ID A0A0C1U773_9ACTN Unreviewed; 385 AA.
AC A0A0C1U773;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:KIE48629.1};
GN ORFNames=MB54_07035 {ECO:0000313|EMBL:KIE48629.1};
OS marine actinobacterium MedAcidi-G2B.
OC Bacteria; Actinomycetota; Actinomycetes.
OX NCBI_TaxID=1550401 {ECO:0000313|EMBL:KIE48629.1, ECO:0000313|Proteomes:UP000031352};
RN [1] {ECO:0000313|EMBL:KIE48629.1, ECO:0000313|Proteomes:UP000031352}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mizuno C.M., Rodriguez-Valera F., Ghai R.;
RT "Novel reconstructed genomes of marine planktonic Acidimicrobiales.";
RL Submitted (SEP-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|ARBA:ARBA00009347, ECO:0000256|RuleBase:RU362125}.
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:KIE48629.1}.
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DR EMBL; JUEO01000026; KIE48629.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0C1U773; -.
DR STRING; 1550401.MB54_07035; -.
DR Proteomes; UP000031352; Unassembled WGS sequence.
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 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; 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; IPR013786; AcylCoA_DH/ox_N.
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; PF00441; Acyl-CoA_dh_1; 1.
DR Pfam; PF02770; Acyl-CoA_dh_M; 1.
DR Pfam; PF02771; Acyl-CoA_dh_N; 1.
DR PIRSF; PIRSF016578; HsaA; 2.
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}.
FT DOMAIN 10..115
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 120..212
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 230..379
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
SQ SEQUENCE 385 AA; 42720 MW; 68CFCA09E101E74C CRC64;
MATDKALADE MISTIRAWVD REVIPNADEF EQEDKFPQAM FDQMCEFGLF GATIPEEYGG
LGLDITTYTR IIEELSRGFM SLAGILNTHK IGVSMIYRYG TEEQKQRFLP RMVDGSFRAS
FSLSEPDAGS DTGALRCKAE QDGDEWVING TKMWVTNGIR SSLVMLLART PDDRITCFLV
EKEPGEKFEG ITASKKISKL GYRGLETVEM SYVDHRVPDT NVLGGEEGLG NGRKYALSAL
ELGRINVASR AVGVAQAAFD AAMAYAQERE TFGQPIFKHQ AIQFKLAEMA TKLQAARLMT
YDAAARADAG ERVDMEAGMA KLFASEAAYE IATDALRIHG GNGYTTEYPV ERYFRDTPLM
IIGEGTSEIQ KMVIARKLLD RYSVE
//
