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Database: UniProt
Entry: A0A226NFP9_CALSU
LinkDB: A0A226NFP9_CALSU
Original site: A0A226NFP9_CALSU 
ID   A0A226NFP9_CALSU        Unreviewed;       521 AA.
AC   A0A226NFP9;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   08-NOV-2023, entry version 17.
DE   RecName: Full=Acyl-coenzyme A oxidase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=ASZ78_000645 {ECO:0000313|EMBL:OXB66220.1};
OS   Callipepla squamata (Scaled quail).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Odontophoridae;
OC   Callipepla.
OX   NCBI_TaxID=9009 {ECO:0000313|EMBL:OXB66220.1, ECO:0000313|Proteomes:UP000198323};
RN   [1] {ECO:0000313|EMBL:OXB66220.1, ECO:0000313|Proteomes:UP000198323}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Texas {ECO:0000313|EMBL:OXB66220.1,
RC   ECO:0000313|Proteomes:UP000198323};
RC   TISSUE=Leg muscle {ECO:0000313|EMBL:OXB66220.1};
RA   Oldeschulte D.L., Halley Y.A., Bhattarai E.K., Brashear W.A., Hill J.,
RA   Metz R.P., Johnson C.D., Rollins D., Peterson M.J., Bickhart D.M.,
RA   Decker J.E., Seabury C.M.;
RT   "Disparate Historic Effective Population Sizes Predicted by Modern Levels
RT   of Genome Diversity for the Scaled Quail (Callipepla squamata) and the
RT   Northern Bobwhite (Colinus virginianus): Inferences from First and Second
RT   Generation Draft Genome Assemblies for Sympatric New World Quail.";
RL   Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
CC   -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000256|ARBA:ARBA00004275}.
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:OXB66220.1}.
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DR   EMBL; MCFN01000068; OXB66220.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A226NFP9; -.
DR   STRING; 9009.A0A226NFP9; -.
DR   Proteomes; UP000198323; Unassembled WGS sequence.
DR   GO; GO:0005777; C:peroxisome; IEA:UniProtKB-SubCell.
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; IPR029320; Acyl-CoA_ox_N.
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; IPR037069; AcylCoA_DH/ox_N_sf.
DR   InterPro; IPR009100; AcylCoA_DH/oxidase_NM_dom_sf.
DR   PANTHER; PTHR10909; ELECTRON TRANSPORT OXIDOREDUCTASE; 1.
DR   PANTHER; PTHR10909:SF344; PEROXISOMAL ACYL-COENZYME A OXIDASE 2; 1.
DR   Pfam; PF01756; ACOX; 1.
DR   Pfam; PF14749; Acyl-CoA_ox_N; 1.
DR   SUPFAM; SSF47203; Acyl-CoA dehydrogenase C-terminal domain-like; 1.
DR   SUPFAM; SSF56645; Acyl-CoA dehydrogenase NM domain-like; 1.
PE   3: Inferred from homology;
KW   Fatty acid metabolism {ECO:0000256|ARBA:ARBA00022832};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Peroxisome {ECO:0000256|ARBA:ARBA00023140};
KW   Reference proteome {ECO:0000313|Proteomes:UP000198323}.
FT   DOMAIN          33..148
FT                   /note="Acyl-coenzyme A oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF14749"
FT   DOMAIN          336..514
FT                   /note="Acyl-CoA oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01756"
SQ   SEQUENCE   521 AA;  58145 MW;  1A09D1186610F379 CRC64;
     MALLDATKDT QGFGLTNVNP DLASERLTGS FSVPRLTAVL DGGAERTRLR RAVVDIIESD
     PVFGRENQYF QNQNERYEAA VRKAVHVRKK MQELGWSEDG PESVYVYRAL SGDVAFLLHR
     VFMRSISMLG SDKQVAKWIP LATEYQLIGS YGQTELGHVG RSATHTVVFA QLYIHGKCYG
     VHPFIVQIRS LQDHSLCPGI TAGDIGPKMN FEHVDNGYLM LKNVRIPREN MLNKFCEVQP
     DGTYIRHGSQ QINYFTMTSV RISLISDEVI LPLMKACTIA IRYSVVRRQS KLKPGFLIKC
     FAAASAGQPV PPSVTYLAAM KPGKCPAKDK LDFLSPDMYT DAYQHAAIRL ISSTAAKLQD
     LIQSGAESHE AWNQCTVQLV QAAKAHCHYI TVKNFVETVE KLESTAGIQN IMKHLRDLFA
     LHGIFSNAGI FLHDGYLTGA QMDMVTASYL DLLAIVRKDA VPLVDAFDFT DKSLNSALGA
     YDGQVYQRLY EWAQKAPTNK QISPAYEKYL KPLLHNKLSK L
//
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