ID W2ENP6_9ACTN Unreviewed; 538 AA.
AC W2ENP6;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 08-NOV-2023, entry version 31.
DE SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:ETK32477.1};
GN ORFNames=MPTA5024_29600 {ECO:0000313|EMBL:ETK32477.1};
OS Microbispora sp. ATCC PTA-5024.
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Streptosporangiaceae; Microbispora.
OX NCBI_TaxID=316330 {ECO:0000313|EMBL:ETK32477.1, ECO:0000313|Proteomes:UP000018869};
RN [1] {ECO:0000313|EMBL:ETK32477.1, ECO:0000313|Proteomes:UP000018869}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC PTA-5024 {ECO:0000313|EMBL:ETK32477.1,
RC ECO:0000313|Proteomes:UP000018869};
RX PubMed=24459268;
RA Sosio M., Gallo G., Pozzi R., Serina S., Monciardini P., Bera A.,
RA Stegmann E., Weber T.;
RT "Draft Genome Sequence of the Microbispora sp. Strain ATCC-PTA-5024,
RT Producing the Lantibiotic NAI-107.";
RL Genome Announc. 2:e01198-13(2014).
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:ETK32477.1}.
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; AWEV01000234; ETK32477.1; -; Genomic_DNA.
DR RefSeq; WP_036330174.1; NZ_KI866525.1.
DR AlphaFoldDB; W2ENP6; -.
DR STRING; 316330.MPTA5024_29600; -.
DR PATRIC; fig|316330.3.peg.5708; -.
DR HOGENOM; CLU_016513_0_0_11; -.
DR OrthoDB; 9771038at2; -.
DR Proteomes; UP000018869; 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; 2.40.110.20; -; 1.
DR Gene3D; 6.10.250.600; -; 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; IPR036250; AcylCo_DH-like_C.
DR InterPro; IPR009075; AcylCo_DH/oxidase_C.
DR InterPro; IPR009100; AcylCoA_DH/oxidase_NM_dom_sf.
DR InterPro; IPR041504; AidB_N.
DR PANTHER; PTHR42707; ACYL-COA DEHYDROGENASE; 1.
DR PANTHER; PTHR42707:SF3; ACYL-COA DEHYDROGENASE AIDB-RELATED; 1.
DR Pfam; PF00441; Acyl-CoA_dh_1; 1.
DR Pfam; PF02770; Acyl-CoA_dh_M; 1.
DR Pfam; PF18158; AidB_N; 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.
DR PROSITE; PS00073; ACYL_COA_DH_2; 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:UP000018869}.
FT DOMAIN 7..160
FT /note="Adaptive response protein AidB N-terminal"
FT /evidence="ECO:0000259|Pfam:PF18158"
FT DOMAIN 175..268
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 279..435
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
SQ SEQUENCE 538 AA; 57898 MW; D97C76717C34D64C CRC64;
MTHDVTNQVP PLTGHDVAAD PALLEGLARE GADWAVGELR QLGLLAGSAR AQEWGRLANE
HPPVLRTHDR YGHRIDEVEF HPAWHELMAV AVENGLHAAP WTSARPGAHV ARAAKFHVWS
QVEAGHGCPI SMTYAAVAAL RHSPALRAEW EPLLASRTYD FGLRPPLDKR GVLAGMAMTE
KQGGSDVRAN TTRAEPLADG TFALTGHKWF NSAPMCDAFL VLAQAPGGLS CFLLPRVLPD
GTRNAMRLMR LKDKLGNRSN ASAEVEYEGA VAHLVGEEGR GVRTIIEMVN MTRLDCVIGS
AAGMRYGLTQ ALHHARHRRV FGRELADQPL MRAVLADLAL ESEAATALMT RLAGATDRAV
RGDAGEGLFR RAALAAAKYW ICKRAPVHAA EALECLGGNG YVEESQMPRL FRESPLNGVW
EGSGNVAALD LMRVMAREPE AVDAFFAEVA LAGDRRVADA SERLLKRLAS AGEADARRVA
EEMTLVLQAS LLVRHAPAAV SDAFCASRLS GDWGRAFGTL PAGLDLEAVI ERAGRPGV
//
