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Database: UniProt
Entry: A0A317SXJ2_9PEZI
LinkDB: A0A317SXJ2_9PEZI
Original site: A0A317SXJ2_9PEZI 
ID   A0A317SXJ2_9PEZI        Unreviewed;       389 AA.
AC   A0A317SXJ2;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   27-MAR-2024, entry version 13.
DE   SubName: Full=Acyl-CoA dehydrogenase NM domain-like protein {ECO:0000313|EMBL:PWW78136.1};
GN   ORFNames=C7212DRAFT_357206 {ECO:0000313|EMBL:PWW78136.1};
OS   Tuber magnatum (white Piedmont truffle).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Pezizomycetes;
OC   Pezizales; Tuberaceae; Tuber.
OX   NCBI_TaxID=42249 {ECO:0000313|EMBL:PWW78136.1, ECO:0000313|Proteomes:UP000246991};
RN   [1] {ECO:0000313|EMBL:PWW78136.1, ECO:0000313|Proteomes:UP000246991}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=091103-1 {ECO:0000313|EMBL:PWW78136.1};
RA   Murat C., Payen T., Noel B., Kuo A., Martin F.M.;
RT   "Genomes of Pezizomycetes fungi and the evolution of truffles.";
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         ECO:0000256|RuleBase:RU362125};
CC   -!- SIMILARITY: Belongs to the acyl-CoA dehydrogenase family.
CC       {ECO:0000256|ARBA:ARBA00009347, ECO:0000256|RuleBase:RU362125}.
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:PWW78136.1}.
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DR   EMBL; PYWC01000017; PWW78136.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A317SXJ2; -.
DR   STRING; 42249.A0A317SXJ2; -.
DR   Proteomes; UP000246991; Unassembled WGS sequence.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:UniProtKB-UniRule.
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; 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; 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: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; 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, ECO:0000256|RuleBase:RU362125};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW   ECO:0000256|RuleBase:RU362125};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU362125};
KW   Reference proteome {ECO:0000313|Proteomes:UP000246991}.
FT   DOMAIN          17..143
FT                   /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02771"
FT   DOMAIN          147..249
FT                   /note="Acyl-CoA oxidase/dehydrogenase middle"
FT                   /evidence="ECO:0000259|Pfam:PF02770"
FT   DOMAIN          294..354
FT                   /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00441"
SQ   SEQUENCE   389 AA;  42935 MW;  4DC700DF3634C3A5 CRC64;
     MTTYQIPSLV ASKVSPSAHA LLQKVHHFVE TECIPADAVF DAQQPTDPAK RFLNTYPTII
     DMLKARAREQ GLWNLFLSQK HYPEGVPLTN LEYGLMAEIM GRSLIASEAM NCSAPDTGNM
     EVLAKYGSSA QKAQWLTPLL EGKIRSAFVM TERHRASADA KNINLEIARQ GNEYILNGTK
     WWSSGAGDPR CKLYLVMGKS DASNPNPYKQ QSVVIVPAGT PGVQVRRTLS VYGYDDAPHG
     HCEIAFTDVR VPLENMVLGP GRGFEIIQGR LGPGRIHHCM RSIDNSDAKG AMSFIAQAKV
     YVPNMSLAVI DRAVQAHGAA GVSQDFPLAR MWAHQRTLRI ADGPDEVHLN QLGRTENTRS
     GEIEDKIAMQ TKKTQELMRE FGIQVRANL
//
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