ID A0A132PNQ0_9MYCO Unreviewed; 439 AA.
AC A0A132PNQ0;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=ferredoxin--NADP(+) reductase {ECO:0000256|ARBA:ARBA00013223};
DE EC=1.18.1.2 {ECO:0000256|ARBA:ARBA00013223};
GN ORFNames=AFM11_11375 {ECO:0000313|EMBL:KWX23969.1};
OS Mycolicibacterium wolinskyi.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=59750 {ECO:0000313|EMBL:KWX23969.1, ECO:0000313|Proteomes:UP000070612};
RN [1] {ECO:0000313|EMBL:KWX23969.1, ECO:0000313|Proteomes:UP000070612}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CDC_01 {ECO:0000313|EMBL:KWX23969.1,
RC ECO:0000313|Proteomes:UP000070612};
RA de Man T.J., Perry K.A., Coulliette A.D., Jensen B., Toney N.C.,
RA Limbago B.M., Noble-Wang J.;
RT "A draft genome sequence of Mycobacterium wolinskyi.";
RL Submitted (JUL-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 -!- 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:KWX23969.1}.
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DR EMBL; LGTW01000006; KWX23969.1; -; Genomic_DNA.
DR RefSeq; WP_067848199.1; NZ_LGTW01000006.1.
DR AlphaFoldDB; A0A132PNQ0; -.
DR STRING; 59750.AWC31_30520; -.
DR PATRIC; fig|59750.3.peg.6352; -.
DR Proteomes; UP000070612; 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 PANTHER; PTHR11938; FAD NADPH DEHYDROGENASE/OXIDOREDUCTASE; 1.
DR PANTHER; PTHR11938:SF91; NADPH:ADRENODOXIN OXIDOREDUCTASE, MITOCHONDRIAL; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR PRINTS; PR00419; ADXRDTASE.
DR SUPFAM; SSF51971; Nucleotide-binding domain; 1.
PE 4: Predicted;
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW NADP {ECO:0000256|ARBA:ARBA00022857};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000070612}.
FT DOMAIN 21..182
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
SQ SEQUENCE 439 AA; 47343 MW; 8A3C7FF5DCB9DAF1 CRC64;
MYDPNLVAAP ASASNPLRPA IAVVGSGPSG CYVAQFLAKQ WADADITIFE SLPAPYGLIR
YGVAADHQGA KGVARQFDRM FTKGSVRFAG NVSVGRDIDF DLLAGSFDIV VLATGLPEDR
PLGIPQEPGT RVIGAGALLR ALNGFPSKTL PQDATGRHIP LGRRLAVVGM GNVAVDVIRL
LSKDRDGFVG SDIDDELLRE LRPAAPETID VISRSAVTDA KCDTAMLREV VSLSNIDLEV
TGLHEHDSGP TADLLRPFAC SPAAAPGFDT HRTRVRLHFG AVPELIENSD GCTLLRARNR
YGDHRPVDFA VDTLITAVGF TCGPSDDRCC PSQAWAGAHV YRVGWLSRGA KGTIPENRKD
AQRIVGEIVK DAESRRIPLG RPGFRAVEAL VGDRVVSFAD WQRIEAYERR SAHPDRCRRK
VVDLDKMIEI ATAPVTSNL
//
