ID A0A177DSQ6_ALTAL Unreviewed; 443 AA.
AC A0A177DSQ6;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 08-NOV-2023, entry version 23.
DE SubName: Full=Short-chain specific acyl-CoA dehydrogenase mitochondrial {ECO:0000313|EMBL:OAG22181.1};
GN ORFNames=CC77DRAFT_1093629 {ECO:0000313|EMBL:OAG22181.1};
OS Alternaria alternata (Alternaria rot fungus) (Torula alternata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae; Alternaria;
OC Alternaria sect. Alternaria; Alternaria alternata complex.
OX NCBI_TaxID=5599 {ECO:0000313|EMBL:OAG22181.1, ECO:0000313|Proteomes:UP000077248};
RN [1] {ECO:0000313|EMBL:OAG22181.1, ECO:0000313|Proteomes:UP000077248}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SRC1lrK2f {ECO:0000313|EMBL:OAG22181.1,
RC ECO:0000313|Proteomes:UP000077248};
RG DOE Joint Genome Institute;
RA Zeiner C.A., Purvine S.O., Zink E.M., Wu S., Pasa-Tolic L., Chaput D.L.,
RA Haridas S., Grigoriev I.V., Santelli C.M., Hansel C.M.;
RT "Comparative analysis of secretome profiles of manganese(II)-oxidizing
RT ascomycete fungi.";
RL Submitted (MAY-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 -!- SIMILARITY: Belongs to the acyl-CoA dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00009347, ECO:0000256|RuleBase:RU362125}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KV441475; OAG22181.1; -; Genomic_DNA.
DR RefSeq; XP_018387602.1; XM_018529689.1.
DR AlphaFoldDB; A0A177DSQ6; -.
DR STRING; 5599.A0A177DSQ6; -.
DR GeneID; 29115283; -.
DR KEGG; aalt:CC77DRAFT_1093629; -.
DR VEuPathDB; FungiDB:CC77DRAFT_1093629; -.
DR OMA; YTTMAVR; -.
DR OrthoDB; 2784306at2759; -.
DR Proteomes; UP000077248; 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:SF15; ACYL-COA DEHYDROGENASE APDG; 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:UP000077248}.
FT DOMAIN 25..154
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 158..254
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 266..422
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
SQ SEQUENCE 443 AA; 48780 MW; C5EB7DAADF17B986 CRC64;
MSSTAFVPFS EPPYIVGLPS PYYKETHLRW QKACREFVDK HMLEKSLEWD TNETVPEHVF
ETFAKAGMLL PTLPAPLPVE WLKKLGIHDI LGVVKVEEWD YIHTMIYADE MARTGLAGPS
GSLTTGMSFG VPPIIKYGNK QLQERFLPEL LTGKKRTCIA ITEPEAGSDV ANITTTATKT
PDGKHYIVNG TKKWITNGIW SDYSSMAVRT GGPGPTGLSM LVVPLKGYPG VNMRRLKVGG
QVSAGTTFIE LDDVKVPVEN LIGEEGMGMK YIMTNFNHER LTIAIGATRQ ARVALSAAME
YVLKREAFGK PLVDQPVVRH RLAKAGALLE SQWAWVEQFV YQMVHIPKAT ADIELGGLTA
MVKAQSGIVL NECAQTAQLL FGGNGYTKSG QGELVERIYR EVPGVRIPGG SEDVMLDLGV
RQLVKNFKNK TKAMERPKGS SKL
//
