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Database: UniProt
Entry: G3J2W9_CORMM
LinkDB: G3J2W9_CORMM
Original site: G3J2W9_CORMM 
ID   G3J2W9_CORMM            Unreviewed;       431 AA.
AC   G3J2W9;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   27-MAR-2024, entry version 42.
DE   SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:EGX97248.1};
GN   ORFNames=CCM_01908 {ECO:0000313|EMBL:EGX97248.1};
OS   Cordyceps militaris (strain CM01) (Caterpillar fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Cordycipitaceae; Cordyceps.
OX   NCBI_TaxID=983644 {ECO:0000313|EMBL:EGX97248.1, ECO:0000313|Proteomes:UP000001610};
RN   [1] {ECO:0000313|EMBL:EGX97248.1, ECO:0000313|Proteomes:UP000001610}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CM01 {ECO:0000313|EMBL:EGX97248.1,
RC   ECO:0000313|Proteomes:UP000001610};
RX   PubMed=22112802; DOI=10.1186/gb-2011-12-11-r116;
RA   Zheng P., Xia Y., Xiao G., Xiong C., Hu X., Zhang S., Zheng H., Huang Y.,
RA   Zhou Y., Wang S., Zhao G.P., Liu X., St Leger R.J., Wang C.;
RT   "Genome sequence of the insect pathogenic fungus Cordyceps militaris, a
RT   valued traditional Chinese medicine.";
RL   Genome Biol. 12:RESEARCH116.1-RESEARCH116.21(2011).
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; JH126399; EGX97248.1; -; Genomic_DNA.
DR   RefSeq; XP_006667125.1; XM_006667062.1.
DR   AlphaFoldDB; G3J2W9; -.
DR   STRING; 983644.G3J2W9; -.
DR   GeneID; 18163937; -.
DR   KEGG; cmt:CCM_01908; -.
DR   VEuPathDB; FungiDB:CCM_01908; -.
DR   eggNOG; KOG0140; Eukaryota.
DR   HOGENOM; CLU_018204_4_1_1; -.
DR   InParanoid; G3J2W9; -.
DR   OMA; GLFTWET; -.
DR   OrthoDB; 1820620at2759; -.
DR   Proteomes; UP000001610; 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:SF17; ACYL-COA DEHYDROGENASE-RELATED; 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:UP000001610}.
FT   DOMAIN          31..152
FT                   /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02771"
FT   DOMAIN          157..251
FT                   /note="Acyl-CoA oxidase/dehydrogenase middle"
FT                   /evidence="ECO:0000259|Pfam:PF02770"
FT   DOMAIN          264..420
FT                   /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00441"
SQ   SEQUENCE   431 AA;  47293 MW;  F01162A282D68331 CRC64;
     MAPDTKLELS PHIPWSEPAW YSSLRSPYYN ESHRKLRDNI RRYIDENVLP HSFEWEEKGE
     APVEASKAWL KSGIGLDDIP VQYRPADVPS LSGLPPGQLD AFHMLIIADE TSRIEGGVGI
     ALGGASSIGA PPIIHFGIDE QKAKWLPGLF TKETSFCLGI TEPSGGSDVA QLRTTAEKTA
     DGKFYVVNGV KKWITGSPWA SHMTTAVRTG ADGAQGISVL VIPMDAPGIT VDKIQNSGQN
     AGGASFVDLD NVKVPVENLI GRENQGFSII MRNFNRERFL LAVQCNRKSR TCLALAFQYA
     LQRETFGKPL MQYQVIRRKL TEVAHRVEAH WAWMEQLAYH IGTSPEGWQS PDVAGRLALL
     KVQGGQMVEL AAREAQQIFG GAGYQRSGPG ATVEQISRDL RMLVVGGGSE EIMADLAIRQ
     ELMMAKSKLK L
//
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