ID A0A423V9M2_9PEZI Unreviewed; 437 AA.
AC A0A423V9M2;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE RecName: Full=Acyl-CoA dehydrogenase/oxidase C-terminal domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=VMCG_10609 {ECO:0000313|EMBL:ROV87583.1};
OS Valsa malicola.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Diaporthales; Valsaceae; Valsa.
OX NCBI_TaxID=356882 {ECO:0000313|EMBL:ROV87583.1, ECO:0000313|Proteomes:UP000283895};
RN [1] {ECO:0000313|EMBL:ROV87583.1, ECO:0000313|Proteomes:UP000283895}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=03-1 {ECO:0000313|EMBL:ROV87583.1,
RC ECO:0000313|Proteomes:UP000283895};
RA Yin Z., Huang L.;
RT "Host preference determinants of Valsa canker pathogens revealed by
RT comparative genomics.";
RL Submitted (SEP-2015) 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 -!- 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:ROV87583.1}.
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DR EMBL; LKEA01000092; ROV87583.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A423V9M2; -.
DR STRING; 356882.A0A423V9M2; -.
DR Proteomes; UP000283895; 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; cd00567; ACAD; 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; 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; PTHR43884:SF40; -; 1.
DR PANTHER; PTHR43884; ACYL-COA DEHYDROGENASE; 1.
DR Pfam; PF00441; Acyl-CoA_dh_1; 1.
DR Pfam; PF02771; Acyl-CoA_dh_N; 1.
DR SUPFAM; SSF47203; Acyl-CoA dehydrogenase C-terminal domain-like; 1.
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:ARBA00022827};
KW Reference proteome {ECO:0000313|Proteomes:UP000283895}.
FT DOMAIN 7..121
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 269..421
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
SQ SEQUENCE 437 AA; 46621 MW; B14BF2CBF85EE896 CRC64;
MIDFTLTESQ QALRHNAAAF AQAHLKEAHL TYAQHTTQKA RFRSTRPIYA AAVKKGLIRG
QIPTTLGGGA QGLVDAAILI EEFFAVDPSA ALTILGTGLG LTPLILVGSE EQRGRLLGKF
LACGDGDDDD GAGARLASFV HSEPGGTANW LERGGKGLAT TARREGDEWV INGEKLWTTN
SGGWDGKGAD LQCVVCRNSP DGGPPDPTRD PAQDILILLV TREIIAANKP EAYEVLGEPE
LTGFPSTSGP HSRFQELHVP HANLLCPPGQ GAAVVEQTFG SSAALVGAMG VGIMRATFEA
ALEYAKDQTR GGSVPLLERQ SVGDLLIDIK MRIETSRLLT WKALHAIENG PGGWKARLEL
ALEAKIHSSE AAVQSVVDAM KAVGIASYAK DQPFSRLLND AMALPIFDGG NVGVRRRQIE
RIFQDTSYQP WAATYGD
//
