ID V2X5E6_MONRO Unreviewed; 508 AA.
AC V2X5E6;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 24-JAN-2024, entry version 34.
DE SubName: Full=Acyl-dehydrogenase {ECO:0000313|EMBL:ESK89027.1};
GN ORFNames=Moror_13108 {ECO:0000313|EMBL:ESK89027.1};
OS Moniliophthora roreri (strain MCA 2997) (Cocoa frosty pod rot fungus)
OS (Crinipellis roreri).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Marasmiineae; Marasmiaceae; Moniliophthora.
OX NCBI_TaxID=1381753 {ECO:0000313|EMBL:ESK89027.1, ECO:0000313|Proteomes:UP000017559};
RN [1] {ECO:0000313|EMBL:ESK89027.1, ECO:0000313|Proteomes:UP000017559}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCA 2997 {ECO:0000313|EMBL:ESK89027.1,
RC ECO:0000313|Proteomes:UP000017559};
RX PubMed=24571091; DOI=10.1186/1471-2164-15-164;
RA Meinhardt L.W., Costa G.G.L., Thomazella D.P.T., Teixeira P.J.P.L.,
RA Carazzolle M.F., Schuster S.C., Carlson J.E., Guiltinan M.J.,
RA Mieczkowski P., Farmer A., Ramaraj T., Crozier J., Davis R.E., Shao J.,
RA Melnick R.L., Pereira G.A.G., Bailey B.A.;
RT "Genome and secretome analysis of the hemibiotrophic fungal pathogen,
RT Moniliophthora roreri, which causes frosty pod rot disease of cacao:
RT mechanisms of the biotrophic and necrotrophic phases.";
RL BMC Genomics 15:164-164(2014).
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}.
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:ESK89027.1}.
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DR EMBL; AWSO01000595; ESK89027.1; -; Genomic_DNA.
DR RefSeq; XP_007851656.1; XM_007853465.1.
DR AlphaFoldDB; V2X5E6; -.
DR STRING; 1381753.V2X5E6; -.
DR KEGG; mrr:Moror_13108; -.
DR HOGENOM; CLU_018204_4_4_1; -.
DR OrthoDB; 294001at2759; -.
DR Proteomes; UP000017559; 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 CDD; cd00567; ACAD; 1.
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; 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; 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:UP000017559}.
FT DOMAIN 5..74
FT /note="Cytochrome b5 heme-binding"
FT /evidence="ECO:0000259|PROSITE:PS50255"
SQ SEQUENCE 508 AA; 56262 MW; 7C374DCA02A96DA4 CRC64;
MLNPQHNKRE NLWVIVDSNV YDLSNFASLH PGGIAVLIDQ EVAGQDATEA FFSLHRFEIL
KRPQYLRLKI GTIQGEEPQI NTNPTASLSD VPFAEPTWLT KGYSSPYFNE SHRRLQVAIR
KFNEEVVFPD AQAREEDGKR ASPYIFQERA KRNIPAMALG PGPHLKGLEL MEGAVKPEEF
DCFHELVMIQ EGSRLHARGY TDGLAGGNYI ALPPIMRYAI PDIRDKIVNE VFSGQKFLSL
AVTEAYAGSD VAGIRTRATK VDGGWIVNGS KKWITNGTFA DYFVTACRNK EDGGLIVLLI
ERGEGIKTKL IRTSYSTAAG TAFVTFDDVF VPDGHVLGPR HDGLRIILGN FNHERWAMAC
SSIGTQRAIV EECLKWTAQR KVFGKPLISQ AVVRAKLAAM ISRLESGQNW LENITYQMTK
MNNTQQGALL AGQIAFLKMH ASRAGQDTAR DAVQIFGGRG ITKTGMGRHI EHYHRTLLID
AVGGGAEDII GDLGIRQALR SMPTNARL
//