ID A0A417Y0A8_9ACTN Unreviewed; 393 AA.
AC A0A417Y0A8;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 13.
DE SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:RHW26007.1};
GN ORFNames=D0Z08_16920 {ECO:0000313|EMBL:RHW26007.1};
OS Nocardioides immobilis.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Nocardioidaceae; Nocardioides.
OX NCBI_TaxID=2049295 {ECO:0000313|EMBL:RHW26007.1, ECO:0000313|Proteomes:UP000283644};
RN [1] {ECO:0000313|EMBL:RHW26007.1, ECO:0000313|Proteomes:UP000283644}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCTCC AB 2017083 {ECO:0000313|EMBL:RHW26007.1,
RC ECO:0000313|Proteomes:UP000283644};
RA Li C., Wang G.;
RT "Genome sequencing of Nocardioides immobilis CCTCC AB 2017083 for
RT comparison to Nocardioides silvaticus.";
RL Submitted (SEP-2018) 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:RHW26007.1}.
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DR EMBL; QXGH01000020; RHW26007.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A417Y0A8; -.
DR OrthoDB; 142556at2; -.
DR Proteomes; UP000283644; 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 SUPFAM; SSF47203; Acyl-CoA dehydrogenase C-terminal domain-like; 1.
DR SUPFAM; SSF56645; Acyl-CoA dehydrogenase NM domain-like; 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|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU362125};
KW Reference proteome {ECO:0000313|Proteomes:UP000283644}.
FT DOMAIN 15..124
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 128..228
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 241..389
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
SQ SEQUENCE 393 AA; 43097 MW; A6C67E4D57A1EE37 CRC64;
MPARRSPWMN SADGELDDLR DLARTFCEKE IKPNIEDFIA NKQVDRELWT KAGELGLLCL
SIPEEYGGGG GTFAHEAIVI EEQAYVGDSS WGASLHSGIV AHYILAYGTE EQKHEWLPKL
ASGEAVGAIA MTEPGTGSDL QSVKTKATKI QDGQGDQFYL INGSKTFITN GAQADVVITV
VKTNPEEAAA GISLIIVPTD APGFSRGRVL DKIGMKGQDT AELVYEDVRV PVTNLLGSEE
GQGFIQLMQQ LPQERLIVAV SNVAAMEICM DETMRYVHDR HAFGRPIWGF QNTKFKMAEI
ATEARVARSF VDECIQLHVE GQLDIPTVAM AKLWCSERAQ KVADMCLQLH GGYGYMNEYP
IARAWADLRV SQIYAGTSEI MKEIIARSLP APA
//
