ID   A0A7K7WQB0_9AVES        Unreviewed;       666 AA.
AC   A0A7K7WQB0;
DT   07-APR-2021, integrated into UniProtKB/TrEMBL.
DT   07-APR-2021, sequence version 1.
DT   29-SEP-2021, entry version 3.
DE   SubName: Full=ACOX1 oxidase {ECO:0000313|EMBL:NXA55535.1};
DE   Flags: Fragment;
GN   Name=Acox1 {ECO:0000313|EMBL:NXA55535.1};
GN   ORFNames=NOTJUL_R12381 {ECO:0000313|EMBL:NXA55535.1};
OS   Nothocercus julius.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Palaeognathae; Tinamiformes; Tinamidae; Nothocercus.
OX   NCBI_TaxID=2585813 {ECO:0000313|EMBL:NXA55535.1, ECO:0000313|Proteomes:UP000531559};
RN   [1] {ECO:0000313|EMBL:NXA55535.1, ECO:0000313|Proteomes:UP000531559}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B10K-MSB-01 {ECO:0000313|EMBL:NXA55535.1};
RA   Zhang G.;
RT   "Bird 10,000 Genomes (B10K) Project - Family phase.";
RL   Submitted (SEP-2019) 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:NXA55535.1}.
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DR   EMBL; VZSV01000294; NXA55535.1; -; Genomic_DNA.
DR   Proteomes; UP000531559; 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:0005504; F:fatty acid binding; IEA:InterPro.
DR   GO; GO:0033540; P:fatty acid beta-oxidation using acyl-CoA oxidase; IEA:InterPro.
DR   CDD; cd01150; AXO; 1.
DR   Gene3D; 1.10.540.10; -; 1.
DR   InterPro; IPR034171; ACO.
DR   InterPro; IPR029320; Acyl-CoA_ox_N.
DR   InterPro; IPR006091; Acyl-CoA_Oxase/DH_cen-dom.
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.
DR   PANTHER; PTHR10909; PTHR10909; 1.
DR   Pfam; PF01756; ACOX; 1.
DR   Pfam; PF02770; Acyl-CoA_dh_M; 1.
DR   Pfam; PF14749; Acyl-CoA_ox_N; 1.
DR   PIRSF; PIRSF000168; Acyl-CoA_oxidase; 1.
DR   SUPFAM; SSF47203; SSF47203; 2.
DR   SUPFAM; SSF56645; SSF56645; 1.
PE   3: Inferred from homology;
KW   FAD {ECO:0000256|PIRSR:PIRSR000168-2};
KW   Fatty acid metabolism {ECO:0000256|ARBA:ARBA00022832};
KW   Flavoprotein {ECO:0000256|PIRSR:PIRSR000168-2};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW   Peroxisome {ECO:0000256|ARBA:ARBA00023140};
KW   Reference proteome {ECO:0000313|Proteomes:UP000531559}.
FT   DOMAIN          21..138
FT                   /note="Acyl-CoA_ox_N"
FT                   /evidence="ECO:0000259|Pfam:PF14749"
FT   DOMAIN          141..249
FT                   /note="Acyl-CoA_dh_M"
FT                   /evidence="ECO:0000259|Pfam:PF02770"
FT   DOMAIN          485..662
FT                   /note="ACOX"
FT                   /evidence="ECO:0000259|Pfam:PF01756"
FT   ACT_SITE        426
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000168-1"
FT   BINDING         144
FT                   /note="FAD"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000168-2"
FT   BINDING         183
FT                   /note="FAD; via amide nitrogen"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000168-2"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:NXA55535.1"
FT   NON_TER         666
FT                   /evidence="ECO:0000313|EMBL:NXA55535.1"
SQ   SEQUENCE   666 AA;  74887 MW;  51C443149D2F2FD6 CRC64;
     VVTMVMNADL RRERAAATFQ PELLTNVLDG GAERTRRRRE IEALVINDPD FQHEDLNFLS
     RSQRYEQAIR KSSLMVMKLR EHGIADPDEI YLFKSFVHRG HPEPLDLHLG MFLPTLLTQA
     TPEQQDRFFM PSWNLEIIGT YAQTEMGHGS HIRGLETTAT YDPATQEFIL NSPTVTSIKW
     WPGGLGKSSN HAIVLAQLYT QGQCKGLHAF IVPIRQMGTH EPLPGITVGD IGPKFGYDEI
     DNGYLKMDNF RIPRENMLMK YAQVEPDGTY VKPLSDKLTY GTMVFIRSMI VGDSARALSR
     ACTIAIRYSA VRHQSELKAG EPEPQILDYQ TQQYKLFPLL ATAYAFHFVG TYMKDTYRRI
     SADIIEGDLS ELPELHALSA GLKAFSSWVA NAGVEECRMA CGGHGYSRCS GLPDIYVTFT
     PCCTYEGENT VMMLQTARFL IKSYMQVGSG QRVTGMVSYL NDLSRQHIQP QHVAARPVSV
     LINDPVSLVE AYKARAAWLV EAAAKNLQAE LNHRKSREDA WNVTSVDLVR ASDAHCHYVV
     VKLFTAKLSE ISNAAVRAVV TDLCLLYMLH GISKNAGDFL QAGILTNTQV NQVNQRVKEL
     LAIIRLNAVA LVDSFDFSDN YLGSVLGRYD GNVYENMFEW AKKSPLNKTE VHESFYKYLK
     PMQAKL
//