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Database: UniProt
Entry: G4UYG5_NEUT9
LinkDB: G4UYG5_NEUT9
Original site: G4UYG5_NEUT9 
ID   G4UYG5_NEUT9            Unreviewed;       546 AA.
AC   G4UYG5;
DT   14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT   14-DEC-2011, sequence version 1.
DT   08-NOV-2023, entry version 45.
DE   SubName: Full=Acyl-CoA dehydrogenase NM domain-like protein {ECO:0000313|EMBL:EGZ69074.1};
GN   ORFNames=NEUTE2DRAFT_151881 {ECO:0000313|EMBL:EGZ69074.1};
OS   Neurospora tetrasperma (strain FGSC 2509 / P0656).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX   NCBI_TaxID=510952 {ECO:0000313|EMBL:EGZ69074.1, ECO:0000313|Proteomes:UP000008513};
RN   [1] {ECO:0000313|EMBL:EGZ69074.1, ECO:0000313|Proteomes:UP000008513}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=strain FGSC 2509 / P0656 {ECO:0000313|Proteomes:UP000008513};
RX   PubMed=21750257; DOI=10.1534/genetics.111.130690;
RA   Ellison C.E., Stajich J.E., Jacobson D.J., Natvig D.O., Lapidus A.,
RA   Foster B., Aerts A., Riley R., Lindquist E.A., Grigoriev I.V., Taylor J.W.;
RT   "Massive changes in genome architecture accompany the transition to self-
RT   fertility in the filamentous fungus Neurospora tetrasperma.";
RL   Genetics 189:55-69(2011).
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; GL891258; EGZ69074.1; -; Genomic_DNA.
DR   AlphaFoldDB; G4UYG5; -.
DR   STRING; 510952.G4UYG5; -.
DR   eggNOG; KOG0139; Eukaryota.
DR   eggNOG; KOG0537; Eukaryota.
DR   HOGENOM; CLU_018204_4_4_1; -.
DR   OMA; PYFNQTH; -.
DR   Proteomes; UP000008513; 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   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; 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)-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   Pfam; PF00173; Cyt-b5; 1.
DR   PRINTS; PR00363; CYTOCHROMEB5.
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; 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:UP000008513}.
FT   DOMAIN          2..78
FT                   /note="Cytochrome b5 heme-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50255"
FT   REGION          79..115
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   546 AA;  60685 MW;  2B1B2D2EBDCD3277 CRC64;
     MSKIFTQADV SSHSKPDSLW IVIDGDVYDV TKFADDHPGG KKILQRVGGK DASKQFWKYH
     NEGILKKYQG KLQIGSLDSK PKAAAPAPAA APAPAPKAAP KPKASTASSS SHEQSEALEP
     FGQLIPFADP SWYQSYHSPY YNETHAALRA EIREWVETAI DPYVTEWDEK KEVPAEIYKE
     MGKRGYLAGL LGTKYQSNYV ENPIKSVPAE KWDLFHEMLV TDELSRTGSG GFVWNVIGGF
     GIGCPPLVKF GKKPLVDRIL PGILNGDKRI CLAITEPDAG SDVANLTCEA KLTEDGKHYI
     VNGEKKWITN GIWSDYFTTA VRTGGPGMNG VSLLLIERDF PGVSTRRMDC QGVWSSGTTY
     ITFEDVKVPV ENLIGKENQG FRVIMTNFNH ERIGIIIQCL RFSRVCYEES VKYANKRRTF
     GKKLIEHPVI RLKLAHMARQ IEASYNWLEN LIYQCEKMGD TEAMLRLGGA IASLKAQATV
     TFEFCAREAS QIFGGLSYSR GGQGGKVERL YRDVRAYAIP GGSEEIMLDL SIRQSLRVSK
     MTGMKL
//
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