ID A0A1H6D660_9ACTN Unreviewed; 586 AA.
AC A0A1H6D660;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Ferredoxin-NADP reductase {ECO:0000313|EMBL:SEG80820.1};
GN ORFNames=SAMN05216223_112107 {ECO:0000313|EMBL:SEG80820.1};
OS Actinacidiphila yanglinensis.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Actinacidiphila.
OX NCBI_TaxID=310779 {ECO:0000313|EMBL:SEG80820.1, ECO:0000313|Proteomes:UP000236754};
RN [1] {ECO:0000313|EMBL:SEG80820.1, ECO:0000313|Proteomes:UP000236754}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 4.2023 {ECO:0000313|EMBL:SEG80820.1,
RC ECO:0000313|Proteomes:UP000236754};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; FNVU01000012; SEG80820.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H6D660; -.
DR OrthoDB; 9801223at2; -.
DR Proteomes; UP000236754; Unassembled WGS sequence.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0030151; F:molybdenum ion binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR CDD; cd00207; fer2; 1.
DR CDD; cd06184; flavohem_like_fad_nad_binding; 1.
DR Gene3D; 3.10.20.30; -; 1.
DR Gene3D; 3.40.50.80; Nucleotide-binding domain of ferredoxin-NADP reductase (FNR) module; 1.
DR Gene3D; 2.40.33.20; PK beta-barrel domain-like; 1.
DR Gene3D; 2.40.30.10; Translation factors; 1.
DR InterPro; IPR036010; 2Fe-2S_ferredoxin-like_sf.
DR InterPro; IPR001041; 2Fe-2S_ferredoxin-type.
DR InterPro; IPR012675; Beta-grasp_dom_sf.
DR InterPro; IPR008333; Cbr1-like_FAD-bd_dom.
DR InterPro; IPR017927; FAD-bd_FR_type.
DR InterPro; IPR039261; FNR_nucleotide-bd.
DR InterPro; IPR005302; MoCF_Sase_C.
DR InterPro; IPR001433; OxRdtase_FAD/NAD-bd.
DR InterPro; IPR011037; Pyrv_Knase-like_insert_dom_sf.
DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR InterPro; IPR005163; YiiM-like_3-alpha_domain.
DR PANTHER; PTHR30212:SF2; PROTEIN YIIM; 1.
DR PANTHER; PTHR30212; UNCHARACTERIZED; 1.
DR Pfam; PF00970; FAD_binding_6; 1.
DR Pfam; PF00111; Fer2; 1.
DR Pfam; PF03473; MOSC; 1.
DR Pfam; PF00175; NAD_binding_1; 1.
DR Pfam; PF03475; YiiM_3-alpha; 1.
DR PRINTS; PR00409; PHDIOXRDTASE.
DR SUPFAM; SSF54292; 2Fe-2S ferredoxin-like; 1.
DR SUPFAM; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1.
DR SUPFAM; SSF50800; PK beta-barrel domain-like; 1.
DR SUPFAM; SSF63380; Riboflavin synthase domain-like; 1.
DR PROSITE; PS51085; 2FE2S_FER_2; 1.
DR PROSITE; PS51384; FAD_FR; 1.
DR PROSITE; PS51340; MOSC; 1.
PE 4: Predicted;
KW 2Fe-2S {ECO:0000256|ARBA:ARBA00022714};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022714};
KW Reference proteome {ECO:0000313|Proteomes:UP000236754}.
FT DOMAIN 29..164
FT /note="MOSC"
FT /evidence="ECO:0000259|PROSITE:PS51340"
FT DOMAIN 239..343
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT DOMAIN 504..586
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
SQ SEQUENCE 586 AA; 63403 MW; BD7C90DE7B2611A4 CRC64;
MATLLSVNVG MPKDVSWQGR TVRTGAWKAP VEGPRMVRRL NVEGDGQGDL AGHGGEIRAV
LVYQAQSHRY WEKQLGRDDL SFGIFGENFT VDGLPDDEVC IGDRYRIGDA EFEVTQPRVT
CYRVGMRLGE PTMASLLVAH HRPGFYLRVL TEGQVQAGDE ITLTRRGPQE LSVAETDALL
YLPDRDPDKL RRALDIPALS PGWQQSFREL VDAQQPQQEP GWPGERAGCR QTGEAAGWPG
FKSMRVARIV PETPTISSVY LDTADGSPLS EARAGQYLSL RLPVGDAAPS VRSYSLSSAP
GAGTYRISVK HEPHGKVSGY IHATLRTGDL VDVASPRGTF VLQEGTRPVV LLSAGIGATP
VLAMLHRLAD RRDPRPVWWI HTTHDRAHHV FAGESRALLE RLPHARAHVY YTSEDPRGGE
EHATRGRPTA RSLAALGIDT DADAYLCGPT AFMDALGGLL RDHGLAAERI HTEQFSALSA
INPGVTSGTA ARPHQPPGPE GTGPRITFAR SGISTPWSPA HASLLELAEA CDVPTRWSCR
TGVCHTCVTP LVEGDLTYTT PPLEPPEAGS ALICCSTPVT EVVLDL
//
