ID A0A1E5MMG4_9MICO Unreviewed; 701 AA.
AC A0A1E5MMG4;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:OEI69806.1};
GN ORFNames=Cus16_0422 {ECO:0000313|EMBL:OEI69806.1};
OS Curtobacterium sp. ER1/6.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Curtobacterium.
OX NCBI_TaxID=1891920 {ECO:0000313|EMBL:OEI69806.1, ECO:0000313|Proteomes:UP000095245};
RN [1] {ECO:0000313|EMBL:OEI69806.1, ECO:0000313|Proteomes:UP000095245}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ER1/6 {ECO:0000313|EMBL:OEI69806.1,
RC ECO:0000313|Proteomes:UP000095245};
RA Garrido L.M., Alves J.M., Oliveira L.S., Gruber A., Padilla G.,
RA Araujo W.L.;
RT "Draft genome sequence of Curtobacterium sp. strain ER1/6, an endophytic
RT strain isolated from Citrus sinensis with potential to be used as a
RT biocontrol agent.";
RL Submitted (AUG-2016) 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 -!- SIMILARITY: Belongs to the acyl-CoA oxidase family.
CC {ECO:0000256|ARBA:ARBA00006288}.
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:OEI69806.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; MJAK01000001; OEI69806.1; -; Genomic_DNA.
DR RefSeq; WP_069710940.1; NZ_MJAK01000001.1.
DR AlphaFoldDB; A0A1E5MMG4; -.
DR STRING; 1891920.Cus16_0422; -.
DR PATRIC; fig|1891920.3.peg.440; -.
DR OrthoDB; 1144545at2; -.
DR Proteomes; UP000095245; Unassembled WGS sequence.
DR GO; GO:0005777; C:peroxisome; IEA:InterPro.
DR GO; GO:0003997; F:acyl-CoA oxidase activity; IEA:InterPro.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0006635; P:fatty acid beta-oxidation; 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; IPR012258; Acyl-CoA_oxidase.
DR InterPro; IPR002655; Acyl-CoA_oxidase_C.
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; PTHR10909:SF378; ACYL-COENZYME A OXIDASE-LIKE PROTEIN; 1.
DR PANTHER; PTHR10909; ELECTRON TRANSPORT OXIDOREDUCTASE; 1.
DR Pfam; PF01756; ACOX; 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 PIRSF; PIRSF000168; Acyl-CoA_oxidase; 1.
DR SUPFAM; SSF47203; Acyl-CoA dehydrogenase C-terminal domain-like; 2.
DR SUPFAM; SSF56645; Acyl-CoA dehydrogenase NM domain-like; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Reference proteome {ECO:0000313|Proteomes:UP000095245}.
FT DOMAIN 87..162
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 168..277
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 404..471
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
FT DOMAIN 528..667
FT /note="Acyl-CoA oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF01756"
FT REGION 1..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 701 AA; 76056 MW; FA891E0902CF17C1 CRC64;
MVDTAPAHLT STPAAEAPDA DATGDAAAGT PVGATDTDVH IDTTLLGELL LGRWAEDRRI
SRRLTLDPGL HKIEGQPVPE HRARTLEQLR VLVDAGAIQR PYPTEFGGQE NHGGNLAAFE
ELTTADPSLQ IKAGVQWGLF GSAVHHLGTE RNHREFLPGI IRFDVPGCFA MTETGHGSDV
QSIATTATYD AATQEFVVHT PFRGAWKDYI GNAALHGRAA VVFAKLVTQG VDHGVHAFYV
PLRDDAGAFL PGVGGEDDGV KGGLNGIDNG RLWFDHVRVP RTNLLNRYGD VAEDGTYSSP
IASPGRRFFT MLGTLVQGRV SLDGAAVVAQ KLALQIALTY AAERRQFPTG GGDEGVLLDY
GRHQRRLIPR LATVFAQSFA HEQLLQTFDD VFSGRKDTPE RREDLETQAA AFKSMSTWSA
LDTLQECREA CGGAGFLAEN RLTGLRADLD VYVTFEGDNT ILLQLVGKRL LTDFRARAPR
DAASTARFVA AQAASKLADA SGLRRLGQTV ADRGSLAASV SDLQDPRTQR ALLAGRVDTM
VAEIGMRLAS AGKDRARAAK LLNRSQHELI EAAKAHAELM QWDAFTEAIE SVAPGDTRRV
LVWLRDLFAL GLLEQHLDWH LLHGRLTAQR ARAVSAYVDR LVARIRPVVP QLVESFGYAP
EHVRAPIALG EERARQEEAA AWFAAEAAAG RLPEQEKKPR P
//
