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
//