ACOX1_DICDI
ID ACOX1_DICDI Reviewed; 700 AA.
AC Q54GQ6;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Peroxisomal acyl-coenzyme A oxidase 1;
DE EC=1.3.3.6;
GN Name=acox1; ORFNames=DDB_G0289993;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
CC -!- FUNCTION: Catalyzes the desaturation of acyl-CoAs to 2-trans-enoyl-
CC CoAs. First enzyme of the fatty acid beta-oxidation pathway.
CC {ECO:0000250|UniProtKB:Q15067}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 2,3-saturated acyl-CoA + O2 = a (2E)-enoyl-CoA + H2O2;
CC Xref=Rhea:RHEA:38959, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240,
CC ChEBI:CHEBI:58856, ChEBI:CHEBI:65111; EC=1.3.3.6;
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the acyl-CoA oxidase family. {ECO:0000305}.
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DR EMBL; AAFI02000150; EAL62442.1; -; Genomic_DNA.
DR RefSeq; XP_635946.1; XM_630854.1.
DR AlphaFoldDB; Q54GQ6; -.
DR SMR; Q54GQ6; -.
DR STRING; 44689.DDB0234154; -.
DR PaxDb; Q54GQ6; -.
DR EnsemblProtists; EAL62442; EAL62442; DDB_G0289993.
DR GeneID; 8627428; -.
DR KEGG; ddi:DDB_G0289993; -.
DR dictyBase; DDB_G0289993; -.
DR eggNOG; KOG0136; Eukaryota.
DR HOGENOM; CLU_014629_3_1_1; -.
DR InParanoid; Q54GQ6; -.
DR OMA; WMITQQT; -.
DR PhylomeDB; Q54GQ6; -.
DR Reactome; R-DDI-193368; Synthesis of bile acids and bile salts via 7alpha-hydroxycholesterol.
DR Reactome; R-DDI-2046106; alpha-linolenic acid (ALA) metabolism.
DR Reactome; R-DDI-389887; Beta-oxidation of pristanoyl-CoA.
DR Reactome; R-DDI-390247; Beta-oxidation of very long chain fatty acids.
DR Reactome; R-DDI-9033241; Peroxisomal protein import.
DR PRO; PR:Q54GQ6; -.
DR Proteomes; UP000002195; Chromosome 5.
DR GO; GO:0005777; C:peroxisome; ISS:UniProtKB.
DR GO; GO:0003997; F:acyl-CoA oxidase activity; ISS:UniProtKB.
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:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0033540; P:fatty acid beta-oxidation using acyl-CoA oxidase; IBA:GO_Central.
DR GO; GO:0009062; P:fatty acid catabolic process; ISS:UniProtKB.
DR GO; GO:0019395; P:fatty acid oxidation; ISS:UniProtKB.
DR GO; GO:0006091; P:generation of precursor metabolites and energy; ISS:UniProtKB.
DR GO; GO:0050665; P:hydrogen peroxide biosynthetic process; ISS:UniProtKB.
DR GO; GO:0055088; P:lipid homeostasis; IBA:GO_Central.
DR GO; GO:0006629; P:lipid metabolic process; ISS:UniProtKB.
DR GO; GO:0006693; P:prostaglandin metabolic process; ISS:UniProtKB.
DR GO; GO:0140493; P:very long-chain fatty acid beta-oxidation; ISS:UniProtKB.
DR Gene3D; 1.10.540.10; -; 1.
DR Gene3D; 2.40.110.10; -; 1.
DR InterPro; IPR029320; Acyl-CoA_ox_N.
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; 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; Fatty acid metabolism; Flavoprotein; Lipid metabolism; Oxidoreductase;
KW Peroxisome; Reference proteome.
FT CHAIN 1..700
FT /note="Peroxisomal acyl-coenzyme A oxidase 1"
FT /id="PRO_0000330929"
FT MOTIF 698..700
FT /note="Microbody targeting signal"
FT /evidence="ECO:0000255"
FT ACT_SITE 437
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P07872"
FT BINDING 147
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P07872"
FT BINDING 186
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P07872"
FT BINDING 412..417
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
SQ SEQUENCE 700 AA; 79762 MW; 3F286207CFD33958 CRC64;
MYCPKAYENE KKNEDLEFER SQSTFSVSEL NFILNNNDHN IINIKNEIKK FIDNDEIISK
PQEIHFLSRE EQYKRALYVS SKLIEIKKRF GEIGRDQYYQ SLFEEIPFVI NDIVFACAFK
SLASDEQMNR LYSKFENYQY FGSYSQTEIG HGSNVQGIET TCTFIKETGE FELNSPNLTS
TKFWIGGLGK LATHTIVFAQ LLIPSSIDGK LKNYGPHPFI LQVRSLDDHS PLPGVTVGDI
GPKLGFNSID NGFLRLDHVR IPRENMLSRF FRVNEQGEYE KPKHPKLIYA GMVGVRSSMI
ENSFVSLSRA VTIAIRYSTI RKQFKSNRLD KQEKKIIEYS NQMNRIIPYL AQTFAYFFTG
KRFSIEFDQM MKAVKHNQDT TLLSELHANS SGLKSLMTQS TSDGIESCRL SCGGHGYSQF
SGLPYLWSNY VHMSSAEGES NLLPQQTTKY LLTILRKVLS GGGGSSDTTT ADDDNKPIGK
SVKYINDEFQ SSFENINQFI QEKGLNSIIH PDSLLQLFKH RSFILIKSIA ESIQEQMSNG
NKDIPQIWSD LNVEINHCSK AHCQLYVIQS FYDQILLLSS NSSSCSSSIT TVLIQLLQTY
SIWIINSNLV DFLQDQYVEL SQIDFLKKSL INFYKLLRPN LVPLVDSFDL CNTTLGSALG
SYNGDVYSTL YKWASTQPFN KNSLPLGFNE TIKPLINSKL
