ID K2RL73_MACPH Unreviewed; 546 AA.
AC K2RL73;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE SubName: Full=Cytochrome b5 {ECO:0000313|EMBL:EKG15443.1};
GN ORFNames=MPH_07367 {ECO:0000313|EMBL:EKG15443.1};
OS Macrophomina phaseolina (strain MS6) (Charcoal rot fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetes incertae sedis; Botryosphaeriales; Botryosphaeriaceae;
OC Macrophomina.
OX NCBI_TaxID=1126212 {ECO:0000313|EMBL:EKG15443.1, ECO:0000313|Proteomes:UP000007129};
RN [1] {ECO:0000313|EMBL:EKG15443.1, ECO:0000313|Proteomes:UP000007129}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MS6 {ECO:0000313|EMBL:EKG15443.1,
RC ECO:0000313|Proteomes:UP000007129};
RX PubMed=22992219; DOI=10.1186/1471-2164-13-493;
RA Islam M.S., Haque M.S., Islam M.M., Emdad E.M., Halim A., Hossen Q.M.M.,
RA Hossain M.Z., Ahmed B., Rahim S., Rahman M.S., Alam M.M., Hou S., Wan X.,
RA Saito J.A., Alam M.;
RT "Tools to kill: Genome of one of the most destructive plant pathogenic
RT fungi Macrophomina phaseolina.";
RL BMC Genomics 13:493-493(2012).
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:EKG15443.1}.
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DR EMBL; AHHD01000298; EKG15443.1; -; Genomic_DNA.
DR AlphaFoldDB; K2RL73; -.
DR STRING; 1126212.K2RL73; -.
DR VEuPathDB; FungiDB:MPH_07367; -.
DR eggNOG; KOG0137; Eukaryota.
DR eggNOG; KOG0537; Eukaryota.
DR HOGENOM; CLU_018204_4_4_1; -.
DR InParanoid; K2RL73; -.
DR OrthoDB; 1474114at2759; -.
DR Proteomes; UP000007129; 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:UP000007129}.
FT DOMAIN 2..78
FT /note="Cytochrome b5 heme-binding"
FT /evidence="ECO:0000259|PROSITE:PS50255"
FT REGION 78..106
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 84..99
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 546 AA; 61193 MW; 1BC75E0437DD900D CRC64;
MAGTFSKADV AAHSKPDNLW IIVDEDVYDL TKFQDEHPGG KKILQRVAGK DASKQFWKYH
NEGILKKYQK QLQIGSLDSK PKPAAAAPPT PPKTPPAKPK AEPGTVSAVP EEDFEALEQF
GDLIPFADPS WYQTYHSPYF NQSHADLRAE AREWVENEII PNVTEWDEAK RVPEEIYKAM
GERGYLAGLL GLHKWPSHLT DKRVASVAPE KWDLFHEMLL TDELSRSGSG GFVWNVIGGF
GIGCPPVVKH GKKELVERIL PGILSGDKRI CLAITEPDAG SDVANLTCEA KLSEDGKHYI
VNGEKKWITN GIWCDYFTTA VRTGKEGMNG VSVLLIERDM GGVSTRRMDC QGVWSSGTTY
ITFEDVKVPV ENLIGKENQG FKVIMTNFNH ERIGIIIQCL RFSRVCYEDC VKYAHKRRTF
GKKLIDHPVI RLKLAHMARQ IEASYNWLEN LIFQCQRMNE MEAMLKLGGA IASLKAQATT
TFEFCAREAS QIFGGLSYSR GGQGGRIERL YRDVRAYAIP GGSEEIMLDL SIRQSLRVHK
ALGMKL
//
