ID I2NBR8_STRT9 Unreviewed; 385 AA.
AC I2NBR8;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2012, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:QKM65911.1};
GN ORFNames=STSU_000800 {ECO:0000313|EMBL:QKM65911.1};
OS Streptomyces tsukubensis (strain DSM 42081 / NBRC 108919 / NRRL 18488 /
OS 9993).
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1114943 {ECO:0000313|EMBL:QKM65911.1, ECO:0000313|Proteomes:UP000005940};
RN [1] {ECO:0000313|EMBL:QKM65911.1, ECO:0000313|Proteomes:UP000005940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 42081 / NBRC 108919 / NRRL 18488 / 9993
RC {ECO:0000313|Proteomes:UP000005940};
RX PubMed=22740677; DOI=10.1128/JB.00692-12;
RA Barreiro C., Prieto C., Sola-Landa A., Solera E., Martinez-Castro M.,
RA Perez-Redondo R., Garcia-Estrada C., Aparicio J.F.,
RA Fernandez-Martinez L.T., Santos-Aberturas J., Salehi-Najafabadi Z.,
RA Rodriguez-Garcia A., Tauch A., Martin J.F.;
RT "Draft genome of Streptomyces tsukubaensis NRRL 18488, the producer of the
RT clinically important immunosuppressant tacrolimus (FK506).";
RL J. Bacteriol. 194:3756-3757(2012).
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}.
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DR EMBL; CP029159; QKM65911.1; -; Genomic_DNA.
DR RefSeq; WP_006344677.1; NZ_CP029159.1.
DR AlphaFoldDB; I2NBR8; -.
DR Proteomes; UP000005940; Chromosome.
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; 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}.
FT DOMAIN 26..114
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 118..219
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 239..381
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
SQ SEQUENCE 385 AA; 38841 MW; E013B58092B8B3EF CRC64;
MTPATAATAG AGIDTAAIDA LVGDGPAAWD AAGRIPVALL RKLGAAGVLC AEVPAALGGP
GADPLANGEL TAHIGALCSS LRSIMTVHGI AAATVHRFGD RAQRRDYLGQ LTSGRLACVG
FSEPGAGSDL SGMTTRIRPA GDSSGDLLVT GEKMWITGAV YADTVLVFGQ YGAGPAGSGG
AVGAAAMVPA DAPGVSIEPV KDPLGCRAAT HCRIVLDDVR IPASAVLGGG GQPLSLLFTT
ALSYGRMSVA WGCAGILRAC LTAATADART REQGGVPIAE HQLVARHIAE LYTSEQIATQ
ACRHAAQQWT RGAPDAAVAA VLAKQVAATH AARGAATAVQ VLASRGFTDG HVTARAYRDA
KAMELIEGST EISQLILARH ALDIH
//
