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Database: UniProt
Entry: C5KU68_PERM5
LinkDB: C5KU68_PERM5
Original site: C5KU68_PERM5 
ID   C5KU68_PERM5            Unreviewed;       905 AA.
AC   C5KU68;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   27-MAR-2024, entry version 54.
DE   SubName: Full=Acyl-coa dehydrogenase, putative {ECO:0000313|EMBL:EER12110.1};
GN   ORFNames=Pmar_PMAR019216 {ECO:0000313|EMBL:EER12110.1};
OS   Perkinsus marinus (strain ATCC 50983 / TXsc).
OC   Eukaryota; Sar; Alveolata; Perkinsozoa; Perkinsea; Perkinsida; Perkinsidae;
OC   Perkinsus.
OX   NCBI_TaxID=423536 {ECO:0000313|Proteomes:UP000007800};
RN   [1] {ECO:0000313|EMBL:EER12110.1, ECO:0000313|Proteomes:UP000007800}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 50983 / TXsc {ECO:0000313|Proteomes:UP000007800};
RA   El-Sayed N., Caler E., Inman J., Amedeo P., Hass B., Wortman J.;
RL   Submitted (JUL-2008) 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}.
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DR   EMBL; GG676180; EER12110.1; -; Genomic_DNA.
DR   RefSeq; XP_002780315.1; XM_002780269.1.
DR   AlphaFoldDB; C5KU68; -.
DR   EnsemblProtists; EER12110; EER12110; Pmar_PMAR019216.
DR   GeneID; 9061098; -.
DR   InParanoid; C5KU68; -.
DR   OrthoDB; 275353at2759; -.
DR   Proteomes; UP000007800; Unassembled WGS sequence.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0016627; F:oxidoreductase activity, acting on the CH-CH group of donors; IEA:InterPro.
DR   Gene3D; 1.10.540.10; Acyl-CoA dehydrogenase/oxidase, N-terminal domain; 2.
DR   Gene3D; 2.40.110.10; Butyryl-CoA Dehydrogenase, subunit A, domain 2; 2.
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; 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; PTHR48083:SF20; LONG-CHAIN SPECIFIC ACYL-COA DEHYDROGENASE, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR48083; MEDIUM-CHAIN SPECIFIC ACYL-COA DEHYDROGENASE, MITOCHONDRIAL-RELATED; 1.
DR   Pfam; PF00441; Acyl-CoA_dh_1; 2.
DR   Pfam; PF02770; Acyl-CoA_dh_M; 2.
DR   Pfam; PF02771; Acyl-CoA_dh_N; 2.
DR   SUPFAM; SSF47203; Acyl-CoA dehydrogenase C-terminal domain-like; 2.
DR   SUPFAM; SSF56645; Acyl-CoA dehydrogenase NM domain-like; 2.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils}; FAD {ECO:0000256|ARBA:ARBA00022827};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007800}.
FT   DOMAIN          39..162
FT                   /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02771"
FT   DOMAIN          166..261
FT                   /note="Acyl-CoA oxidase/dehydrogenase middle"
FT                   /evidence="ECO:0000259|Pfam:PF02770"
FT   DOMAIN          273..429
FT                   /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00441"
FT   DOMAIN          490..613
FT                   /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02771"
FT   DOMAIN          617..712
FT                   /note="Acyl-CoA oxidase/dehydrogenase middle"
FT                   /evidence="ECO:0000259|Pfam:PF02770"
FT   DOMAIN          724..880
FT                   /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00441"
FT   COILED          427..461
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   905 AA;  100688 MW;  F90A11A80C36E7CD CRC64;
     MSMIQQAKRM GVNTEVFGDA SPFGDPNWYQ SYNSPYYDDS HKRLRAFMRT LVEEKLMPHV
     HEWDENLEIP REVHKMLGQS GINVLAMGHP YPVEYQSPPD VLKGVPLDTF HELVLSDELA
     RAGSGGLAWG LVGGLTIGLP PVLRFGPKAM RDRIVPECLS GEKIICLAIT EPTAGSDVAN
     IRCSAKKSSC GKYYIVNGEK KWITNGIWAD YFTVAVRTGG PGMDGISLLL IEKTMPGVTT
     RRMKCSGVWS SGTTFISFDD VKVPIENLIG KENKGFKCIM HNFNHERLAL CALTNRFARV
     CYEEALKHAN KRKTFGKTLV QHPVIRFKLG EMARQIEATH AWVEQVAYQV GTMHPLEANM
     KLGGVTALLK VQCTKVFEYC ARESAQIFGG LSYSRGGVGE KVERLNREVR AMAVPGGSEE
     IMLDLGVKQM SKLAEMAKVL VEQAEQENAA NKKQMAMARS MGVNTDVFGD ANAFGDPYWY
     QAGNSPFYNE SHKKLREYVR DLFEKEVLPH VFEWDENLEI PREVHRRMGA LGLTSLAMGH
     PYPVQYGGIP KFLEGVKIDV FHELIVSDEL CRCGSGGVAW GLVGGLTIGL PPVLRFGPKA
     MRDRIVPECL SGEKIICLAI TEPTAGSDVA NIRCSAKKSS CGKYYIVNGE KKWITNGIWA
     DYFTVAVRTG GPGMDGISLL LIEKTMPGVT TRRMKCSGVW SSGTTFISFD DVKVPIENLI
     GKENKGFKCI MHNFNHERFA LCAQTNRFAR VCYEEALKHA HRRKTFGKPL IQHQVIRWKL
     AEMSRLIEAT HAWLENVAYQ LSTMHPLEAN MKLGGVTALL KVQCTKVFEY CARESAQIFG
     GLSYSRGGVG EKVERLNREV RAMAVPGGSE EIMLDLGVRQ MRKLAEMAKT LVAEDNQTNE
     AASRL
//
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