ID A0A150GES3_GONPE Unreviewed; 654 AA.
AC A0A150GES3;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 08-NOV-2023, entry version 27.
DE RecName: Full=Acyl-coenzyme A oxidase {ECO:0000256|PIRNR:PIRNR000168};
GN ORFNames=GPECTOR_29g92 {ECO:0000313|EMBL:KXZ48318.1};
OS Gonium pectorale (Green alga).
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC CS clade; Chlamydomonadales; Volvocaceae; Gonium.
OX NCBI_TaxID=33097 {ECO:0000313|EMBL:KXZ48318.1, ECO:0000313|Proteomes:UP000075714};
RN [1] {ECO:0000313|Proteomes:UP000075714}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIES-2863 {ECO:0000313|Proteomes:UP000075714};
RX PubMed=27102219; DOI=10.1038/ncomms11370;
RA Hanschen E.R., Marriage T.N., Ferris P.J., Hamaji T., Toyoda A.,
RA Fujiyama A., Neme R., Noguchi H., Minakuchi Y., Suzuki M.,
RA Kawai-Toyooka H., Smith D.R., Sparks H., Anderson J., Bakaric R., Luria V.,
RA Karger A., Kirschner M.W., Durand P.M., Michod R.E., Nozaki H., Olson B.J.;
RT "The Gonium pectorale genome demonstrates co-option of cell cycle
RT regulation during the evolution of multicellularity.";
RL Nat. Commun. 7:11370-11370(2016).
CC -!- SIMILARITY: Belongs to the acyl-CoA oxidase family.
CC {ECO:0000256|PIRNR:PIRNR000168}.
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:KXZ48318.1}.
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DR EMBL; LSYV01000030; KXZ48318.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A150GES3; -.
DR STRING; 33097.A0A150GES3; -.
DR OrthoDB; 5473219at2759; -.
DR Proteomes; UP000075714; 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:0006631; P:fatty acid metabolic process; 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; IPR036250; AcylCo_DH-like_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; PF02770; Acyl-CoA_dh_M; 1.
DR PIRSF; PIRSF000168; Acyl-CoA_oxidase; 2.
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|PIRNR:PIRNR000168, ECO:0000256|PIRSR:PIRSR000168-2};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW ECO:0000256|PIRNR:PIRNR000168};
KW Reference proteome {ECO:0000313|Proteomes:UP000075714}.
FT DOMAIN 152..261
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT REGION 431..457
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 436..454
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 156
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000168-2"
SQ SEQUENCE 654 AA; 70353 MW; 736F89F40BD62FF3 CRC64;
MDDATRRLRV VSGHFRVQKA QSAQASGVPF DVKELQRLLD HDNHEHRQKM KEFMNDDLYV
PQYDISLADE RELALQRLKR VCRAGFISVS DFRTNPFRIF AAHEVAALAD PSMGTKMTVQ
FNLFGGTVLK LGTERHHGPF LRDMDMLDAV GCFALTELGF GNNAVEMQTT AVYDPATQEF
VINTPGSLAQ KYWITNSAVH AQWAVVFAQL CVGGRQEGIH GFLVRIRNPD MSVCGGVRVE
DMGHKMGCNG VDNGKLWFDN VRVPRTALLN ASSDVAPDGS FASSVPRPRD RFLRVADQLL
SGRLCIAAMM QSGSKLALTI AFRYAGSRLC VGPSGRSDTP ILDYQLQQRA LVPLLARTTA
LAVGLNYVKE RWAAASGFVP GQAVDPVTAT EVVVLCCAIK PLCSWNIEQC GTVCRERCGG
QGYLSCNRTS RSGPLIPTHS PPPPPPPRPP LPRSPQGGDA LSLLGDLALL RRLMVVREGR
LVRRLGAAMD AAGRAAGGSA SEATFETWMK RESDLVQGTA LAFAEREVLD ALLRALGTDP
QPGANPAAAA ACPPPPRLSG GVAGVLRGVA VLFALRCVEA DLAWFVAEGE LPAKAGRSVP
EAVRSAVLAL SPAACTGLIE SFGIPDHLVA APIAGDWARY NQVDNKGELF GADV
//
