ID A0A084WHR2_ANOSI Unreviewed; 670 AA.
AC A0A084WHR2;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=Acyl-coenzyme A oxidase {ECO:0000256|PIRNR:PIRNR000168};
GN ORFNames=ZHAS_00017769 {ECO:0000313|EMBL:KFB49756.1};
OS Anopheles sinensis (Mosquito).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Anophelinae; Anopheles.
OX NCBI_TaxID=74873 {ECO:0000313|EMBL:KFB49756.1};
RN [1] {ECO:0000313|EMBL:KFB49756.1, ECO:0000313|Proteomes:UP000030765}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=24438588; DOI=10.1186/1471-2164-15-42;
RA Zhou D., Zhang D., Ding G., Shi L., Hou Q., Ye Y., Xu Y., Zhou H.,
RA Xiong C., Li S., Yu J., Hong S., Yu X., Zou P., Chen C., Chang X., Wang W.,
RA Lv Y., Sun Y., Ma L., Shen B., Zhu C.;
RT "Genome sequence of Anopheles sinensis provides insight into genetics basis
RT of mosquito competence for malaria parasites.";
RL BMC Genomics 15:42-42(2014).
RN [2] {ECO:0000313|EnsemblMetazoa:ASIC017769-PA}
RP IDENTIFICATION.
RG EnsemblMetazoa;
RL Submitted (MAY-2020) to UniProtKB.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- PATHWAY: Lipid metabolism; peroxisomal fatty acid beta-oxidation.
CC {ECO:0000256|ARBA:ARBA00004846}.
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 EMBL; ATLV01023873; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ATLV01023874; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ATLV01023875; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; KE525347; KFB49756.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A084WHR2; -.
DR STRING; 74873.A0A084WHR2; -.
DR EnsemblMetazoa; ASIC017769-RA; ASIC017769-PA; ASIC017769.
DR VEuPathDB; VectorBase:ASIC017769; -.
DR VEuPathDB; VectorBase:ASIS009981; -.
DR OMA; VAMIEHH; -.
DR Proteomes; UP000030765; 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:0009058; P:biosynthetic process; IEA:UniProt.
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; 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_sf.
DR PANTHER; PTHR10909; ELECTRON TRANSPORT OXIDOREDUCTASE; 1.
DR PANTHER; PTHR10909:SF250; PEROXISOMAL ACYL-COENZYME A OXIDASE 1; 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; 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|ARBA:ARBA00022827, ECO:0000256|PIRNR:PIRNR000168};
KW Fatty acid metabolism {ECO:0000256|ARBA:ARBA00022832};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW ECO:0000256|PIRNR:PIRNR000168};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW Peroxisome {ECO:0000256|ARBA:ARBA00023140};
KW Reference proteome {ECO:0000313|Proteomes:UP000030765}.
FT DOMAIN 20..146
FT /note="Acyl-coenzyme A oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF14749"
FT DOMAIN 149..258
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 486..667
FT /note="Acyl-CoA oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF01756"
FT ACT_SITE 434
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000168-1"
FT BINDING 152
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000168-2"
FT BINDING 191
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000168-2"
SQ SEQUENCE 670 AA; 75262 MW; EB0AF205B77DA58E CRC64;
MPSSSVNKDL QAERDKCSFD KNEFTLWWVG GKERLKEKED LEDFFLNDPE LQEKVPLHFL
SHKELYEESV RKATVAFRKV RKMQEMGQDG VDNYSALLGG LLGTGILKQG NPLTVHYVMF
LPAILGHGTP EQQAEWFGRA WNCEIIGTYA QTELGHGTFL RGLETTATYD EKTKEFVLHS
PTLTAYKWWP GGLAHTANYC VVMAQLFSKG KCHGIQPFIV QLRDEESHMP LKGITIGEIG
NKLGMNGVNN GFLGFDQVRI PRKNMLMKNA KLLEDGTFVK PPSQALTYGT MMFVRVVICR
DMAAYLSKAV TIAIRYSAVR RQSHINPDQP EVQVIDHLTQ QYKLFPALSK SIIFKLASDN
LWEMYNQVTS ELDKGDLERL PELHAIACCL KAITTADAAT GVEVCRLACG GHGYMTCSNF
YGTYGMVTAA CTYEGENTVL LLQTARYLLK AWQQAKRGQE LVPTVQYLAR FLSNNNRRVD
WDDSIDGIIR SLQTVAAGKL RLAAEHIEQR QKAGATQEEA TNQTSIELAR TADAHCRAFL
VQSGREMIEK ACQTASPELA RVLRTLYFLY AYDEALKALG DLLRFTTISE SDINRLQAKL
EATLAELRPN AVGIVDSFDL PDDVLGSPLG AYDGNVYERL YEEAKKSPLN QEPVNQSFHK
YLKPFMKSNL
//
