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Database: UniProt
Entry: A0A0Q8VN88_9ACTN
LinkDB: A0A0Q8VN88_9ACTN
Original site: A0A0Q8VN88_9ACTN 
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
//
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