ID   A0A208XSY5_9BURK        Unreviewed;       410 AA.
AC   A0A208XSY5;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 15.
DE   SubName: Full=Monooxygenase {ECO:0000313|EMBL:OVZ59064.1};
GN   ORFNames=CDO44_13690 {ECO:0000313|EMBL:OVZ59064.1};
OS   Pigmentiphaga sp. NML080357.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Pigmentiphaga.
OX   NCBI_TaxID=2008675 {ECO:0000313|EMBL:OVZ59064.1, ECO:0000313|Proteomes:UP000196551};
RN   [1] {ECO:0000313|EMBL:OVZ59064.1, ECO:0000313|Proteomes:UP000196551}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NML080357 {ECO:0000313|EMBL:OVZ59064.1,
RC   ECO:0000313|Proteomes:UP000196551};
RA   Bernier A.-M., Bernard K.;
RT   "Pigmentiphaga species Genome sequencing and assembly.";
RL   Submitted (MAY-2017) 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:OVZ59064.1}.
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; NINW01000031; OVZ59064.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A208XSY5; -.
DR   OrthoDB; 7316074at2; -.
DR   Proteomes; UP000196551; 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:SF12; COMPLEX I ASSEMBLY FACTOR ACAD9, MITOCHONDRIAL-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:OVZ59064.1};
KW   Oxidoreductase {ECO:0000313|EMBL:OVZ59064.1}.
FT   DOMAIN          254..389
FT                   /note="Acyl-CoA dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08028"
SQ   SEQUENCE   410 AA;  43009 MW;  D8C4FE4E1EA3ED27 CRC64;
     MSSFAEHAIL SPPGGTDAPS PPLVAALREL APGLRAAARE VEAARRIPAA HMELVRATGF
     FDLVKPAAYG GAEQSFAALV EANLLLAQHC ASTAWVCGLL AAHQWLLAGF PAEAQHDVWG
     ADPDALLCGS YAPASRAQPA PGGLRLSGSW SFASGCENAR WALCAAMVPC ADDPSRLEPA
     FLLVPATDYR IVDTWNVVGL AGTGSKTLVL DDVYVPAHRL LTFAQTTSGN TPGAAHYRQV
     PGYRIPMLTV IPSCLASVAV GAAQGALDEY VAVTSGRVTR GAVAGAHQKM AEFATVQLRV
     AEAAASADAA REILLRDLRW VTARVGGGHA VTEEDRIVCR RGQSFAVSLA LRAIEALNAS
     TGGAGLQMDN PVQRAWRDIN AVGRHISMNW DAVGTMYGQM ALGLTPRGQY
//