ID   A0A494SVN7_9NOCA        Unreviewed;       393 AA.
AC   A0A494SVN7;
DT   05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT   05-JUN-2019, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   SubName: Full=Hydroxylase {ECO:0000313|EMBL:AYJ48303.1};
GN   ORFNames=D8W71_08090 {ECO:0000313|EMBL:AYJ48303.1};
OS   Rhodococcus sp. P1Y.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC   Rhodococcus.
OX   NCBI_TaxID=1302308 {ECO:0000313|EMBL:AYJ48303.1, ECO:0000313|Proteomes:UP000277147};
RN   [1] {ECO:0000313|Proteomes:UP000277147}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=P1Y {ECO:0000313|Proteomes:UP000277147};
RA   Belimov A., Safronova V.I., Ismailov T.;
RT   "Complete genome sequence of the abscisic acid utilizing strain Rhodococcus
RT   sp. P1Y.";
RL   Submitted (OCT-2018) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000277147}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=P1Y {ECO:0000313|Proteomes:UP000277147};
RA   Nikolaichik Y.A., Gogoleva N.E., Khlopko Y.A., Gogolev Y.V.;
RL   Submitted (OCT-2018) to the EMBL/GenBank/DDBJ databases.
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; CP032762; AYJ48303.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A494SVN7; -.
DR   KEGG; rhop:D8W71_08090; -.
DR   OrthoDB; 3404950at2; -.
DR   Proteomes; UP000277147; Chromosome.
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; 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   Reference proteome {ECO:0000313|Proteomes:UP000277147}.
FT   DOMAIN          238..367
FT                   /note="Acyl-CoA dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08028"
SQ   SEQUENCE   393 AA;  42885 MW;  6B0096ACC4A18DFB CRC64;
     MSHEVLDNII AMAEDLRARA DEAESLGRLP DDMAKGIRHA GTMRMLARKE YGGFEAHPRD
     FAQVVMKTGS IYGSAGWVSG IVGVHPWQLA FADPKVQEEV LGSDSDTWQA SPYMPGGVAV
     PVEGGYVLSG RWQFSSGTDH CDWIFLGAMV GDKNGIPIMP PQSLHVIMPR ADYSIIEDSW
     DVVGLRGTGS KDIVVTEQFI PDYRVMDGGK VIDGTAAEEY GVTETLYKMP WSTMFPLGIT
     SATIGIAEGV LAAGVAYQRE RVGATGTAIK DDPYTLHALG EAAAEIDASR QQVLTNVDRM
     WDRIEAGETI TFEQRAEGRR NQTRAAWRAV RAADEIFDRS GGNALRMDNP LQRFWRDAHA
     GLHHAIHVSS IPYHSSALSS LGADPQGTLR IMI
//