ID   A0A229UU76_9BACL        Unreviewed;       394 AA.
AC   A0A229UU76;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   24-JAN-2024, entry version 14.
DE   SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:OXM86968.1};
GN   ORFNames=CF651_07440 {ECO:0000313|EMBL:OXM86968.1};
OS   Paenibacillus rigui.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=554312 {ECO:0000313|EMBL:OXM86968.1, ECO:0000313|Proteomes:UP000215509};
RN   [1] {ECO:0000313|EMBL:OXM86968.1, ECO:0000313|Proteomes:UP000215509}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 16352 {ECO:0000313|EMBL:OXM86968.1,
RC   ECO:0000313|Proteomes:UP000215509};
RA   Mayilraj S.;
RT   "Genome sequencing and assembly of Paenibacillus rigui.";
RL   Submitted (JUL-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:OXM86968.1}.
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; NMQW01000011; OXM86968.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A229UU76; -.
DR   OrthoDB; 1170793at2; -.
DR   Proteomes; UP000215509; Unassembled WGS sequence.
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; PTHR48083:SF2; MEDIUM-CHAIN SPECIFIC ACYL-COA DEHYDROGENASE, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR48083; MEDIUM-CHAIN SPECIFIC ACYL-COA DEHYDROGENASE, 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:UP000215509}.
FT   DOMAIN          248..370
FT                   /note="Acyl-CoA dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08028"
SQ   SEQUENCE   394 AA;  43689 MW;  0C1A2C3A0D14A717 CRC64;
     MSNLVLKEQN DVVAQVLDAA EKVGKLAEQE ALEAEANATI SENVINLMKE TQLSRLMLPK
     KYGGPQIDLK TFAQVVRKVA NYNISAAWLA YLYPLHNMLP AYLPPAGRDE VVNQGGLICD
     IFAALGKAES DGDGYRISGK WNFVSGVLFS DWVGVGVMIT FPGKSKPEFC LPIVRKSEIQ
     VVNNWDTFGL RGSGSNQVIA DNVYVPMERI LRLEAAESTR RPPEADYDKE YPYYHVPFYP
     AFYLGFPYMA LGGAERILAE FKKLTENRVR LMDGVRESES PRSQRVLAEM TTEFHAAEGL
     LDQYVRLLEN YEQNGASTSP AEFFAIRTKA IKMCTDIAVR ALLTLGGGAL YKGGTMELFL
     RDIIAVATHK TSLYEDSVAA YGKELFGFDS GVRG
//