ID A0A1R3GNC3_COCAP Unreviewed; 664 AA.
AC A0A1R3GNC3;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Acyl-coenzyme A oxidase {ECO:0000256|PIRNR:PIRNR000168};
GN ORFNames=CCACVL1_24721 {ECO:0000313|EMBL:OMO59615.1};
OS Corchorus capsularis (Jute).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Malvales; Malvaceae; Grewioideae; Apeibeae; Corchorus.
OX NCBI_TaxID=210143 {ECO:0000313|EMBL:OMO59615.1, ECO:0000313|Proteomes:UP000188268};
RN [1] {ECO:0000313|EMBL:OMO59615.1, ECO:0000313|Proteomes:UP000188268}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. CVL-1 {ECO:0000313|Proteomes:UP000188268};
RC TISSUE=Whole seedling {ECO:0000313|EMBL:OMO59615.1};
RA Alam M., Haque M.S., Islam M.S., Emdad E.M., Islam M.M., Ahmed B.,
RA Halim A., Hossen Q.M.M., Hossain M.Z., Ahmed R., Khan M.M., Islam R.,
RA Rashid M.M., Khan S.A., Rahman M.S., Alam M.;
RT "Corchorus capsularis genome sequencing.";
RL Submitted (SEP-2013) 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, ECO:0000256|PIRNR:PIRNR000168}.
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:OMO59615.1}.
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DR EMBL; AWWV01013892; OMO59615.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1R3GNC3; -.
DR STRING; 210143.A0A1R3GNC3; -.
DR EnsemblPlants; OMO59615; OMO59615; CCACVL1_24721.
DR Gramene; OMO59615; OMO59615; CCACVL1_24721.
DR OMA; ICTRFSA; -.
DR OrthoDB; 5473219at2759; -.
DR Proteomes; UP000188268; 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:SF250; PEROXISOMAL ACYL-COENZYME A OXIDASE 1; 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 Peroxisome {ECO:0000256|ARBA:ARBA00023140};
KW Reference proteome {ECO:0000313|Proteomes:UP000188268}.
FT DOMAIN 17..132
FT /note="Acyl-coenzyme A oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF14749"
FT DOMAIN 479..655
FT /note="Acyl-CoA oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF01756"
FT ACT_SITE 424
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000168-1"
FT BINDING 138
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000168-2"
FT BINDING 177
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000168-2"
SQ SEQUENCE 664 AA; 74289 MW; 9D9894C3C1D7E3FB CRC64;
MEALDYHAEE RRKAEFDVEE MKIVWAGSRH AYEVSDRVAR IVASDPVFQK DNRTMLSRKD
LFKDTLKKAA HAWKRIIELR LSEEEATELR FFVDQPAYTD LHWGMFVPAI KGQGTEEQQK
KWLPMAYKMQ IIGCYAQTEL GHGSNVQGLE TTATFDPQTD EFIIHSPTLT SSKWWPGGLG
KVSTHAVVYA RLITDGQDYG VHGFIVQLRS LDDHLPLPGI TVGDIGMKFG SGAYNSMDNG
LLRFDHVQIP RDQMLMRLSQ VTREGKYMPS DVPRQLVYGT MVYVRQTIVS DASSALSKAV
CIATRYSAIR RQFGSQNGGP ETQVINYKTQ QNRLFPLLAS AYAFRFVGEW LKWLYTDVTE
RLQANDFSTL PEAHACTAGL KSITTTATAD AIEECRKLCG GHGYLSSSGL PELFAVYVPA
CTYEGDNVVL LLQVARFLMK TVSQLGSGKK PVGTTAYMGR AEHLMQCSCD VQRAEDWLNP
SVIVEAFEAR ALRMSVACAQ SLSKFSNPEE GFAELSPNLV EAAVAHCQLI VVSKFIEKLQ
QDIPGKGVKR QLEILCNVYA LYLVHKHLGD FVSTGSITPK QGALANEQLR SLYSQVRPNA
IALVDAFNYT DHFLSSILGR YDGNVYAKLY EAAWKDPLND SVVPDGYHDY VKPLLRQQLI
TARL
//
