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Database: UniProt
Entry: U7MVT7_9CORY
LinkDB: U7MVT7_9CORY
Original site: U7MVT7_9CORY 
ID   U7MVT7_9CORY            Unreviewed;       716 AA.
AC   U7MVT7;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   27-MAR-2024, entry version 45.
DE   RecName: Full=Acyl-CoA oxidase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=HMPREF1290_00402 {ECO:0000313|EMBL:ERS75333.1};
OS   Corynebacterium sp. KPL1989.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC   Corynebacteriaceae; Corynebacterium.
OX   NCBI_TaxID=1203622 {ECO:0000313|EMBL:ERS75333.1, ECO:0000313|Proteomes:UP000017102};
RN   [1] {ECO:0000313|EMBL:ERS75333.1, ECO:0000313|Proteomes:UP000017102}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KPL1989 {ECO:0000313|EMBL:ERS75333.1,
RC   ECO:0000313|Proteomes:UP000017102};
RG   The Broad Institute Genomics Platform;
RA   Earl A., Ward D., Feldgarden M., Gevers D., Jacobson B., Goguen K.,
RA   Pagano E., Lemon K.P., Young S.K., Zeng Q., Gargeya S., Fitzgerald M.,
RA   Abouelleil A., Alvarado L., Berlin A.M., Chapman S.B., Gainer-Dewar J.,
RA   Goldberg J., Gnerre S., Griggs A., Gujja S., Hansen M., Howarth C.,
RA   Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C., Pearson M.,
RA   Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sykes S., Wortman J.,
RA   Nusbaum C., Birren B.;
RT   "The Genome Sequence of Corynebacterium sp. KPL1989.";
RL   Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
CC   -!- SIMILARITY: Belongs to the acyl-CoA oxidase family.
CC       {ECO:0000256|ARBA:ARBA00006288}.
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:ERS75333.1}.
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DR   EMBL; AXLR01000001; ERS75333.1; -; Genomic_DNA.
DR   RefSeq; WP_023018506.1; NZ_KI515716.1.
DR   AlphaFoldDB; U7MVT7; -.
DR   PATRIC; fig|1203622.3.peg.388; -.
DR   eggNOG; COG1960; Bacteria.
DR   HOGENOM; CLU_014629_4_0_11; -.
DR   Proteomes; UP000017102; Unassembled WGS sequence.
DR   GO; GO:0005777; C:peroxisome; IEA:InterPro.
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; 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; 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; IPR009075; AcylCo_DH/oxidase_C.
DR   InterPro; IPR009100; AcylCoA_DH/oxidase_NM_dom_sf.
DR   PANTHER; PTHR10909:SF378; ACYL-COENZYME A OXIDASE-LIKE PROTEIN; 1.
DR   PANTHER; PTHR10909; ELECTRON TRANSPORT OXIDOREDUCTASE; 1.
DR   Pfam; PF01756; ACOX; 1.
DR   Pfam; PF00441; Acyl-CoA_dh_1; 1.
DR   Pfam; PF02770; Acyl-CoA_dh_M; 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};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   Reference proteome {ECO:0000313|Proteomes:UP000017102}.
FT   DOMAIN          188..299
FT                   /note="Acyl-CoA oxidase/dehydrogenase middle"
FT                   /evidence="ECO:0000259|Pfam:PF02770"
FT   DOMAIN          333..505
FT                   /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00441"
FT   DOMAIN          575..693
FT                   /note="Acyl-CoA oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01756"
FT   REGION          1..61
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        10..24
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        43..57
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   716 AA;  78649 MW;  D1B4AD268316C52E CRC64;
     MNRIAEFAKN LGKDSGKDSD NGVKDSGAKG AGVKDVDLET NSAKGTPEPS SPRTLPTEPD
     HSAAGELQTL LDGKAAPYRK AVRETLEEKD LKLDLNGGID AVRDRMYEHI KFLVESGESR
     HSFSKENGGS GNALAAVSGI ETIGAVNPSL TIKSGVQWGL WGGAVDNLGS ERHRHYIEKI
     QNAELLGCYA MTERGHGSNV QELETTATYD PDTHEFIINS PTDSARKVYI GNAGRDGRMA
     AVFAQLYTPG EEESHGVHCL IVPIRDEDGN PLDGVEIGDH GRKGGLLGVD NGTLLFNNVR
     VPRENLLNRF GDVEEDGTYV SPIDSRNRRF FTMLGTLIRG RITVGGAGLA ATRTASDIAI
     RYANRRRQFE GGEKGVEKRL IDYRQHRRRL LIPLARTYAL TLLQNRILER YDDMLNKQAS
     GQWSVTDPTE EQLFASREME SLAAAVKAAS TEHANKTLQE MREACGGAGY MSENLLTTLR
     ADADIYSTFE GDNTVLIQMV GKHLLTAFGR DMQDLSPWDM VKYGVETAAD TVRRRTGIRS
     GVQSVIDLVS NRDEDSLFDA GYQVKLIEDR EQAVLRSLVR RIAPARKADR AEAAEIVDKT
     QDHLIAVSWA HVDSLLMRTM VEAELELPEG SAARQVFEQV RSLFFFDLLI KHAGWYQEHN
     MLPSGRVKAA RAAINDLVDS LGPWSQVLSE AFATPKSAWN VPMLNDGGVD GGDNKA
//
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