ID A0A239H344_9ACTN Unreviewed; 386 AA.
AC A0A239H344;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=Acyl-CoA dehydrogenase {ECO:0008006|Google:ProtNLM};
GN ORFNames=SAMN04488107_3656 {ECO:0000313|EMBL:SNS75448.1};
OS Geodermatophilus saharensis.
OC Bacteria; Actinomycetota; Actinomycetes; Geodermatophilales;
OC Geodermatophilaceae; Geodermatophilus.
OX NCBI_TaxID=1137994 {ECO:0000313|EMBL:SNS75448.1, ECO:0000313|Proteomes:UP000198386};
RN [1] {ECO:0000313|EMBL:SNS75448.1, ECO:0000313|Proteomes:UP000198386}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45423 {ECO:0000313|EMBL:SNS75448.1,
RC ECO:0000313|Proteomes:UP000198386};
RA Kim H.J., Triplett B.A.;
RL Submitted (JUN-2017) 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}.
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DR EMBL; FZOH01000008; SNS75448.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A239H344; -.
DR OrthoDB; 8876745at2; -.
DR Proteomes; UP000198386; Unassembled WGS sequence.
DR GO; GO:0003995; F:acyl-CoA dehydrogenase activity; IEA:InterPro.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:UniProtKB-UniRule.
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; IPR006089; Acyl-CoA_DH_CS.
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; 1.
DR SUPFAM; SSF47203; Acyl-CoA dehydrogenase C-terminal domain-like; 1.
DR SUPFAM; SSF56645; Acyl-CoA dehydrogenase NM domain-like; 1.
DR PROSITE; PS00072; ACYL_COA_DH_1; 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|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU362125}.
FT DOMAIN 6..116
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 121..217
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 231..379
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
SQ SEQUENCE 386 AA; 41907 MW; 400D44BFA7ECEBA9 CRC64;
MTELSREERD VVATVRTFVD REVRPVVRAL EHADTYPEAL VERMKQLGVF GLAVPEPWGE
APVSMPCYAL VTAELARGWM SLAGAMGGHT VVAKLLVAFG TREQQDRWLP RMATGEVRAT
MALTEPGGGS DLQAMTTVAR RDGDGDGYVV DGAKTWITNS RRSQLIALLC KTDPAAQPRH
RGVSVLLVEH GPGLTVSRDL PKLGYKGVES CELVFDGYRA PADAVLGGVE GRGFAQMMTG
LETGRIQVAA RAVGVAQAAF DDALRYAQQR ESFGRPIWQH QSVGNLLADM ATSLTAARQL
VLHAAERYES GQRCNLEAGM AKLFASETAM RIALDAIRVH GGHGYSTEFD VERYFRDAPL
MIVGEGTNEI QRDVIARQLV ARGGLD
//
