ID A0A1A2L4Y3_9MYCO Unreviewed; 360 AA.
AC A0A1A2L4Y3;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Ferredoxin reductase {ECO:0000313|EMBL:OBG85629.1};
GN ORFNames=A5699_23865 {ECO:0000313|EMBL:OBG85629.1};
OS Mycobacterium sp. E802.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=1834152 {ECO:0000313|EMBL:OBG85629.1, ECO:0000313|Proteomes:UP000092062};
RN [1] {ECO:0000313|EMBL:OBG85629.1, ECO:0000313|Proteomes:UP000092062}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=E802 {ECO:0000313|EMBL:OBG85629.1,
RC ECO:0000313|Proteomes:UP000092062};
RA Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
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:OBG85629.1}.
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DR EMBL; LZJD01000082; OBG85629.1; -; Genomic_DNA.
DR RefSeq; WP_067769652.1; NZ_LZJD01000082.1.
DR AlphaFoldDB; A0A1A2L4Y3; -.
DR Proteomes; UP000092062; Unassembled WGS sequence.
DR GO; GO:0051537; F:2 iron, 2 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:InterPro.
DR CDD; cd00207; fer2; 1.
DR CDD; cd06216; FNR_iron_sulfur_binding_2; 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; 2.40.30.10; 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; IPR001433; OxRdtase_FAD/NAD-bd.
DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR PANTHER; PTHR47354; NADH OXIDOREDUCTASE HCR; 1.
DR PANTHER; PTHR47354:SF3; OXIDOREDUCTASE; 1.
DR Pfam; PF00970; FAD_binding_6; 1.
DR Pfam; PF00111; Fer2; 1.
DR Pfam; PF00175; NAD_binding_1; 1.
DR PRINTS; PR00410; PHEHYDRXLASE.
DR SUPFAM; SSF54292; 2Fe-2S ferredoxin-like; 1.
DR SUPFAM; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1.
DR SUPFAM; SSF63380; Riboflavin synthase domain-like; 1.
DR PROSITE; PS51384; FAD_FR; 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}.
FT DOMAIN 46..147
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
SQ SEQUENCE 360 AA; 38003 MW; 24D987E338148D04 CRC64;
MFTQTMAEGV GRRLLAGPRL SALANLLTGP HGVDRYTELV EPTWTRGEAR AKVVAVRRQT
SRSVTLTLEP NAAFAGFRAG QHINLSVEIN GRRLTRCYSP ANAEGARHLE LTIGRHDGGL
VSNYLCDHAY PGMVLGLDSV GGDFVLPEVR PQRILFVSGG SGITPVLSML RTLRAQAFTG
EIAFVHYARS ADEACYRTEL AGMFGVRVLH GFTRDGGGDL DGHFGPAHLA AAFPDATPDA
VFVCGPPALV DTVREHCPGA HSESFVPPTF AVSGEATGGT ITFTDSSVTV TDDGQTLLAQ
AEAAGLTPES GCRMGICHSC TRLKSRGAVR NLITGAVSTA DCEDIQICVT APVGDVDIDL
//
