ID A0A1E7JRG3_9ACTN Unreviewed; 642 AA.
AC A0A1E7JRG3;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:OEU91374.1};
GN ORFNames=AN216_24850 {ECO:0000313|EMBL:OEU91374.1};
OS Streptomyces oceani.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1075402 {ECO:0000313|EMBL:OEU91374.1, ECO:0000313|Proteomes:UP000176101};
RN [1] {ECO:0000313|EMBL:OEU91374.1, ECO:0000313|Proteomes:UP000176101}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SCSIO 02100 {ECO:0000313|EMBL:OEU91374.1,
RC ECO:0000313|Proteomes:UP000176101};
RX PubMed=27446038; DOI=10.3389/fmicb.2016.00998;
RA Tian X., Zhang Z., Yang T., Chen M., Li J., Chen F., Yang J., Li W.,
RA Zhang B., Zhang Z., Wu J., Zhang C., Long L., Xiao J.;
RT "Comparative Genomics Analysis of Streptomyces Species Reveals Their
RT Adaptation to the Marine Environment and Their Diversity at the Genomic
RT Level.";
RL Front. Microbiol. 7:998-998(2016).
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:OEU91374.1}.
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DR EMBL; LJGU01000158; OEU91374.1; -; Genomic_DNA.
DR RefSeq; WP_070198958.1; NZ_LJGU01000158.1.
DR AlphaFoldDB; A0A1E7JRG3; -.
DR STRING; 1075402.AN216_24850; -.
DR PATRIC; fig|1075402.3.peg.5454; -.
DR OrthoDB; 8876745at2; -.
DR Proteomes; UP000176101; 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; 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; 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.
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:UP000176101}.
FT DOMAIN 55..160
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 164..260
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 272..430
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
FT REGION 621..642
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 642 AA; 69668 MW; 3BF844C7D4CF812F CRC64;
MTVTEREARE VAEAAREQDW RKPSFAKELF LGRFRLDLIH PHPEAEAESV RRGEKFLATL
RDFCMSSIDG PLIERESRIP DEVMRGLKEI GALGMKVGTE YGGLGLSQVY YNKALALVSS
ASPAVGALLS AHQSIGVPQP LKLFGTQEQR DAFLPRCAST DISAFLLTEP DVGSDPARLA
TSAVPDGEDY LLDGVKLWTT NGVVADLLVV MARVPAGEGH RGGVSAFVVE GDSPGITVEN
RNAFMGLRGL ENGVTRFHQV RVPAANRIGP EGAGLKIALT TLNTGRLSLP ATCVGSGKWC
LKIAREWTEA RVQWGKPVAK HEAVGGKMSF IAATTFALEA VVDLSSQMAD EERNDIRIEA
ALAKLFGSEM AWRMADELVQ IRGGRGFETA ESLAARGERG VPAEQLLRDL RINRIFEGST
EIMHLLIARE AVDAHLSVAG DLIDPEKSVS DKGKAAVAAG GFYARWLPRL VAGPGQLPGA
YTEFDTLAPH LRYVERTARK LARSTFYAMS RWQGKLETKQ GFLARIVDIG AELFAMSAAC
VRADKLRAEG DWAAGAGEGP GGQAAYQLAD AFCRQSRIRV EELFGRLWHN TDDLDRSVVR
GILAGSYTWL EEGVIDASTE GPWIADATPG PSTRENVHRP IR
//
