ID A0A0S9CQS8_9MICC Unreviewed; 706 AA.
AC A0A0S9CQS8;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:KQN95950.1};
GN ORFNames=ASF21_15520 {ECO:0000313|EMBL:KQN95950.1};
OS Arthrobacter sp. Leaf234.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Arthrobacter.
OX NCBI_TaxID=1736303 {ECO:0000313|EMBL:KQN95950.1, ECO:0000313|Proteomes:UP000053418};
RN [1] {ECO:0000313|Proteomes:UP000053418}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf234 {ECO:0000313|Proteomes:UP000053418};
RA Garrido-Oter R., Mueller D.B.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000053418}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf234 {ECO:0000313|Proteomes:UP000053418};
RA Vorholt J.;
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 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:KQN95950.1}.
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DR EMBL; LMLU01000011; KQN95950.1; -; Genomic_DNA.
DR RefSeq; WP_055773447.1; NZ_LMLU01000011.1.
DR AlphaFoldDB; A0A0S9CQS8; -.
DR STRING; 1736303.ASF21_15520; -.
DR Proteomes; UP000053418; 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; 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; IPR009100; AcylCoA_DH/oxidase_NM_dom_sf.
DR PANTHER; PTHR10909:SF382; ACYL-COENZYME A OXIDASE; 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 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}.
FT DOMAIN 152..261
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 295..456
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
FT DOMAIN 518..655
FT /note="Acyl-CoA oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF01756"
SQ SEQUENCE 706 AA; 77672 MW; B1D384DD449D153B CRC64;
MTQTISRPQQ IPATVDIRDD ERATVDTAEL GELLLGKWAD VRRVARELAG RPEVHKIEGL
THHDHRLRCF DQLHYLVQQQ AVHRAFPVAF GGNDDHGGNI AGFEELVVAD PSLQIKAGVQ
WGLFGSAVMH LGTQNHHEAW LPGIMDMEIP GCFAMTETGH GSDVASIATT ATFDAATDEF
VINTPFRAAW KDYIGNGAID GRAAVVFAQL ITNGVNHGVH GLYVELRTED GSFTPGVGGE
DDGIKGGLNG IDNGRLHFTD VRVPRTNLLN RYGDVAEDGT YTSPIASPGR RFFTMLGTLV
QGRVSLDGAA VAASKLALTA AVTYSTQRRQ FNASSDLKEE VLMDYQRHQR RLLPRLAATY
AASFAHEELL EKFDDVFSGA HDTDEDRQDL ETLAAALKPL STWLALDTLQ ECREATGGQG
FLIENRFASL RADLDVYVTF EGDNTVLLQL VAKRLLTDYA KEFKGVDFGV LARYAVSQAA
GRTLHRSGLR RVAQTVADSG SGKKSAIALR DEDTQHELLS DRVQTRVAEL AGALRGARGM
SQEKSAALFN LHQNELIEVA HAHAELLQWE AFTRGLERIE DPGTREVLTR LRDLFGLCLI
EKDLAWFLMN GRLSSQRART LDGYINRLLA KIRPHALDLV EAFGYGPEHL RSEIATGVED
LRQEEAAEYM RRRRAGGDAP IDEKTLLARV AKDKKAKKAK KAARAG
//
