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Database: UniProt
Entry: A0A1R1I9U8_9ACTN
LinkDB: A0A1R1I9U8_9ACTN
Original site: A0A1R1I9U8_9ACTN 
ID   A0A1R1I9U8_9ACTN        Unreviewed;       654 AA.
AC   A0A1R1I9U8;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   RecName: Full=Acyl-CoA oxidase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=BJN44_09290 {ECO:0000313|EMBL:OMG55541.1};
OS   Tessaracoccus sp. ZS01.
OC   Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC   Propionibacteriaceae; Tessaracoccus.
OX   NCBI_TaxID=1906324 {ECO:0000313|EMBL:OMG55541.1, ECO:0000313|Proteomes:UP000187142};
RN   [1] {ECO:0000313|EMBL:OMG55541.1, ECO:0000313|Proteomes:UP000187142}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ZS01 {ECO:0000313|EMBL:OMG55541.1,
RC   ECO:0000313|Proteomes:UP000187142};
RA   Salah Z., Rout S.P., Humphreys P.N.;
RT   "Range of isolates obtained from hyperalkaline sediments.";
RL   Submitted (OCT-2016) 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 dehydrogenase family.
CC       {ECO:0000256|ARBA:ARBA00009347}.
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:OMG55541.1}.
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DR   EMBL; MTHC01000008; OMG55541.1; -; Genomic_DNA.
DR   RefSeq; WP_076061973.1; NZ_PQFE01000008.1.
DR   AlphaFoldDB; A0A1R1I9U8; -.
DR   STRING; 1906324.BJN44_09290; -.
DR   OrthoDB; 1144545at2; -.
DR   Proteomes; UP000187142; 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; 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; 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; IPR013786; AcylCoA_DH/ox_N.
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   Pfam; PF01756; ACOX; 1.
DR   Pfam; PF00441; Acyl-CoA_dh_1; 1.
DR   Pfam; PF02770; Acyl-CoA_dh_M; 1.
DR   Pfam; PF02771; Acyl-CoA_dh_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};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000187142}.
FT   DOMAIN          34..125
FT                   /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02771"
FT   DOMAIN          132..241
FT                   /note="Acyl-CoA oxidase/dehydrogenase middle"
FT                   /evidence="ECO:0000259|Pfam:PF02770"
FT   DOMAIN          275..436
FT                   /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00441"
FT   DOMAIN          496..626
FT                   /note="Acyl-CoA oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01756"
SQ   SEQUENCE   654 AA;  71925 MW;  07DDC8CFAA2EB1C7 CRC64;
     MTITPTGEGL RRALDGPFHA LKQRWRNEVS ADDVVRDTDL TIEEAREWTF DRLKRLTQRE
     FVTAGFPAAQ GGTGTSAESV ANFEMMAMGD LSLTIKSGVQ HGLFGGAITN LGTQWHHETF
     LPGAIDASLP GCFAMTELGH GSDVQSIETS ITWDAETGEL VVHSPSPTAA KAYIGNVARD
     GRMAAVFGQL WVNDVHHGVH VALVPIRDEQ GNPMPGVTIG DHGHKGGLLG VDNGTLMFEH
     VRVPRRMLLD RYGGVDETGD YHSPIESQNA RFFTMLGTLV RGRICVGGGA ASATRKALSI
     AVRYANRRRQ FRQPGLGEEI LLMDYLQHQR RLLPDVARAY AYGFAQNEVS LQLQRIMEAD
     GSDPQAAREL ETRAAGMKAV LTRWANDTLQ ECREASGGAG YMSDNGITLA RQDADIFATF
     EGDNTVLLQL VAKALLLDYK STWGDMDLAG TAQKTAKLLG GRFLERTTAR SAIDRLVATA
     KRRPEAEQLR ARGWHVEMFE YRERHMVEGL AQRMRAAGRA KSFDAINACQ PHMIEAAKAH
     VDRVVLEAFI QGIEECGDDY VKALLIKVCD LYALATIETN RAWFLEHEVF DAKRSKTITS
     TVDALCGELR PQSLALAEGL GVPEEWLVHP RRAVPPMMQA EAPVAEAEEL RRVS
//
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