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Database: UniProt
Entry: A0A1Y2GH32_9FUNG
LinkDB: A0A1Y2GH32_9FUNG
Original site: A0A1Y2GH32_9FUNG 
ID   A0A1Y2GH32_9FUNG        Unreviewed;       432 AA.
AC   A0A1Y2GH32;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   24-JAN-2024, entry version 17.
DE   SubName: Full=Acyl-CoA dehydrogenase/oxidase {ECO:0000313|EMBL:ORZ09374.1};
GN   ORFNames=BCR41DRAFT_358611 {ECO:0000313|EMBL:ORZ09374.1};
OS   Lobosporangium transversale.
OC   Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mortierellomycotina;
OC   Mortierellomycetes; Mortierellales; Mortierellaceae; Lobosporangium.
OX   NCBI_TaxID=64571 {ECO:0000313|EMBL:ORZ09374.1, ECO:0000313|Proteomes:UP000193648};
RN   [1] {ECO:0000313|EMBL:ORZ09374.1, ECO:0000313|Proteomes:UP000193648}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL 3116 {ECO:0000313|EMBL:ORZ09374.1,
RC   ECO:0000313|Proteomes:UP000193648};
RG   DOE Joint Genome Institute;
RA   Mondo S.J., Dannebaum R.O., Kuo R.C., Labutti K., Haridas S., Kuo A.,
RA   Salamov A., Ahrendt S.R., Lipzen A., Sullivan W., Andreopoulos W.B.,
RA   Clum A., Lindquist E., Daum C., Ramamoorthy G.K., Gryganskyi A., Culley D.,
RA   Magnuson J.K., James T.Y., O'Malley M.A., Stajich J.E., Spatafora J.W.,
RA   Visel A., Grigoriev I.V.;
RT   "Pervasive Adenine N6-methylation of Active Genes in Fungi.";
RL   Submitted (JUL-2016) 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   -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
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:ORZ09374.1}.
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DR   EMBL; MCFF01000034; ORZ09374.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y2GH32; -.
DR   STRING; 64571.A0A1Y2GH32; -.
DR   InParanoid; A0A1Y2GH32; -.
DR   OrthoDB; 276350at2759; -.
DR   Proteomes; UP000193648; 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:UP000193648}.
FT   DOMAIN          12..134
FT                   /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02771"
FT   DOMAIN          138..240
FT                   /note="Acyl-CoA oxidase/dehydrogenase middle"
FT                   /evidence="ECO:0000259|Pfam:PF02770"
FT   DOMAIN          252..403
FT                   /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00441"
SQ   SEQUENCE   432 AA;  47885 MW;  DB2A6115E3F9D44C CRC64;
     MTSIFEVSPR CQELQKKLID FVENDCLPAE EVYESQVGTG DQRWKTVPPI MEELKAKAKS
     LGLWNLFLPK SYPEGPGLTN LEYATLCEIT GRCPRVAPEA LNCSAPDTGN MEVFAKYGTP
     AQKQQYLVPL MNGEIRSAFA MTEIAVSSSD ATNIETRIER VGDHYIINGH KWWISGAGDP
     RCKVFLVMGK SDPNNEHKYR QQSIVIVPAD APGIEVVRPM TVYGYDDAPE GHCEVKFTNV
     KVPVSNIIAG EGRGFEVIQG RLGPGRIHHC MRAIGVAERT LDIMISRVTN PSRRTFGKVL
     ARHGTVAADV AKMRIEINAA RLMVLAAADK IDKLNAKGAM RDIAMAKIMV PQMLQRTVDL
     AIQAHGAAGL SQDFPLARFY ALARTLRIAD GPDEVHMMQL ARFELMRGDE IREKDEKIRA
     RRAQILSNGS KL
//
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