ID A0A124I4X8_9ACTN Unreviewed; 523 AA.
AC A0A124I4X8;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE RecName: Full=FAD-binding PCMH-type domain-containing protein {ECO:0000259|PROSITE:PS51387};
GN ORFNames=AQJ66_07530 {ECO:0000313|EMBL:KUN88200.1};
OS Streptomyces bungoensis.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=285568 {ECO:0000313|EMBL:KUN88200.1, ECO:0000313|Proteomes:UP000053024};
RN [1] {ECO:0000313|EMBL:KUN88200.1, ECO:0000313|Proteomes:UP000053024}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 41781 {ECO:0000313|EMBL:KUN88200.1,
RC ECO:0000313|Proteomes:UP000053024};
RA Ruckert C., Winkler A., Kalinowski J., Kampfer P., Glaeser S.;
RT "Draft genome sequence of Streptomyces bungoensis DSM 41781, type strain
RT for the species Streptomyces bungoensis.";
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
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}.
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:KUN88200.1}.
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DR EMBL; LMWX01000012; KUN88200.1; -; Genomic_DNA.
DR RefSeq; WP_061918405.1; NZ_KQ948853.1.
DR AlphaFoldDB; A0A124I4X8; -.
DR STRING; 285568.AQJ66_07530; -.
DR OrthoDB; 545125at2; -.
DR Proteomes; UP000053024; Unassembled WGS sequence.
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 Gene3D; 3.30.43.10; Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase, domain 2; 1.
DR InterPro; IPR012951; BBE.
DR InterPro; IPR016166; FAD-bd_PCMH.
DR InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR InterPro; IPR016167; FAD-bd_PCMH_sub1.
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; PS51257; PROKAR_LIPOPROTEIN; 1.
DR PROSITE; PS51318; TAT; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000053024};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..523
FT /note="FAD-binding PCMH-type domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5039651616"
FT DOMAIN 89..259
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 523 AA; 54806 MW; D74DE136DF70C3B9 CRC64;
MQRRAFISGG AAALATTALA GCDSGSGASA GSSHSLSAHG TGLSGTPLKT TGQVAAANWA
ALARDLDGPL VRPGDATWKT AHQLYNTRFD GLKPAAVAYV AHVGDIRTTL AYAHAHGLRV
AIRNGGHSYA GYSSGNGRLI LDVSRLNRIR VSGGQAVVGA GSKLIDVYRG LAAKGVTIPA
GSCPTVGVSG LVLGGGHGVA SRAYGLTCDS LTRATIVTAD GTQVTADARD HADLFWALRG
AGNGNFGVVT ELHFTTHPAP QAVTAYLSWP WAKAAAVFQA WQEWGPTQPD EIWSSLHLSG
TPGGTPSVSV SCFSLGTYGE LQNAVDRLAH RAGADARYVS LRRRGYEEAM EIYAGCSSFA
DDAECHLPGS TPGRDPHGAL RRETYAARSD FFDRSLSPAG VRTLLRQIGS VRGGAGSIAF
TALGGAVNRV SPTATAFVHR RSRMLAQYIA SWGTGGSGTT AQSWLTSAHD ALRPYASGAA
YQNYTDPTLT DWRRAYYGDA ATRLGKVKKQ YDPQRFFSYQ QGL
//
