ID E2PWZ8_STRCL Unreviewed; 573 AA.
AC E2PWZ8;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE SubName: Full=Putative secreted FAD-linked oxidase {ECO:0000313|EMBL:EFG10075.1};
GN ORFNames=SCLAV_5002 {ECO:0000313|EMBL:EFG10075.1};
OS Streptomyces clavuligerus.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1901 {ECO:0000313|EMBL:EFG10075.1, ECO:0000313|Proteomes:UP000002357};
RN [1] {ECO:0000313|EMBL:EFG10075.1, ECO:0000313|Proteomes:UP000002357}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27064 / DSM 738 / JCM 4710 / NBRC 13307 / NCIMB 12785 /
RC NRRL 3585 / VKM Ac-602 {ECO:0000313|Proteomes:UP000002357};
RX PubMed=20624727; DOI=10.1093/gbe/evq013;
RA Medema M.H., Trefzer A., Kovalchuk A., van den Berg M., Mueller U.,
RA Heijne W., Wu L., Alam M.T., Ronning C.M., Nierman W.C., Bovenberg R.A.L.,
RA Breitling R., Takano E.;
RT "The sequence of a 1.8-mb bacterial linear plasmid reveals a rich
RT evolutionary reservoir of secondary metabolic pathways.";
RL Genome Biol. Evol. 2:212-224(2010).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- SIMILARITY: Belongs to the oxygen-dependent FAD-linked oxidoreductase
CC family. {ECO:0000256|ARBA:ARBA00005466}.
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DR EMBL; CM000913; EFG10075.1; -; Genomic_DNA.
DR RefSeq; WP_003962313.1; NZ_WMCC01000455.1.
DR AlphaFoldDB; E2PWZ8; -.
DR STRING; 1901.BB341_03945; -.
DR GeneID; 61468937; -.
DR KEGG; sclf:BB341_03945; -.
DR eggNOG; COG0277; Bacteria.
DR OrthoDB; 545125at2; -.
DR Proteomes; UP000002357; Chromosome.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR Gene3D; 3.30.465.10; -; 1.
DR Gene3D; 3.40.462.20; -; 1.
DR InterPro; IPR012951; BBE.
DR InterPro; IPR016166; FAD-bd_PCMH.
DR InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR InterPro; IPR016169; FAD-bd_PCMH_sub2.
DR InterPro; IPR006094; Oxid_FAD_bind_N.
DR InterPro; IPR006311; TAT_signal.
DR PANTHER; PTHR42973; BINDING OXIDOREDUCTASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_1G17690)-RELATED; 1.
DR PANTHER; PTHR42973:SF39; FAD-BINDING PCMH-TYPE DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF08031; BBE; 1.
DR Pfam; PF01565; FAD_binding_4; 1.
DR SUPFAM; SSF56176; FAD-binding/transporter-associated domain-like; 1.
DR PROSITE; PS51387; FAD_PCMH; 1.
DR PROSITE; PS51318; TAT; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000002357};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..37
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 38..573
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5038452550"
FT DOMAIN 80..270
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 573 AA; 62020 MW; CD61CD0E233F48FE CRC64;
MSEKNPHRGD VGRRSVLTGA AAVAGGAALS TALPAGAAQA APKAAAATAG TRAITVPDVI
NVDRGDRRFP DLVRGNNQRW VANPDRVVLV TNPHQAARVV QETVSAGKRF TVRSGGHCYE
DFVYSKDVQV VIDLSNMNKV GFDPAMDAFE VQAGASNFDV YETLYKLYGV SIPAGTCGTV
GAGGHIMGGG YGLLSRLHGL TVDYLHAVEV VTVDTNGNAT ARIARRSDAF PKPGDPTPDP
KLGHLYWAHT GGGGGNFGLL TRYWLRIPDA TGGPANLLPK PPSEVFVQAL AWKWDKITQT
DFVQLVANFG TWHEKNSASN SPYNSLCGLL KLNNRAHGEI GLLTQMSADE PNARELLAAY
QAEMSKGIGV APTAMTLPMG EHAALPGFKE PRRLPWFHAT DALSGGTAGK YGKYKSSYSP
KGFSEFQIRA MYTHLTNGYD NGDALLQIDS YGGRINDVAA DATAVPQRSS VLKSQFQTYW
LQPGEEARHV KWIRDFYEAV YAQTGGVPVP NEFNDGCYVN YPDVDLGDPA RNTSTTTWQT
LYYKNNYRRL QLAKALWDPN NHFRHAQSIT GKA
//
