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Database: UniProt
Entry: A0A1B8ER96_9PEZI
LinkDB: A0A1B8ER96_9PEZI
Original site: A0A1B8ER96_9PEZI 
ID   A0A1B8ER96_9PEZI        Unreviewed;       449 AA.
AC   A0A1B8ER96;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:OBT73822.1};
GN   ORFNames=VF21_06716 {ECO:0000313|EMBL:OBT73822.1};
OS   Pseudogymnoascus sp. 05NY08.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX   NCBI_TaxID=1622149 {ECO:0000313|EMBL:OBT73822.1, ECO:0000313|Proteomes:UP000092096};
RN   [1] {ECO:0000313|EMBL:OBT73822.1, ECO:0000313|Proteomes:UP000092096}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=05NY08 {ECO:0000313|EMBL:OBT73822.1,
RC   ECO:0000313|Proteomes:UP000092096};
RA   Palmer J.M., Drees K.P., Foster J.T., Lindner D.L.;
RT   "Comparative genomics of Pseudogymnoascus destructans, the fungus causing
RT   white-nose syndrome of bats.";
RL   Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000092096}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=05NY08 {ECO:0000313|Proteomes:UP000092096};
RX   PubMed=29295979; DOI=10.1038/s41467-017-02441-z;
RA   Palmer J.M., Drees K.P., Foster J.T., Lindner D.L.;
RT   "Extreme sensitivity to ultraviolet light in the fungal pathogen causing
RT   white-nose syndrome of bats.";
RL   Nat. Commun. 9:35-35(2018).
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}.
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DR   EMBL; KV458855; OBT73822.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1B8ER96; -.
DR   STRING; 1622149.A0A1B8ER96; -.
DR   OrthoDB; 276350at2759; -.
DR   Proteomes; UP000092096; 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:UP000092096}.
FT   DOMAIN          15..140
FT                   /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02771"
FT   DOMAIN          144..246
FT                   /note="Acyl-CoA oxidase/dehydrogenase middle"
FT                   /evidence="ECO:0000259|Pfam:PF02770"
FT   DOMAIN          258..409
FT                   /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00441"
SQ   SEQUENCE   449 AA;  49512 MW;  3F188DC25CC179A5 CRC64;
     MSSRIPIIAQ PFVSEKAKQT LDIVRKFVEE RCIPVDAVFH AQIPVGETRW DSYPKIIDDL
     KAEARELGLW NMFLAKGHYK ESPGFTNLEY GLMAEWLGRS RTASEACNCA APDTGNMEVL
     AKYGNDAQKK EWLGPLMAGK IRSAFLMTEP AIASSDATNI EMKMERDGDH YVLNGSKWWS
     SGAGDPRCQV YIVMAKSDPT NKDKYRQQSV ILVPASAKGI TIHRMLSVYG YDDAPHGHAH
     ITFENVRVPV SQIVLGPGRG FEIIQGRLGP GRIHHAMRSI GAAENALDWM LMRINDPKKT
     PFGKQLKEHG VIIEWVARSR IEIDAARLVV LNAAIQIDAG GAKSALREIA EAKVLVPNMA
     LAVIDRAVQS FGAAGVCQDT PLANSWAGIR TLKLADGPDE VHLAQLGKNE NKRNAEVTAL
     ITRQRETSAK LFEKYGVKHV QPGPTKSRM
//
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