ID W2ES32_9ACTN Unreviewed; 744 AA.
AC W2ES32;
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:ETK33627.1};
GN ORFNames=MPTA5024_23610 {ECO:0000313|EMBL:ETK33627.1};
OS Microbispora sp. ATCC PTA-5024.
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Streptosporangiaceae; Microbispora.
OX NCBI_TaxID=316330 {ECO:0000313|EMBL:ETK33627.1, ECO:0000313|Proteomes:UP000018869};
RN [1] {ECO:0000313|EMBL:ETK33627.1, ECO:0000313|Proteomes:UP000018869}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC PTA-5024 {ECO:0000313|EMBL:ETK33627.1,
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 -!- SIMILARITY: Belongs to the acyl-CoA dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00009347}.
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:ETK33627.1}.
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DR EMBL; AWEV01000179; ETK33627.1; -; Genomic_DNA.
DR RefSeq; WP_036327806.1; NZ_KI866524.1.
DR AlphaFoldDB; W2ES32; -.
DR STRING; 316330.MPTA5024_23610; -.
DR PATRIC; fig|316330.3.peg.4550; -.
DR HOGENOM; CLU_018204_9_3_11; -.
DR OrthoDB; 3778631at2; -.
DR Proteomes; UP000018869; Unassembled WGS sequence.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
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; 2.
DR Gene3D; 2.40.110.10; Butyryl-CoA Dehydrogenase, subunit A, domain 2; 2.
DR Gene3D; 1.20.140.10; Butyryl-CoA Dehydrogenase, subunit A, domain 3; 2.
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:SF4; ACYL-COA DEHYDROGENASE FADE34; 1.
DR Pfam; PF00441; Acyl-CoA_dh_1; 2.
DR Pfam; PF02770; Acyl-CoA_dh_M; 1.
DR Pfam; PF02771; Acyl-CoA_dh_N; 2.
DR SUPFAM; SSF47203; Acyl-CoA dehydrogenase C-terminal domain-like; 2.
DR SUPFAM; SSF56645; Acyl-CoA dehydrogenase NM domain-like; 2.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Reference proteome {ECO:0000313|Proteomes:UP000018869}.
FT DOMAIN 6..119
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 216..343
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
FT DOMAIN 367..474
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 478..572
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 584..734
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
SQ SEQUENCE 744 AA; 77936 MW; 19C550A7350FA346 CRC64;
MAIGLSEEHE ALRESVAGWA ERAVPADLVR GAAGVLADSG TEERPAFWAG LADQGLLGLH
IPEEHGGSGY GLLEAAVAIE ALSERVAPGP FVPTVLAGAV ILASSAKAQA ALLPGLADGS
AIGAVALNGA VSGVREGGVL RITGTAEPVL GGALADVLVL PVTTDLGEEW VAVDASQATV
TPVKPLDLTR GVAKVEVDGV AVPPERVLDG LGRAEVLNLA AIVFGADATG VAAWCVAAAA
DYAKVRVQFG RPIGQFQGIK HKLSRMLVAL EQARATVWDA TRATGEERAY AAAIAGVMAP
DAAVQCAKDA IQTFGGIGYT FEHDAHLYYR RALTLRALLG SSAEWAETVA SLALGGVSRE
MEIDLPEESE PLREAIRAEL AEIAGIDDTA DGEGRRGSAR KRALAAAGFV MPHLPRPWGR
DASPLEQVLI HQEIRAAGLK LPQMVIGAWV VPSIVSYGTR EQQERFLPPT LSGEMVWCQL
FSEPGAGSDL ASLQMKAEKV EGGWKLNGQK IWTSVAHVAE WGICIARSDT SKPKHDGITY
FIVDMKSPGV TVRPLTEMTG ENLFNEVFLD DVFVPDDLVV GEVNDGWRVA RNTLSNERVS
LSSGSGGTGS SLPDLLGLAG RLGRELTPAE RQELAAVACE AHSINALSLR VTLKQLAGAE
PGADASVRKL LSTSHAQHVS EAAVNLLGAA AVTAADWKLG DAGYWNRAVL ATRAMTIYGG
TTEVQLNIIG ERMLGLPRDP EPGK
//
