ID A0A498LRS5_LABRO Unreviewed; 791 AA.
AC A0A498LRS5;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE SubName: Full=Acyl-coenzyme A oxidase {ECO:0000313|EMBL:RXN09444.1};
GN ORFNames=ROHU_011080 {ECO:0000313|EMBL:RXN09444.1};
OS Labeo rohita (Indian major carp) (Cyprinus rohita).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Cyprinidae; Labeoninae; Labeonini; Labeo.
OX NCBI_TaxID=84645 {ECO:0000313|EMBL:RXN09444.1, ECO:0000313|Proteomes:UP000290572};
RN [1] {ECO:0000313|EMBL:RXN09444.1, ECO:0000313|Proteomes:UP000290572}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DASCIFA01 {ECO:0000313|EMBL:RXN09444.1};
RC TISSUE=Testis {ECO:0000313|EMBL:RXN09444.1};
RA Das P., Kushwaha B., Joshi C.G., Kumar D., Nagpure N.S., Sahoo L.,
RA Das S.P., Bit A., Patnaik S., Meher P.K., Jayasankar P., Koringa P.G.,
RA Patel N.V., Hinsu A.T., Kumar R., Pandey M., Agarwal S., Srivastava S.,
RA Singh M., Iquebal M.A., Jaiswal S., Angadi U.B., Kumar N., Raza M.,
RA Shah T.M., Rai A., Jena J.K.;
RT "Draft genome sequence of Rohu Carp (Labeo rohita).";
RL Submitted (MAR-2018) 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:RXN09444.1}.
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DR EMBL; QBIY01013282; RXN09444.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A498LRS5; -.
DR STRING; 84645.A0A498LRS5; -.
DR Proteomes; UP000290572; 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 InterPro; IPR015040; Bcl-x_interacting_BH3_dom.
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 Pfam; PF08945; Bclx_interact; 1.
DR SUPFAM; SSF47203; Acyl-CoA dehydrogenase C-terminal domain-like; 2.
DR SUPFAM; SSF56645; Acyl-CoA dehydrogenase NM domain-like; 1.
PE 1: Evidence at protein level;
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Proteomics identification {ECO:0007829|PeptideAtlas:A0A498LRS5};
KW Reference proteome {ECO:0000313|Proteomes:UP000290572}.
FT DOMAIN 112..219
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 250..411
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
FT DOMAIN 457..597
FT /note="Acyl-CoA oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF01756"
FT DOMAIN 727..751
FT /note="Bcl-x interacting BH3"
FT /evidence="ECO:0000259|Pfam:PF08945"
FT REGION 618..675
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 657..675
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 791 AA; 88802 MW; B86BB0EE92DB7865 CRC64;
MVLLSMDQKH PSSLARYLDG EFWEIRDAFR DAISKCELFQ SSSYELTLDQ RRDLTAERLH
HLLSLPFMKE HLRNQLKEKQ KDFTNKSLSF TEIICSADMA TGVKELEFTG MFAMTERGHG
SNVRGIITEA RYDQSTQEFV IHTPSEDAQK MYIGNAMKGN NAAVFAQLII NGECQGPHCF
IVPIRDQNGV MWPGVTTIDM KHKEGLNGVD NGILIFNNVR IPRENLLRKF GSVSADGLYS
SPILNKSSRF NAMLAALTPT RLCLAVQTMA AMKLGLIIAV RYSHSRRQFG PKDQDEVKII
EHQTQSLRLM PHLAAALALT FTTRYTAGLM DDALCQGQDL QSNRALQALI AGLKAYSTWE
NVACLQDCRE CTGGMGFMME NRIPSLKCDS DVFVTFEGDN MVMLQVVVRE LLTQYTKQMG
NNLVMGLIRN WTTSLSDSLR TSFLGFSMDK VGDLMFLLKA VSYRERVLQR SLASRLYTKV
EKNKEEFFMA WNACLHHVTA LAMAHIHRVT LEQFALAVQE CHIKEDRALL TKFCLLHGTS
LVYQERAWYL EHNYLTPNTS RQIRNQLLEL CRSVKDDALK VVDDFNIPSC CIQAPIAGVA
NPRAEWAFYP QPQSKLEQTL ANGPASRGSG ESAGGGAVLR SEHFDFPQPS DGDPLRGGIS
MSNSHQSRSP MCRTFSRSSS GYFSVDSDSV PGSPLMPNIS EAQDGQNDEV WFAEPSHQRV
QMEAPDEAMG REMAVARELR RIGDEFNRLY CQGAGAGGNN AAQLRAPNEH AIVVWMNVLI
GHVVQFFLRR R
//
