ID M2STX0_COCSN Unreviewed; 549 AA.
AC M2STX0;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=Cytochrome b5 heme-binding domain-containing protein {ECO:0000259|PROSITE:PS50255};
GN ORFNames=COCSADRAFT_114857 {ECO:0000313|EMBL:EMD65730.1};
OS Cochliobolus sativus (strain ND90Pr / ATCC 201652) (Common root rot and
OS spot blotch fungus) (Bipolaris sorokiniana).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae; Bipolaris.
OX NCBI_TaxID=665912 {ECO:0000313|EMBL:EMD65730.1, ECO:0000313|Proteomes:UP000016934};
RN [1] {ECO:0000313|EMBL:EMD65730.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ND90Pr {ECO:0000313|EMBL:EMD65730.1};
RX PubMed=23236275; DOI=10.1371/journal.ppat.1003037;
RA Ohm R.A., Feau N., Henrissat B., Schoch C.L., Horwitz B.A., Barry K.W.,
RA Condon B.J., Copeland A.C., Dhillon B., Glaser F., Hesse C.N., Kosti I.,
RA LaButti K., Lindquist E.A., Lucas S., Salamov A.A., Bradshaw R.E.,
RA Ciuffetti L., Hamelin R.C., Kema G.H.J., Lawrence C., Scott J.A.,
RA Spatafora J.W., Turgeon B.G., de Wit P.J.G.M., Zhong S., Goodwin S.B.,
RA Grigoriev I.V.;
RT "Diverse lifestyles and strategies of plant pathogenesis encoded in the
RT genomes of eighteen Dothideomycetes fungi.";
RL PLoS Pathog. 8:E1003037-E1003037(2012).
RN [2] {ECO:0000313|EMBL:EMD65730.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ND90Pr {ECO:0000313|EMBL:EMD65730.1};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Condon B.J., Leng Y., Wu D., Bushley K.E., Ohm R.A., Otillar R., Martin J.,
RA Schackwitz W., Grimwood J., MohdZainudin N., Xue C., Wang R., Dhillon B.,
RA Tu Z.J., Steffenson B.J., Salamov A., Sun H., Lowry S., LaButti K., Han J.,
RA Copeland A., Lindquist E., Lucas S., Barry K., Schmutz J., Baker S.,
RA Grigoriev I.V., Zhong S., Turgeon B.G.;
RT "Comparative genome structure, secondary metabolite and effector coding
RT capacity across Cochliobolus pathogens.";
RL Submitted (MAY-2012) to the EMBL/GenBank/DDBJ databases.
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; KB445641; EMD65730.1; -; Genomic_DNA.
DR RefSeq; XP_007698796.1; XM_007700606.1.
DR AlphaFoldDB; M2STX0; -.
DR STRING; 665912.M2STX0; -.
DR GeneID; 19130262; -.
DR KEGG; bsc:COCSADRAFT_114857; -.
DR eggNOG; KOG0137; Eukaryota.
DR eggNOG; KOG0537; Eukaryota.
DR HOGENOM; CLU_018204_4_4_1; -.
DR OMA; YQCEKMG; -.
DR OrthoDB; 1474114at2759; -.
DR Proteomes; UP000016934; 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:SF20; LONG-CHAIN SPECIFIC ACYL-COA DEHYDROGENASE, MITOCHONDRIAL; 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:UP000016934}.
FT DOMAIN 2..78
FT /note="Cytochrome b5 heme-binding"
FT /evidence="ECO:0000259|PROSITE:PS50255"
SQ SEQUENCE 549 AA; 61500 MW; 154A860C2EC9CE57 CRC64;
MAKRFSTADV ASHKTANDLW IIVDEDVYDL TKFQDDHPGG KKILQRVAGK DASKQFWKYH
NESILKKYQK QLQVGSLDTK AAPPAPPAAA APEMKEIVKP EANPGVVAPQ PTQAAEEPEP
FDSYGDLVPY ADPSWYQTYH SPYYNETHAA LRAEVRDWVE EKLMPYVTEW DEAKKVPDEI
FLEMGARGYL AGMLGVKYPT QYTDLRVKSV PPEKWDHFHE MIITDEISRT GSGGLVWGLI
GGYGIGGPPL FKFGKKELVQ RIGPDLLSGK KRICLAITEP DAGSDVANLT CEAKLSEDGK
HYIVNGEKKW ITNGIWSDYF TTAVRTGGEG MNGISVLLIE RSAGGVSTRK MDCQGVWSSG
TTYITFEDVK VPVENLIGKE NQGFKVVMTN FNHERIGIII QCLRFSRVCY EESMKYAHKR
KTFGKRLIDH PVIRLKLAHM ARQIEASYNW MENLIYQCEK MDDMEAMLKL GGAIASLKAQ
STTTFEFCAR EASQIFGGLS YSRGGQGAKV ERLYRDVRAY AIPGGSEEIM LDLSIRQALR
VHKVLGMKL
//
