ID A0A171DLY9_9ACTN Unreviewed; 388 AA.
AC A0A171DLY9;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:GAT69930.1};
GN ORFNames=PS9374_05610 {ECO:0000313|EMBL:GAT69930.1};
OS Planomonospora sphaerica.
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Streptosporangiaceae; Planomonospora.
OX NCBI_TaxID=161355 {ECO:0000313|EMBL:GAT69930.1, ECO:0000313|Proteomes:UP000077701};
RN [1] {ECO:0000313|EMBL:GAT69930.1, ECO:0000313|Proteomes:UP000077701}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 9374 {ECO:0000313|EMBL:GAT69930.1,
RC ECO:0000313|Proteomes:UP000077701};
RA Dohra H., Suzuki T., Inoue Y., Kodani S.;
RT "Draft Genome Sequence of Planomonospora sphaerica JCM9374, a Rare
RT Actinomycete.";
RL Genome Announc. 4:e00779-16(2016).
RN [2] {ECO:0000313|Proteomes:UP000077701}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 9374 {ECO:0000313|Proteomes:UP000077701};
RA Suzuki T., Dohra H., Kodani S.;
RT "Planomonospora sphaerica JCM9374 whole genome shotgun sequence.";
RL Submitted (APR-2016) 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:GAT69930.1}.
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DR EMBL; BDCX01000015; GAT69930.1; -; Genomic_DNA.
DR RefSeq; WP_068901734.1; NZ_BDCX01000015.1.
DR AlphaFoldDB; A0A171DLY9; -.
DR STRING; 161355.PS9374_05610; -.
DR OrthoDB; 3778631at2; -.
DR Proteomes; UP000077701; 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; PTHR43292; ACYL-COA DEHYDROGENASE; 1.
DR PANTHER; PTHR43292:SF3; ACYL-COA DEHYDROGENASE FADE29; 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 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|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU362125};
KW Reference proteome {ECO:0000313|Proteomes:UP000077701}.
FT DOMAIN 6..119
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 123..209
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 229..377
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
SQ SEQUENCE 388 AA; 41808 MW; 93B6D01D3E2504D7 CRC64;
MDLRETAAQR RLRTELRSYF ADLLPKDERR RAGEEGVGGD RFREVVRRLG ADGWLGLGWP
VEYGGQGRSA EDQYVFFDEV QRAGIPFPFV TVNTVGPTLM RHGSEEQRRR FLPGILSGDV
VFAIGYTEPG AGTDLASLTT RAVRDGDEFV VDGTKVFTSG ANTADHIWLA CRTDPGAPKH
RGISILIVPT SAPGFSWSPI RTVGGMTVTA TYYSGVRVPA SAVVGEVDGG WGLITTQLNH
ERIGLAALGG RMIRLWEDVL AWAGENGALD LPWVRRDLAR AHARLEAMRL LNWKMAGAVE
RGVLSGADAG AAKVYGTETH IDVQRTLTGI LGAAGRIRPE SPGAVLAGQI EQLSRQGIVN
TFGGGVNEVL RDMVATQGLG LPRRGRAA
//