ID A0A243S8J4_9ACTN Unreviewed; 311 AA.
AC A0A243S8J4;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=Oxidoreductase {ECO:0000313|EMBL:OUD03979.1};
GN ORFNames=CA983_06535 {ECO:0000313|EMBL:OUD03979.1};
OS Streptomyces swartbergensis.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=487165 {ECO:0000313|EMBL:OUD03979.1, ECO:0000313|Proteomes:UP000195105};
RN [1] {ECO:0000313|EMBL:OUD03979.1, ECO:0000313|Proteomes:UP000195105}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HMC13 {ECO:0000313|EMBL:OUD03979.1};
RA Le Roes-Hill M., Prins A., Durrell K.A.;
RT "Biotechnological potential of actinobacteria isolated from South African
RT environments.";
RL Submitted (MAY-2017) 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:OUD03979.1}.
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DR EMBL; NGFN01000024; OUD03979.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A243S8J4; -.
DR Proteomes; UP000195105; 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; cd06185; PDR_like; 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; IPR006058; 2Fe2S_fd_BS.
DR InterPro; IPR012675; Beta-grasp_dom_sf.
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:SF1; CARNITINE MONOOXYGENASE REDUCTASE SUBUNIT; 1.
DR PANTHER; PTHR47354; NADH OXIDOREDUCTASE HCR; 1.
DR Pfam; PF00111; Fer2; 1.
DR Pfam; PF00175; NAD_binding_1; 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; SSF63380; Riboflavin synthase domain-like; 1.
DR PROSITE; PS00197; 2FE2S_FER_1; 1.
DR PROSITE; PS51085; 2FE2S_FER_2; 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 1..105
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT DOMAIN 226..311
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
FT REGION 77..97
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 311 AA; 33547 MW; 78FCF78AC0025F1B CRC64;
MSVYEAELVV ERREFAADGV LALSLRHPLG EPLPAWEPGA HIDVVLGPGL ERQYSLCGDP
ADRSAWRIAV LREPDGRGGS AHVHEQVGQG DKVRVRGPRN NFGLEPAPRY RFVAGGIGIT
PILPMLAAAE AAGAEWTLLY GGRTRRSMAF GEELARYGDR VTIAPEDETG LLDLPSVLDD
VPEGTLVYCC GPGPLLDAVE ERCPSAVLRV ERFRPKEQET GGDTGFEVEL ARSGRTLSVG
PDVSVLDAVR AAGVEVLFSC TEGTCGTCET DVLDGTPEHR DSVLTPEERE SGETMMICVS
RCRGRRLVLD L
//
