ID A0A068RK12_9FUNG Unreviewed; 679 AA.
AC A0A068RK12;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-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=LCOR_01696.1 {ECO:0000313|EMBL:CDH49972.1};
OS Lichtheimia corymbifera JMRC:FSU:9682.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Lichtheimiaceae; Lichtheimia.
OX NCBI_TaxID=1263082 {ECO:0000313|EMBL:CDH49972.1, ECO:0000313|Proteomes:UP000027586};
RN [1] {ECO:0000313|EMBL:CDH49972.1, ECO:0000313|Proteomes:UP000027586}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JMRC:FSU:9682 {ECO:0000313|Proteomes:UP000027586};
RA Schwartze V.U., Winter S., Shelest E., Marcet-Houben M., Horn F.,
RA Wehner S., Hoffmann K., Riege K., Sammeth M., Nowrousian M., Valiante V.,
RA Linde J., Jacobsen I.D., Marz M., Brakhage A.A., Gabaldon T., Bocker S.,
RA Voigt K.;
RT "Gene expansion shapes genome architecture in the human pathogen
RT Lichtheimia corymbifera: an evolutionary genomics analysis in the ancient
RT terrestrial Mucorales (Mucoromycotina).";
RL Submitted (AUG-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:CDH49972.1}.
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DR EMBL; CBTN010000005; CDH49972.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A068RK12; -.
DR STRING; 1263082.A0A068RK12; -.
DR VEuPathDB; FungiDB:LCOR_01696.1; -.
DR OrthoDB; 5777at2759; -.
DR UniPathway; UPA00661; -.
DR Proteomes; UP000027586; Unassembled WGS sequence.
DR GO; GO:0005777; C:peroxisome; IEA:UniProtKB-SubCell.
DR GO; GO:0003997; F:acyl-CoA oxidase activity; IEA:UniProtKB-EC.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0033540; P:fatty acid beta-oxidation using acyl-CoA oxidase; IEA:UniProtKB-UniPathway.
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:UP000027586}.
FT DOMAIN 25..138
FT /note="Acyl-coenzyme A oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF14749"
FT DOMAIN 490..664
FT /note="Acyl-CoA oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF01756"
FT ACT_SITE 431
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000168-1"
FT BINDING 145
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000168-2"
FT BINDING 184
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000168-2"
SQ SEQUENCE 679 AA; 74457 MW; 3C067B4AFC4AB9DD CRC64;
MANSNQLQQS VIDLNAARQK ATFPVDLLTT FIRGGPEALA KRQQIRQILE NEPAIDSSRA
AFQSRQEQLA DSIVAARRMI EIAEERNMSF EEYLQMIAIS EYPTPLTLNY GAFIPVIQSQ
GTDEQIAKWL SASKRHAILG CYAQTELSHG SNVVGLQTTA TFDEATDEFI INSPDITAAK
WWIGGLGVAA THAVLQAQLI LKGKNYGPHI FIVPIRSPVD HKPVKGVTVG DIGPKAYGGF
SVTDNGFAFF DYVRIPRDNM LMRFAKVSKS GEYTPPVHSK LSYGSMVKLR VGIVSDAGWR
LARACTVAVR YCTMRRQFNA TAAADGLESQ VIHYSSVKHR LFPLIASAYA LIVGGMNLGD
DFNLMTEQLA RQDAHMLPEM HITSCALKVW GARRGSEGIE EARKTMGGHG FSVFSGVSEQ
FANFVPANTY EGENFVLCQQ VGRALLKQIK NLASGKDVNL KTVDYLNLLK QGDLTQPVAL
NGDASSLLDS NTQLAILGTR AARLVANLAK KVQSGRAWSD LNLECWEICL AHAEYHLLQQ
LVNKVHQLQS SSQYSALAPV IKSIADLFFL SLAANTALAT LVTTQTIAPT TAELVQDEYH
HALNNIADNA VGLTDAFGFT DKELNTALGR KEGNPYGTLW DVVQKNPVNS EQGKQHFGEL
MKTITHRKDN LSYIKAAKL
//
