ID G1KLB1_ANOCA Unreviewed; 675 AA.
AC G1KLB1;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 2.
DT 27-MAR-2024, entry version 70.
DE RecName: Full=Acyl-coenzyme A oxidase {ECO:0000256|PIRNR:PIRNR000168};
GN Name=ACOX2 {ECO:0000313|Ensembl:ENSACAP00000011389.3};
OS Anolis carolinensis (Green anole) (American chameleon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Iguania; Dactyloidae; Anolis.
OX NCBI_TaxID=28377 {ECO:0000313|Ensembl:ENSACAP00000011389.3, ECO:0000313|Proteomes:UP000001646};
RN [1] {ECO:0000313|Ensembl:ENSACAP00000011389.3, ECO:0000313|Proteomes:UP000001646}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JBL SC #1 {ECO:0000313|Ensembl:ENSACAP00000011389.3,
RC ECO:0000313|Proteomes:UP000001646};
RG The Genome Sequencing Platform;
RA Di Palma F., Alfoldi J., Heiman D., Young S., Grabherr M., Johnson J.,
RA Lander E.S., Lindblad-Toh K.;
RT "The Genome Sequence of Anolis carolinensis (Green Anole Lizard).";
RL Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSACAP00000011389.3}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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, ECO:0000256|PIRNR:PIRNR000168}.
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DR RefSeq; XP_003217885.1; XM_003217837.3.
DR RefSeq; XP_016847170.1; XM_016991681.1.
DR RefSeq; XP_016847171.1; XM_016991682.1.
DR AlphaFoldDB; G1KLB1; -.
DR STRING; 28377.ENSACAP00000011389; -.
DR Ensembl; ENSACAT00000011628.4; ENSACAP00000011389.3; ENSACAG00000011418.4.
DR GeneID; 100556696; -.
DR KEGG; acs:100556696; -.
DR CTD; 8309; -.
DR eggNOG; KOG0136; Eukaryota.
DR GeneTree; ENSGT00940000160985; -.
DR HOGENOM; CLU_014629_3_1_1; -.
DR InParanoid; G1KLB1; -.
DR OrthoDB; 5777at2759; -.
DR TreeFam; TF300672; -.
DR Proteomes; UP000001646; Chromosome 2.
DR Bgee; ENSACAG00000011418; Expressed in liver and 12 other cell types or tissues.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005777; C:peroxisome; IBA:GO_Central.
DR GO; GO:0033791; F:3alpha,7alpha,12alpha-trihydroxy-5beta-cholestanoyl-CoA 24-hydroxylase activity; IBA:GO_Central.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0005504; F:fatty acid binding; IBA:GO_Central.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IBA:GO_Central.
DR GO; GO:0016401; F:palmitoyl-CoA oxidase activity; IBA:GO_Central.
DR GO; GO:0006699; P:bile acid biosynthetic process; IEA:Ensembl.
DR GO; GO:0033540; P:fatty acid beta-oxidation using acyl-CoA oxidase; IBA:GO_Central.
DR GO; GO:0055088; P:lipid homeostasis; IBA:GO_Central.
DR GO; GO:0000038; P:very long-chain fatty acid metabolic process; IBA:GO_Central.
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 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|PIRNR:PIRNR000168, ECO:0000256|PIRSR:PIRSR000168-2};
KW Fatty acid metabolism {ECO:0000256|ARBA:ARBA00022832};
KW Flavoprotein {ECO:0000256|PIRNR:PIRNR000168};
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:UP000001646}.
FT DOMAIN 32..147
FT /note="Acyl-coenzyme A oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF14749"
FT DOMAIN 489..668
FT /note="Acyl-CoA oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF01756"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 437
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000168-1"
FT BINDING 154
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000168-2"
FT BINDING 193
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000168-2"
SQ SEQUENCE 675 AA; 76456 MW; E95128D3617DC4C2 CRC64;
MKKRSLSQIS PNSIMKDVNP DLDIERQNPS FDVERLTNIL DGGAEKTQIR RTVETWIQND
PELSRENQYF QSQNERYEEG IRKSLYLAKK MDEMGWVEGG PHRDYCSRSL SSDLAFNVHQ
VFVKSILGLG TDEQIAKWVP LAQKFYIAGT YAQTELGHGT YLRGLETTAT FDVATQEFIL
NTPTLSAMKW WPGDLGRTAT HAVVFAQLYL NGKSYGMHPF LMQIRSLRDH SPLPGVTVGD
IGPKMNFENV DNGFLVLKNV RVPRENMLAR FSQVLPDGQC KKQGTDKINY LTMIVVRVAM
IQREVVIILM KACTIAIRYS AVRRQSELKP GDPEAKILDY QTQQQKLLPQ LATAYAFHFV
SSYLQEVFDK AYTDTKEGKF DQLPELHALA SGIKVIATEY SSSGVEVCRK ACGGHGYSLL
SGLPSLYTRL VASCTYEGEN TVLLLQTARF LIKCFGMAKD GHPIPSSVAY LSSKNFGKCQ
AWKKGDFLNP DVYIDAYQQR AFRMLQNAAI KLQSLVQLGV AQHEAWNSCS VQLAWAAMAH
IHYIVVEQFA KALQRYEREA DVHRILKHLC DLFALHGMYL NTGDFMQDGY LSTEQVAMVT
ESYLDLLPVI RRDAVPLVDV FDFTDTSLNS ALGSYDGRVY ERLYEWAKKS PTNNQDKRVF
ETYLKPLFKN ALSKL
//
