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Database: UniProt
Entry: A0A164K536_9NOCA
LinkDB: A0A164K536_9NOCA
Original site: A0A164K536_9NOCA 
ID   A0A164K536_9NOCA        Unreviewed;       386 AA.
AC   A0A164K536;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:KZM71042.1};
GN   ORFNames=AWN90_41720 {ECO:0000313|EMBL:KZM71042.1};
OS   Nocardia terpenica.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC   Nocardia.
OX   NCBI_TaxID=455432 {ECO:0000313|EMBL:KZM71042.1, ECO:0000313|Proteomes:UP000076512};
RN   [1] {ECO:0000313|EMBL:KZM71042.1, ECO:0000313|Proteomes:UP000076512}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IFM 0406 {ECO:0000313|EMBL:KZM71042.1,
RC   ECO:0000313|Proteomes:UP000076512};
RA   Evans L.H., Alamgir A., Owens N., Weber N.D., Virtaneva K., Barbian K.,
RA   Babar A., Rosenke K.;
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:KZM71042.1}.
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DR   EMBL; LWGR01000013; KZM71042.1; -; Genomic_DNA.
DR   RefSeq; WP_067595115.1; NZ_KV411304.1.
DR   AlphaFoldDB; A0A164K536; -.
DR   STRING; 455432.AWN90_41720; -.
DR   OrthoDB; 8876745at2; -.
DR   Proteomes; UP000076512; 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   CDD; cd00567; ACAD; 1.
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; PTHR48083:SF1; DEHYDROGENASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_7G06510)-RELATED; 1.
DR   PANTHER; PTHR48083; MEDIUM-CHAIN SPECIFIC ACYL-COA DEHYDROGENASE, 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   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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000076512}.
FT   DOMAIN          6..117
FT                   /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02771"
FT   DOMAIN          123..200
FT                   /note="Acyl-CoA oxidase/dehydrogenase middle"
FT                   /evidence="ECO:0000259|Pfam:PF02770"
FT   DOMAIN          237..378
FT                   /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00441"
SQ   SEQUENCE   386 AA;  41594 MW;  E920011376F202AA CRC64;
     MSFIESDERK QLRAAVAQLA GKYNFRDYVS PKARANQPLS ELWDEAGRLG FLGVNLPEKY
     GGGGAGIYEL SLVLEELSAQ GAGLLLMVVS PAICGTILTR YGTEEQKRYW LTRLADGSSK
     MVFGITEPDA GSNSHHITTT ARRDGGDWIL NGRKIFISGV DQAEAVLIVS RTEDAKTGKL
     KPALFIVPTD APGFEKTRQE MDIIEPDSQF TLFLDDVRLP AEALVGQEDA ALAQLFAGLN
     PERIMGAAMA VGMGRYAIDR AVEYARERQV WKTPIGAHQG LAHPLAQVKI ELELAKLMMQ
     KAAVLYDSGD DFGAAEAANM AKYAAAEASI KALDQAIQTH GGSGLTRDVG LAGMLAAARI
     GRVAPVSREM VLNFVAQHSL GLPKSY
//
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