ID A0A1A0UGL2_9MYCO Unreviewed; 565 AA.
AC A0A1A0UGL2;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=ferredoxin--NADP(+) reductase {ECO:0000256|ARBA:ARBA00013223};
DE EC=1.18.1.2 {ECO:0000256|ARBA:ARBA00013223};
GN ORFNames=A5758_04065 {ECO:0000313|EMBL:OBB69964.1};
OS Mycobacterium sp. 852014-50255_SCH5639931.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=1834112 {ECO:0000313|EMBL:OBB69964.1, ECO:0000313|Proteomes:UP000092113};
RN [1] {ECO:0000313|EMBL:OBB69964.1, ECO:0000313|Proteomes:UP000092113}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=852014-50255_SCH5639931 {ECO:0000313|EMBL:OBB69964.1,
RC ECO:0000313|Proteomes:UP000092113};
RA Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL Submitted (JUN-2016) 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:OBB69964.1}.
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DR EMBL; LZSV01000002; OBB69964.1; -; Genomic_DNA.
DR RefSeq; WP_067735679.1; NZ_LZSV01000002.1.
DR AlphaFoldDB; A0A1A0UGL2; -.
DR STRING; 1834112.A5758_04065; -.
DR OrthoDB; 289202at2; -.
DR Proteomes; UP000092113; Unassembled WGS sequence.
DR GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.30.70.20; -; 1.
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; IPR017896; 4Fe4S_Fe-S-bd.
DR InterPro; IPR017900; 4Fe4S_Fe_S_CS.
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; PF00037; Fer4; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR PRINTS; PR00419; ADXRDTASE.
DR SUPFAM; SSF54862; 4Fe-4S ferredoxins; 1.
DR SUPFAM; SSF51971; Nucleotide-binding domain; 1.
DR PROSITE; PS00198; 4FE4S_FER_1; 1.
DR PROSITE; PS51379; 4FE4S_FER_2; 2.
PE 4: Predicted;
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW NADP {ECO:0000256|ARBA:ARBA00022857};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT DOMAIN 1..29
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 37..66
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT REGION 546..565
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 565 AA; 59849 MW; 7DEE286889931C70 CRC64;
MPHVITQSCC NDGSCVFACP VNCIHPTPDE PGFATSEMLY IDPVACVDCG ACVSACPVGA
IAPDGRLDTK QLPFVEINAS FYPERPEGEK VPPTSKLAPV IPAAQVRARR RPLTVAIVGS
GPAAMYAADE LLTQHGVQVN VFEKLPTPYG LVRAGVAPDH QNTKRVTRLF DRVTGHRRFR
FYLNVEVGRH LSHADLLAHH HAVMYAVGAP DDRRLEIEGM GLPGTGTATE LVAWINGHPD
FADLPVDLSH ERVVIVGNGN VALDVARVLT ANPDDLARTD ISDRALAAFR ASAVREVVIA
ARRGPAQSAF TLPELVGLTG SSDVVLSAAD HELVAADLAA ATDGLTRRKL EILSTLGDDS
GPPRNSGGPR IRLAYRLTPN RVLGDERVTG VEFAVTGTGE LCRLDAGLLL TSIGYRGMPI
RDLPFDQATA VVPNDGGRVV DPDYGAPVSG AYVAGWIKRG PSGFIGTNKS CSLQTVQALV
ADFNAGHLSD PVAEPEALAK LVHARQPHAV DARGWRAIDA AEIARGSADG RPRNKFTEVA
DMLAAAAAAE PAPPPRRGLL DRLLG
//
