ID A0A101CR99_9FLAO Unreviewed; 753 AA.
AC A0A101CR99;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Acyl-CoA oxidase {ECO:0000313|EMBL:KUJ60902.1};
GN ORFNames=AR687_15970 {ECO:0000313|EMBL:KUJ60902.1};
OS Flavobacteriaceae bacterium CRH.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae.
OX NCBI_TaxID=1742859 {ECO:0000313|EMBL:KUJ60902.1, ECO:0000313|Proteomes:UP000053826};
RN [1] {ECO:0000313|EMBL:KUJ60902.1, ECO:0000313|Proteomes:UP000053826}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CRH {ECO:0000313|EMBL:KUJ60902.1,
RC ECO:0000313|Proteomes:UP000053826};
RA Newman J.D., Miller J.R., Jacobs K.T.;
RT "Genome Sequence of Flavobacterium sp. CHR.";
RL Submitted (OCT-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:KUJ60902.1}.
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DR EMBL; LMAJ01000016; KUJ60902.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A101CR99; -.
DR STRING; 1742859.AR687_15970; -.
DR OrthoDB; 1144545at2; -.
DR Proteomes; UP000053826; 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 186..259
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 610..751
FT /note="Acyl-CoA oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF01756"
SQ SEQUENCE 753 AA; 84759 MW; 30771147F64E0D7A CRC64;
MKNTKLQAFI PLFYLVWSDD LLTQKEFATL QEFIRSQTLL NPEEKQLLLS KVDISNPPSR
NELAQWKLDI EKSLKDKSSI KSIFDIAVAL SEKDLDISSL QSDFTKLEND LGVLGEEVIQ
NFKTKEGSFT ANSQTNSNFD IQKITQLLDG KEAAIIKKVK SVISRPEFAY ETSTDINVFR
ETVYKWCKIL ADENLGNMAY PKQYGGGENI ADYFTIMETL SYHDLSLVIK FGVQFGLWGM
SVQSLGTEKH YAKYLKDIGS LKLPGCFAMT ETHHGSNVKG LETTATYNHS NQTFTIHTPH
EKAQKEYIGN AAVHGQMATV FAKLIINDHD YGVNAFVVPL RDTNGNTLNG VTIGDCGHKM
GLNGVDNGTI RFDQVVIPKE NMLDRFASVN DKGEFESPIP SDNRRFFTML GTLVGGRIGI
PRSALAAAKS GLTIAIRYSD QRRQFGPEGG SEVPILNYRM HQRRLLPHLA KTYAVHFALQ
YLTKRFLNKT ESEMQEIEAL AAGMKSYSTW STRDILQECR EAIGGKGYLS ENRIDDLKND
TEIYTTFEGD NTVLMQLVAK NRLAEFRKAF GEMGSLGIIN YVYGNAKVAI SEKNPIATRR
ADDEHLLDSE FHLQAFIHRE KTILASAARR IKKLVDGGLE PYDAFNVVQH QMIDVAQAYL
ERIVLEQFQE AIKTVEDENS KVILTKLYQL YALSQIEKNK AWYLEDGYME AVKTKAIRKI
VNQLCWDIRP DAVALVNAFD IPESCLSAPI AAI
//
