ID A0A0Q8VN88_9ACTN Unreviewed; 735 AA.
AC A0A0Q8VN88;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:KRC58958.1};
GN ORFNames=ASE19_23160 {ECO:0000313|EMBL:KRC58958.1};
OS Nocardioides sp. Root79.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Nocardioidaceae; Nocardioides.
OX NCBI_TaxID=1736600 {ECO:0000313|EMBL:KRC58958.1, ECO:0000313|Proteomes:UP000051414};
RN [1] {ECO:0000313|EMBL:KRC58958.1, ECO:0000313|Proteomes:UP000051414}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root79 {ECO:0000313|EMBL:KRC58958.1,
RC ECO:0000313|Proteomes:UP000051414};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KRC58958.1, ECO:0000313|Proteomes:UP000051414}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root79 {ECO:0000313|EMBL:KRC58958.1,
RC ECO:0000313|Proteomes:UP000051414};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- SIMILARITY: Belongs to the acyl-CoA dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00009347}.
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:KRC58958.1}.
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DR EMBL; LMIP01000002; KRC58958.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0Q8VN88; -.
DR OrthoDB; 4577375at2; -.
DR Proteomes; UP000051414; Unassembled WGS sequence.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
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; 2.
DR Gene3D; 2.40.110.10; Butyryl-CoA Dehydrogenase, subunit A, domain 2; 2.
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; PTHR43292; ACYL-COA DEHYDROGENASE; 1.
DR PANTHER; PTHR43292:SF3; ACYL-COA DEHYDROGENASE FADE29; 1.
DR Pfam; PF00441; Acyl-CoA_dh_1; 2.
DR Pfam; PF02770; Acyl-CoA_dh_M; 1.
DR Pfam; PF02771; Acyl-CoA_dh_N; 2.
DR SUPFAM; SSF47203; Acyl-CoA dehydrogenase C-terminal domain-like; 2.
DR SUPFAM; SSF56645; Acyl-CoA dehydrogenase NM domain-like; 2.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000051414}.
FT DOMAIN 24..116
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 209..316
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
FT DOMAIN 380..469
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 473..562
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 579..725
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
SQ SEQUENCE 735 AA; 79274 MW; F9AF0F8566BA4144 CRC64;
MRSRLEHVTV CIVDAESNNE AGEAVRAVVA EVLERESDAR EWAAWAAAGL TALPVPEEHG
GEGLGLTEVA VLLREAGRHA VQVPAWETLC CGALTLASYG TEVQRKDLLP GIATGELVVT
PALRGDAVYD GSRVTGRKLA VTHVEAAHRL LVVATEGDRE VVVLVDPRGE GVELLPSSAS
SAAPQHTVVL DGAPAEVLED GAAARLRDLA RAGLAVTAAG VLCGARDLTA GYVKGRQQFG
RALAEFQAVS LQMADVYVAS RTLDLAADNA VWRVAEGLPA AEDLAVAGYW ASQVAPYAFR
TCHHLHGGMG VDITYPLVGF TTWGTDLAHA LDTTAAQVPV ESRDAKNLEL TAEQRDLKDR
LRAYFGGVAA QYEGLHDPDP VEGAWDRHGP TYSRLIRQLG TDGWMGVGWP KEYGGHGLGE
IEQTIFANEA QYADVHLPSV TLQTVGPTLI RYGTQKQKDL FLERILKGDV HFAIGYSEPD
AGTDLASLRT TARRDGDHYV VNGQKMWTTG GHHADYLWLA VRTDPDAPKH KGISILIVDT
SDPGYSWTPI ITADGSHHVN ATYFNDVRVP VDMLVGEENQ GWKLITTQLN HERVMLGPAG
RIEGLRDRVI RWADAAGVRD EPDVRDLLGK TTAVFRINEL LNWEVARAAA SGELQVADAS
SSKVFASDQV QHLLADLVSL VHRHGDPGDP ATRDLLDYLD GQAKRNLVIT FGGGVQEVQR
ELISMFGLGL PRVPR
//