ID A0A0F0LAV2_9MICO Unreviewed; 457 AA.
AC A0A0F0LAV2;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 24-JAN-2024, entry version 33.
DE RecName: Full=ferredoxin--NADP(+) reductase {ECO:0000256|ARBA:ARBA00013223};
DE EC=1.18.1.2 {ECO:0000256|ARBA:ARBA00013223};
GN Name=fprA_2 {ECO:0000313|EMBL:KJL29799.1};
GN ORFNames=RS83_01369 {ECO:0000313|EMBL:KJL29799.1};
OS Microbacterium oxydans.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Microbacterium.
OX NCBI_TaxID=82380 {ECO:0000313|EMBL:KJL29799.1, ECO:0000313|Proteomes:UP000033640};
RN [1] {ECO:0000313|EMBL:KJL29799.1, ECO:0000313|Proteomes:UP000033640}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BEL4b {ECO:0000313|EMBL:KJL29799.1,
RC ECO:0000313|Proteomes:UP000033640};
RA Corretto E.;
RT "Draft genome sequences of ten Microbacterium spp. with emphasis on heavy
RT metal contaminated environments.";
RL Submitted (FEB-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:KJL29799.1}.
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DR EMBL; JYIW01000022; KJL29799.1; -; Genomic_DNA.
DR RefSeq; WP_045278765.1; NZ_JYIW01000022.1.
DR AlphaFoldDB; A0A0F0LAV2; -.
DR PATRIC; fig|82380.11.peg.1404; -.
DR OrthoDB; 289202at2; -.
DR Proteomes; UP000033640; Unassembled WGS sequence.
DR GO; GO:0004324; F:ferredoxin-NADP+ reductase activity; IEA:UniProtKB-EC.
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 ECO:0000313|EMBL:KJL29799.1}.
FT DOMAIN 5..175
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 37
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 365
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000362-1"
FT BINDING 372..374
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000362-1"
FT BINDING 372
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR000362-2"
SQ SEQUENCE 457 AA; 50632 MW; 04C08E67189133DE CRC64;
MTKLRLAIVG AGPAGIYAAD ILLKAERKFD VSIDLFEQLP APYGLVRYGV APDHPRIKGI
IGALRDVLDR GDIRLFGNVR FGEDITLDDL KKHYNAVIFA TGAIRDTSLD LPGIDAVASY
GAADYVSWFD GHPDVPREWP LDAASVGVLG NGNVALDVAR MLAKHAEDLL VTEVPANVYE
GLKASEITDV HVFGRRGPAQ VKFTPLELRE LGELRDVDMV VYDEDFDYDD ASKDAVASNK
QVMVIDRVLQ SWRKRDSVNN AGGTASRRLH LHFWARPVEV RKDESGRVAA LVYERTKPDG
QGGAVGTGEL REVPLQALYR AIGYFGSPLP DVPFDKKHGV IPNREGQVLA KDSNQQLPGV
YATGWIKRGP VGLIGHTKSD AMETVRHIIN DQGSWWHPED PSEQAIVDLL QERGVKWTDL
DGWHRLDEHE ISLGAPDERA RVKVVPRDEM VRVSRRE
//
