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Database: UniProt
Entry: A0A177HKF1_9ACTN
LinkDB: A0A177HKF1_9ACTN
Original site: A0A177HKF1_9ACTN 
ID   A0A177HKF1_9ACTN        Unreviewed;       420 AA.
AC   A0A177HKF1;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   SubName: Full=Flavin-dependent monooxygenase, oxygenase subunit HsaA {ECO:0000313|EMBL:OAH10678.1};
DE            EC=1.14.14.12 {ECO:0000313|EMBL:OAH10678.1};
GN   Name=hsaA_3 {ECO:0000313|EMBL:OAH10678.1};
GN   ORFNames=STSP_60000 {ECO:0000313|EMBL:OAH10678.1};
OS   Streptomyces jeddahensis.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1716141 {ECO:0000313|EMBL:OAH10678.1, ECO:0000313|Proteomes:UP000077381};
RN   [1] {ECO:0000313|EMBL:OAH10678.1, ECO:0000313|Proteomes:UP000077381}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=G25(2015) {ECO:0000313|Proteomes:UP000077381};
RA   Poehlein A., Roettig A., Hiessl S., Hauschild P., Schauer J., Madkour M.H.,
RA   Al-Ansari A.M., Almakishah N.H., Steinbuechel A., Daniel R.;
RT   "Genome sequence of Streptomyces sp. G25.";
RL   Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
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:OAH10678.1}.
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DR   EMBL; LOHS01000126; OAH10678.1; -; Genomic_DNA.
DR   RefSeq; WP_067284030.1; NZ_LOHS01000126.1.
DR   AlphaFoldDB; A0A177HKF1; -.
DR   STRING; 1716141.STSP_60000; -.
DR   PATRIC; fig|1716141.3.peg.6313; -.
DR   OrthoDB; 3404950at2; -.
DR   Proteomes; UP000077381; Unassembled WGS sequence.
DR   GO; GO:0036383; F:3-hydroxy-9,10-secoandrosta-1,3,5(10)-triene-9,17-dione monooxygenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0016627; F:oxidoreductase activity, acting on the CH-CH group of donors; IEA:InterPro.
DR   Gene3D; 1.10.540.10; Acyl-CoA dehydrogenase/oxidase, N-terminal domain; 1.
DR   Gene3D; 2.40.110.10; Butyryl-CoA Dehydrogenase, subunit A, domain 2; 1.
DR   Gene3D; 1.20.140.10; Butyryl-CoA Dehydrogenase, subunit A, domain 3; 1.
DR   InterPro; IPR013107; Acyl-CoA_DH_C.
DR   InterPro; IPR046373; Acyl-CoA_Oxase/DH_mid-dom_sf.
DR   InterPro; IPR013786; AcylCoA_DH/ox_N.
DR   InterPro; IPR037069; AcylCoA_DH/ox_N_sf.
DR   InterPro; IPR009100; AcylCoA_DH/oxidase_NM_dom_sf.
DR   Pfam; PF08028; Acyl-CoA_dh_2; 1.
DR   Pfam; PF02771; Acyl-CoA_dh_N; 1.
DR   PIRSF; PIRSF016578; HsaA; 1.
DR   SUPFAM; SSF56645; Acyl-CoA dehydrogenase NM domain-like; 1.
PE   4: Predicted;
KW   Monooxygenase {ECO:0000313|EMBL:OAH10678.1};
KW   Oxidoreductase {ECO:0000313|EMBL:OAH10678.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000077381}.
FT   DOMAIN          33..116
FT                   /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02771"
FT   DOMAIN          260..393
FT                   /note="Acyl-CoA dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08028"
SQ   SEQUENCE   420 AA;  45897 MW;  45DEDF4CBFEC039F CRC64;
     MSVADRTHIP VPEPDLTEAE LVERAVALRP VLLERQEETE RLTHYPSATH EDFLRAGFYR
     TLQPRRYGGY EFGLPTFYRV VVEISRGCPS AGWALSLVSA HVLQVASLFG EEVQTEVFGA
     DGEFRAASTV MPIGVAQPDG DDHYVVDGTW PYSSGAPYST HYVGQTLLAP EKEGDPPGPM
     LLFVAPRSAW TVLDDWHGTL GLRGTGSNSI RIDRGRIPAR LTLPASLLDL PVEGGTPGSR
     LHGNPLYAGR AVSFFHGELA SFMVGTAYAA ADEYAAIISS RPLATDPERT RADLPDYQRY
     LGQALAKIST AEAAVRSAAE EYMEVCRRNT SGEAPFTMAE DDRLAAVFLT AAQLAWEALH
     DILYRTAGSQ HARDGARMQR YFRDGATYLS HVAPNMADPL AQRIGSARVG LPFDHIPLVR
//
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