ID   A0A0Q8RAY2_9SPHN        Unreviewed;       392 AA.
AC   A0A0Q8RAY2;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   SubName: Full=Flavin-dependent monooxygenase {ECO:0000313|EMBL:KRB91273.1};
GN   ORFNames=ASE22_13650 {ECO:0000313|EMBL:KRB91273.1};
OS   Sphingomonas sp. Root720.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingomonas.
OX   NCBI_TaxID=1736595 {ECO:0000313|EMBL:KRB91273.1, ECO:0000313|Proteomes:UP000051570};
RN   [1] {ECO:0000313|Proteomes:UP000051570}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root720 {ECO:0000313|Proteomes:UP000051570};
RA   Garrido-Oter R., Bai Y.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KRB91273.1, ECO:0000313|Proteomes:UP000051570}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root720 {ECO:0000313|EMBL:KRB91273.1,
RC   ECO:0000313|Proteomes:UP000051570};
RA   Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-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:KRB91273.1}.
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DR   EMBL; LMID01000011; KRB91273.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0Q8RAY2; -.
DR   STRING; 1736595.ASE22_13650; -.
DR   Proteomes; UP000051570; Unassembled WGS sequence.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
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; IPR036250; AcylCo_DH-like_C.
DR   InterPro; IPR037069; AcylCoA_DH/ox_N_sf.
DR   InterPro; IPR009100; AcylCoA_DH/oxidase_NM_dom_sf.
DR   PANTHER; PTHR43884; ACYL-COA DEHYDROGENASE; 1.
DR   PANTHER; PTHR43884:SF41; ACYL-COA DEHYDROGENASE YDBM-RELATED; 1.
DR   Pfam; PF08028; Acyl-CoA_dh_2; 1.
DR   PIRSF; PIRSF016578; HsaA; 1.
DR   SUPFAM; SSF47203; Acyl-CoA dehydrogenase C-terminal domain-like; 1.
DR   SUPFAM; SSF56645; Acyl-CoA dehydrogenase NM domain-like; 1.
PE   4: Predicted;
KW   Monooxygenase {ECO:0000313|EMBL:KRB91273.1};
KW   Oxidoreductase {ECO:0000313|EMBL:KRB91273.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000051570}.
FT   DOMAIN          241..370
FT                   /note="Acyl-CoA dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08028"
SQ   SEQUENCE   392 AA;  42349 MW;  38C35B3B9CC010BB CRC64;
     MQGESPSPAE LVERARSLIP VLRERAAAGD AGANVVAETI EDIKKAGLFR ILQPKRWGGY
     EMSPKVFYDV QMALAEGDMS VGWIYGVIGV HNWQIALFDD RAAREVFEND PDAIIASTYM
     PKGKTVPVEG GYRFTGRWQF SSGSKHAQWF FLGGLFPGGG EGIPNMGTFL IPREDVEIVE
     TWNTHGLKAT GSHDVIVKDA FVPDYRTHTH RQGFECDSPG NAVNSGPLYR LPFGQVFLRS
     VSTASIGALQ ALLDEVIGFA SGKLGSFGGK TADNPFAQVA VAEASATIAD LKNTLYANFD
     HLEAHAAAGT TPAIEDRLRF KYQSSEVASR CANVAGKLFR VAGGSGLFLD KPFARILADI
     QSGGQHQANS HELWGANFGA TLLGHENQDI FL
//