ID A0A2Z4V2K4_9ACTN Unreviewed; 310 AA.
AC A0A2Z4V2K4;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=Oxidoreductase {ECO:0008006|Google:ProtNLM};
GN ORFNames=DRB96_26670 {ECO:0000313|EMBL:AWZ15246.1};
OS Streptomyces sp. ICC1.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=2099583 {ECO:0000313|EMBL:AWZ15246.1, ECO:0000313|Proteomes:UP000250268};
RN [1] {ECO:0000313|EMBL:AWZ15246.1, ECO:0000313|Proteomes:UP000250268}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ICC1 {ECO:0000313|EMBL:AWZ15246.1,
RC ECO:0000313|Proteomes:UP000250268};
RA Gosse J.;
RT "Whole genome sequencing and metabolomic study of cave Streptomyces
RT isolates ICC1 and ICC4.";
RL Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP030287; AWZ15246.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2Z4V2K4; -.
DR Proteomes; UP000250268; Chromosome.
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 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; 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 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000250268}.
FT DOMAIN 1..98
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT DOMAIN 223..310
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
SQ SEQUENCE 310 AA; 32614 MW; 94F2A6C5CF1409D4 CRC64;
MRAAVVRAAS ALTPTVTRYW LDRAPGAEPL PAAVPGQHVT LRVGPRLKTF TLLSAGAEGY
ELAVRNRHRG DQADRLSPRL HVGAPLRVSA PGGRFTAESA APFTHFLAAG VGVNPVLAVL
AGGRLRDWQL VYVDRGAREF PFLGRLRELA REQNGSIVTL DTAAAGRPDW AEVVAGTPAG
AVIGACGPAA MVAQVRDAVA GAPEARTLVN DGAADGGCED VAPSVEVECA KTGITFETAQ
HQPLLDALHR NGVPVPSSCR QGICGTCEVE VRTGRIDHRD EVLTDQEKAE SSYMIPCVSK
SIGTRLVLNV
//
