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Database: UniProt
Entry: M5G838_DACPD
LinkDB: M5G838_DACPD
Original site: M5G838_DACPD 
ID   M5G838_DACPD            Unreviewed;       519 AA.
AC   M5G838;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   27-MAR-2024, entry version 38.
DE   SubName: Full=Acyl-CoA dehydrogenase NM domain-like protein {ECO:0000313|EMBL:EJU04929.1};
GN   ORFNames=DACRYDRAFT_63229 {ECO:0000313|EMBL:EJU04929.1};
OS   Dacryopinax primogenitus (strain DJM 731) (Brown rot fungus).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Dacrymycetes;
OC   Dacrymycetales; Dacrymycetaceae; Dacryopinax.
OX   NCBI_TaxID=1858805 {ECO:0000313|EMBL:EJU04929.1, ECO:0000313|Proteomes:UP000030653};
RN   [1] {ECO:0000313|EMBL:EJU04929.1, ECO:0000313|Proteomes:UP000030653}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DJM-731 SS1 {ECO:0000313|EMBL:EJU04929.1,
RC   ECO:0000313|Proteomes:UP000030653};
RX   PubMed=22745431; DOI=10.1126/science.1221748;
RA   Floudas D., Binder M., Riley R., Barry K., Blanchette R.A., Henrissat B.,
RA   Martinez A.T., Otillar R., Spatafora J.W., Yadav J.S., Aerts A., Benoit I.,
RA   Boyd A., Carlson A., Copeland A., Coutinho P.M., de Vries R.P.,
RA   Ferreira P., Findley K., Foster B., Gaskell J., Glotzer D., Gorecki P.,
RA   Heitman J., Hesse C., Hori C., Igarashi K., Jurgens J.A., Kallen N.,
RA   Kersten P., Kohler A., Kuees U., Kumar T.K.A., Kuo A., LaButti K.,
RA   Larrondo L.F., Lindquist E., Ling A., Lombard V., Lucas S., Lundell T.,
RA   Martin R., McLaughlin D.J., Morgenstern I., Morin E., Murat C., Nagy L.G.,
RA   Nolan M., Ohm R.A., Patyshakuliyeva A., Rokas A., Ruiz-Duenas F.J.,
RA   Sabat G., Salamov A., Samejima M., Schmutz J., Slot J.C., St John F.,
RA   Stenlid J., Sun H., Sun S., Syed K., Tsang A., Wiebenga A., Young D.,
RA   Pisabarro A., Eastwood D.C., Martin F., Cullen D., Grigoriev I.V.,
RA   Hibbett D.S.;
RT   "The Paleozoic origin of enzymatic lignin decomposition reconstructed from
RT   31 fungal genomes.";
RL   Science 336:1715-1719(2012).
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}.
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DR   EMBL; JH795857; EJU04929.1; -; Genomic_DNA.
DR   AlphaFoldDB; M5G838; -.
DR   STRING; 1858805.M5G838; -.
DR   HOGENOM; CLU_018204_4_4_1; -.
DR   OMA; MAFCASE; -.
DR   OrthoDB; 294001at2759; -.
DR   Proteomes; UP000030653; Unassembled WGS sequence.
DR   GO; GO:0003995; F:acyl-CoA dehydrogenase activity; IEA:InterPro.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; 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   Gene3D; 3.10.120.10; Cytochrome b5-like heme/steroid binding domain; 1.
DR   InterPro; IPR006089; Acyl-CoA_DH_CS.
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   InterPro; IPR001199; Cyt_B5-like_heme/steroid-bd.
DR   InterPro; IPR036400; Cyt_B5-like_heme/steroid_sf.
DR   PANTHER; PTHR48083:SF28; ACYL-COA DEHYDROGENASE FAMILY PROTEIN (AFU_ORTHOLOGUE AFUA_6G10880); 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   Pfam; PF00173; Cyt-b5; 1.
DR   SMART; SM01117; Cyt-b5; 1.
DR   SUPFAM; SSF47203; Acyl-CoA dehydrogenase C-terminal domain-like; 1.
DR   SUPFAM; SSF56645; Acyl-CoA dehydrogenase NM domain-like; 1.
DR   SUPFAM; SSF55856; Cytochrome b5-like heme/steroid binding domain; 1.
DR   PROSITE; PS00072; ACYL_COA_DH_1; 1.
DR   PROSITE; PS50255; CYTOCHROME_B5_2; 1.
PE   3: Inferred from homology;
KW   FAD {ECO:0000256|ARBA:ARBA00022827};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030653}.
FT   DOMAIN          6..85
FT                   /note="Cytochrome b5 heme-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50255"
SQ   SEQUENCE   519 AA;  58080 MW;  F03CFF3E0F15248A CRC64;
     MSKKEMRILS TDEIAKHNKP DDLWVIIDAK VYDLSRFAEM HPGGAAVLYD PEVAGQDATD
     AFFGLHRMEV LLRPQYKRFL IGTVQGEESK IIFPKPGDIS QVPYAEPTWL NEGYYSPYFT
     ENHRQFQLAV RKFVDEYVTP DAHDREEDGK RPSQSVFDKM AEMEMHAMRL GPGKHLKGRK
     LMGGLVDPEK FDYFHELIIT QELARTGSRG YGDGMLGGMV IGLPPVLNFG SEEVKRMVVP
     DVLAGKKFIC LAISEAFAGS DVAGLRCTAV KSEDGKEWII NGTKKWITNG TFADWFTVGC
     KTEGGLTVIL VPRCEGLQTK QIKTSYSPTA GTAYIKFDNV RVPVGYTLGP EDGGLLVILS
     NFNHERWVMC CASARSQRHV VEECLKWAHQ RKAFGKPLTG QAIIRAKLAQ MISRVEAVQS
     WLEAVTYQMC HMSYKQQSSK LAGQIAFLKM FCTKTAQQTA EEATQVFGGR GITRTGMGRF
     IEHYHRTVPF DSLLGGAEDV LADLGVRQAM RKIPENTRL
//
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