          5..165
FT                   /note="FAD/NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF07992"
FT   BINDING         14
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000362-1"
FT   BINDING         45
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000362-1"
FT   BINDING         151..154
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000362-2"
FT   BINDING         195..196
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000362-2"
FT   BINDING         207
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000362-2"
FT   BINDING         358
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000362-1"
FT   BINDING         365..367
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000362-1"
FT   BINDING         365
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000362-2"
SQ   SEQUENCE   449 AA;  49441 MW;  B28723FFFB986EEF CRC64;
     MTKLRLAIVG AGPAGIYAAD ILLKHERSFE VSIDLFDQLP APYGLVRYGV APDHPRIKGI
     INALRDVLDS GDIRIFGNVR YGTDITLDDL KRHYNAVIFA TGAVRDAELS IPGIDLEGSY
     GAADFVSWYD GHPDVPREWP LTAQSVAVIG NGNVALDVAR VLAKHPEDLL PTEIPDNVHA
     GLEASPVTDV HVFGRRGPMQ VKFTPLELRE LGELRDVDMI VHDEDFEYDD AARAAIASNK
     QLFVIDKVFS QWRARETGQA SRRLHLHFYA KPVEVLGEDG RVVGFRYERT RPDGAGGVVG
     TGELREVPVQ AVYRAVGYFG SPLDGIPFDD RHGVIPNHEG RVLGDDNAVL PGVYATGWIK
     RGPVGLIGHT KSDAMETIQH VLNGQAGWWS PSEPDEGAVV ELLRSRGVLY TDLDGWRRLD
     AHEQELGAAR GRARIKVVPR DEMVRISRD
//
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