ID A0A076MU03_AMYME Unreviewed; 418 AA.
AC A0A076MU03;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 35.
DE SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:AIJ21287.1};
GN Name=acd {ECO:0000313|EMBL:AIJ21287.1};
GN ORFNames=AMETH_1195 {ECO:0000313|EMBL:AIJ21287.1};
OS Amycolatopsis methanolica 239.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Amycolatopsis; Amycolatopsis methanolica group.
OX NCBI_TaxID=1068978 {ECO:0000313|EMBL:AIJ21287.1, ECO:0000313|Proteomes:UP000062973};
RN [1] {ECO:0000313|EMBL:AIJ21287.1, ECO:0000313|Proteomes:UP000062973}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=239 {ECO:0000313|EMBL:AIJ21287.1,
RC ECO:0000313|Proteomes:UP000062973};
RA Tang B.;
RT "Whole Genome Sequence of the Amycolatopsis methanolica 239.";
RL Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974,
CC ECO:0000256|RuleBase:RU362125};
CC -!- SIMILARITY: Belongs to the acyl-CoA dehydrogenase family.
CC {ECO:0000256|RuleBase:RU362125}.
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DR EMBL; CP009110; AIJ21287.1; -; Genomic_DNA.
DR RefSeq; WP_017987153.1; NZ_CP009110.1.
DR AlphaFoldDB; A0A076MU03; -.
DR STRING; 1068978.AMETH_1195; -.
DR KEGG; amq:AMETH_1195; -.
DR PATRIC; fig|1068978.7.peg.1259; -.
DR eggNOG; COG1960; Bacteria.
DR HOGENOM; CLU_018204_3_6_11; -.
DR OrthoDB; 8876745at2; -.
DR Proteomes; UP000062973; Chromosome.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016627; F:oxidoreductase activity, acting on the CH-CH group of donors; IEA:InterPro.
DR CDD; cd00567; ACAD; 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; IPR006091; Acyl-CoA_Oxase/DH_mid-dom.
DR InterPro; IPR046373; Acyl-CoA_Oxase/DH_mid-dom_sf.
DR InterPro; IPR036250; AcylCo_DH-like_C.
DR InterPro; IPR009075; AcylCo_DH/oxidase_C.
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; PF00441; Acyl-CoA_dh_1; 1.
DR Pfam; PF02770; Acyl-CoA_dh_M; 1.
DR SUPFAM; SSF47203; Acyl-CoA dehydrogenase C-terminal domain-like; 1.
DR SUPFAM; SSF56645; Acyl-CoA dehydrogenase NM domain-like; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|RuleBase:RU362125};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW ECO:0000256|RuleBase:RU362125};
KW Oxidoreductase {ECO:0000256|RuleBase:RU362125};
KW Reference proteome {ECO:0000313|Proteomes:UP000062973}.
FT DOMAIN 139..236
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 256..397
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
SQ SEQUENCE 418 AA; 46560 MW; 81F34A4A6909639F CRC64;
MTISFDLPAG TRQLLAELRE WSLHEVRPLA RTADTLETKV FEAGKRALES CPIDMSPLAV
PELGLVRSGG GKRYRASDSD DDNHVLGVLA MEAMCYGDGW AWGALPRNAN LEKILSVIGT
PQQLERWETP PGEQPIQSSF AFTEEHCGSD ISAIRTQAVR DGDEWVINGR KRFSSQGAEA
TVMLVFVTVD PARGMSGLRG VMVPQDSPGI KILRETEERK LGMRYLRQST IEFEDVRVPY
DHMLGDPDDP KGFLEGLNVL NRTRPFCMAW NVGTLRGATD YVGDWVKSQT PGFNARRRQR
IEEDLGEIRA SMDDLMRLLV NAAWKADHGL PHRTEAAMAK SHGPRIVERG YRRLVQIMGS
EGSSERHLLE KWYRDAVCFD LLEGTSQILK LTVGRGIFAA ANRELETDIA AALRPVSG
//
