ID A0A0Q4RNZ0_9FLAO Unreviewed; 753 AA.
AC A0A0Q4RNZ0;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Acyl-CoA oxidase {ECO:0000313|EMBL:KQO23058.1};
GN ORFNames=ASF10_10620 {ECO:0000313|EMBL:KQO23058.1};
OS Flavobacterium sp. Leaf82.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Flavobacterium.
OX NCBI_TaxID=1736238 {ECO:0000313|EMBL:KQO23058.1, ECO:0000313|Proteomes:UP000051828};
RN [1] {ECO:0000313|EMBL:KQO23058.1, ECO:0000313|Proteomes:UP000051828}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf82 {ECO:0000313|EMBL:KQO23058.1,
RC ECO:0000313|Proteomes:UP000051828};
RX PubMed=26633631; DOI=.1038/nature16192;
RA Bai Y., Muller D.B., Srinivas G., Garrido-Oter R., Potthoff E., Rott M.,
RA Dombrowski N., Munch P.C., Spaepen S., Remus-Emsermann M., Huttel B.,
RA McHardy A.C., Vorholt J.A., Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiota.";
RL Nature 528:364-369(2015).
RN [2] {ECO:0000313|Proteomes:UP000051828}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf82 {ECO:0000313|Proteomes:UP000051828};
RA Garrido-Oter R., Mueller D.B.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Proteomes:UP000051828}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf82 {ECO:0000313|Proteomes:UP000051828};
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 -!- 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:KQO23058.1}.
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DR EMBL; LMMA01000032; KQO23058.1; -; Genomic_DNA.
DR RefSeq; WP_056251523.1; NZ_LMMA01000032.1.
DR AlphaFoldDB; A0A0Q4RNZ0; -.
DR OrthoDB; 1144545at2; -.
DR Proteomes; UP000051828; 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}.
FT DOMAIN 187..258
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 266..375
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 409..561
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
FT DOMAIN 612..751
FT /note="Acyl-CoA oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF01756"
SQ SEQUENCE 753 AA; 84841 MW; B8C9260FFAB22E6E CRC64;
MKNTKLQAFT PLFYLVWSDD LLTQKEFTTI QKFINDLTWL SPEEKQELVS RLDISNPPSR
NELTQWKLDI EKSIQNKTDI KSIFDIAVAL SEKDVDISTL ESNFIKLEND LGILGEEALQ
NFKTKANSFT ANSQTNSDFD IQKITKILNG KEAAIINKVK SVISRPEFAY ETSTDINVYR
QTVYSWCKIL AEENLGNMAY PKQYGGGENI ADYFAIMETL SYHDLSLVIK FGVQFGLWGM
SVQSLGTDKH YAKYLKDIGT LKIPGCFAMT ETHHGSNVKG LETTATYNHN DQTFTIHTPN
KNAQKEYIGN AAVHGQMATV FAKLVIDGHD YGVNAFVVPL RDTNGNTLNG ITIGDCGHKM
GLNGVDNGTI SFENVVIPKE NMLDRFASVN DKGEFESPIP SDNRRFFIML GTLVGGRIGI
PRSALAAAKS GLTIAIRYSD QRRQFGPEGG SEVPILNYRM HQRRLIPPLA KTYAVHFALQ
YLTNRFLNKT EAEMQEIEAL AAGMKSYSTW STRDILQECR EACGGKGYLS ENRIDALKND
TEIYTTFEGD NTVLMQLVAK NRLSEFRKSF GEMGSLGIIN YVYENAKTAI TEKNPIATRK
TDDEHLLDNE FHLQAFIHRE KTILASAARR IKKLVDGGLE PYDAFNVVQH QMIDVAQAYL
ERVVLEQFQL AIKEIEDVQS KEILTKLNHL YALSQIEKNK AWYLEDGYME AVKTKAIRKM
VNQLCWDIRP DAVSLVNAFD IPESCLSAPI AVR
//
