ID V6L1V1_9ACTN Unreviewed; 380 AA.
AC V6L1V1;
DT 19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT 19-FEB-2014, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:EST38372.1};
GN ORFNames=N566_07810 {ECO:0000313|EMBL:EST38372.1};
OS Streptomycetaceae bacterium MP113-05.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae.
OX NCBI_TaxID=1380770 {ECO:0000313|EMBL:EST38372.1, ECO:0000313|Proteomes:UP000017915};
RN [1] {ECO:0000313|EMBL:EST38372.1, ECO:0000313|Proteomes:UP000017915}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MP113-05 {ECO:0000313|EMBL:EST38372.1,
RC ECO:0000313|Proteomes:UP000017915};
RA Valde M., Degnes K.F., Sletta H., Ruckert C., Kalinowski J., Zotchev S.B.;
RT "Streptomyces bacterium from a marine sponge: physiological
RT characterization and genome-based analysis of secondary metabolite
RT biosynthesis potential.";
RL Submitted (SEP-2013) 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:EST38372.1}.
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DR EMBL; AWQV01000232; EST38372.1; -; Genomic_DNA.
DR AlphaFoldDB; V6L1V1; -.
DR STRING; 1380770.N566_07810; -.
DR PATRIC; fig|1380770.3.peg.1378; -.
DR HOGENOM; CLU_018204_0_2_11; -.
DR OrthoDB; 8876745at2; -.
DR Proteomes; UP000017915; 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; 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|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU362125};
KW Reference proteome {ECO:0000313|Proteomes:UP000017915}.
FT DOMAIN 7..119
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 123..218
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 236..379
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
SQ SEQUENCE 380 AA; 41464 MW; FD5C3DDF3F5E8416 CRC64;
MQRQIFTPDH EAFRHTVRTF LAKEVEPDYT QWEKDGIVSR TAWLAAGRQG LLGIAVPEEY
GGGGEPDFRY AAVLAEEFAR AGAPGIAIGL HNDVIGPYLT SLATEEQKRR WLPGFCTGET
VTAIAMTEPG AGSDLQGIRT TAEDRGDHWL LNGAKTFISN GILADLVVVV AKTAPEGGAK
GLSLLVVERG AEGFTRGRNL DKVGQKSQDT AELFFHDVKL PKENLLGDRD GAFGHLMTNL
AQERMTIAVA AATAAEHVLD YTTAYVKERQ AFGRPLAKFQ HIRFQIAELA TECAVTRAFV
DRCIADHAVG ALDAAHASMA KYWATEQQVR VTDRCLQLHG GYGYMNEQPI ARAYADARVQ
TIYGGTTEIM KEIIGRSLLD
//
