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
//