ID   W2K3V4_PHYPR            Unreviewed;       801 AA.
AC   W2K3V4;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   27-MAR-2024, entry version 41.
DE   RecName: Full=Acyl-CoA dehydrogenase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=L917_19627 {ECO:0000313|EMBL:ETL79797.1};
OS   Phytophthora parasitica (Potato buckeye rot agent).
OC   Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC   Phytophthora.
OX   NCBI_TaxID=4792 {ECO:0000313|EMBL:ETL79797.1};
RN   [1] {ECO:0000313|EMBL:ETL79797.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CHvinca01 {ECO:0000313|EMBL:ETL79797.1};
RG   The Broad Institute Genomics Platform;
RA   Russ C., Tyler B., Panabieres F., Shan W., Tripathy S., Grunwald N.,
RA   Machado M., Johnson C.S., Arredondo F., Hong C., Coffey M., Young S.K.,
RA   Zeng Q., Gargeya S., Fitzgerald M., Abouelleil A., Alvarado L.,
RA   Chapman S.B., Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA   Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C.,
RA   Pearson M., Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sykes S.,
RA   Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Phytophthora parasitica CHvinca01.";
RL   Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
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DR   EMBL; KI682919; ETL79797.1; -; Genomic_DNA.
DR   AlphaFoldDB; W2K3V4; -.
DR   EnsemblProtists; ETL79797; ETL79797; L917_19627.
DR   VEuPathDB; FungiDB:PPTG_05779; -.
DR   Proteomes; UP000054423; 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   CDD; cd05154; ACAD10_11_N-like; 1.
DR   Gene3D; 3.90.1200.10; -; 1.
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; 1.
DR   InterPro; IPR041726; ACAD10_11_N.
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; IPR037069; AcylCoA_DH/ox_N_sf.
DR   InterPro; IPR009100; AcylCoA_DH/oxidase_NM_dom_sf.
DR   InterPro; IPR002575; Aminoglycoside_PTrfase.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   PANTHER; PTHR48083:SF13; ACYL-COA DEHYDROGENASE FAMILY MEMBER 11; 1.
DR   PANTHER; PTHR48083; MEDIUM-CHAIN SPECIFIC ACYL-COA DEHYDROGENASE, MITOCHONDRIAL-RELATED; 1.
DR   Pfam; PF00441; Acyl-CoA_dh_1; 1.
DR   Pfam; PF02770; Acyl-CoA_dh_M; 1.
DR   Pfam; PF01636; APH; 1.
DR   SUPFAM; SSF47203; Acyl-CoA dehydrogenase C-terminal domain-like; 1.
DR   SUPFAM; SSF56645; Acyl-CoA dehydrogenase NM domain-like; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
PE   4: Predicted;
KW   FAD {ECO:0000256|ARBA:ARBA00022827};
KW   Fatty acid metabolism {ECO:0000256|ARBA:ARBA00022832};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00023098}.
FT   DOMAIN          33..267
FT                   /note="Aminoglycoside phosphotransferase"
FT                   /evidence="ECO:0000259|Pfam:PF01636"
FT   DOMAIN          528..628
FT                   /note="Acyl-CoA oxidase/dehydrogenase middle"
FT                   /evidence="ECO:0000259|Pfam:PF02770"
FT   DOMAIN          645..793
FT                   /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00441"
SQ   SEQUENCE   801 AA;  89450 MW;  4A27AA3AEA5D93F0 CRC64;
     MTQQDVRQAL DAPALTAYIH SRLGASHGAI ASIRQFQHGQ SNPTYLLTMA GSKAKWVLRK
     KPHGQILPSA HAVEREYRVL EALEHTEVPV PRAVLLCEDP KVIGTPFYLM EYVHGRIFQD
     PSLPGIKPMY RYAMYSSALD ALVKLHELDY KKIGLADFGR PEKYCHRVVA RWSRQVQGSH
     KVFAEAGVKE NPKMTQLQHW LEQNADDAEK ATTRAEGASI VHGDFRIDNM IFHPTEPRVL
     AILDWELCTI GNPFSDVATL ASTYRLPLDN SNTIMTPGLS DAPLKKLGIP SESDLLLGYC
     RRARRFPLTT QTWNFFMGMV VYRFAAICHG VYARALLGNA SSANAACAKT TMDRLLAMSD
     DIMDASADIY PEPELEHILP FPIRPNALQI YKKLLKFCQN RVYPAEYVHI AQIAKAREEG
     REWQIVPPII DELKAEAKAL GLWNLFLPEC VVPALDGNGP DVNYGGDLTN LEYGLMCEVM
     GRSLVLAPEV FNCSAPDTGN MEILTRFCTV EQKHKWLVPL LKGEIRSCFA MTEKRVASSD
     ATNIETSIVR DEQRQEYVIN GHKTYISGAG DPRCKIIVLM GKHSERANES SFKQQSMILV
     PMDTPGVQVV RPMHVFGYDD APHGHMEMLF KDVRVPFSNV LLGEGRGFEI AQARLGPGRI
     HHCMRAIGAA ERCLELMVQR AKTRTAFKQL LAENPLVCSQ IAKSRCELDS ARLLTLQAAH
     QMDKHGNKVA QQAIAMIKIV APNMALDVCD RAIQIHGAAG VSQDFILSYL YAALRTLRIA
     DGPDEVHMRT IAKLELSHSK L
//