ID K2RU69_MACPH Unreviewed; 446 AA.
AC K2RU69;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE SubName: Full=Monooxygenase FAD-binding protein {ECO:0000313|EMBL:EKG18343.1};
GN ORFNames=MPH_04425 {ECO:0000313|EMBL:EKG18343.1};
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:EKG18343.1, ECO:0000313|Proteomes:UP000007129};
RN [1] {ECO:0000313|EMBL:EKG18343.1, ECO:0000313|Proteomes:UP000007129}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MS6 {ECO:0000313|EMBL:EKG18343.1,
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 -!- SIMILARITY: Belongs to the paxM FAD-dependent monooxygenase family.
CC {ECO:0000256|ARBA:ARBA00007992}.
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:EKG18343.1}.
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DR EMBL; AHHD01000209; EKG18343.1; -; Genomic_DNA.
DR AlphaFoldDB; K2RU69; -.
DR STRING; 1126212.K2RU69; -.
DR VEuPathDB; FungiDB:MPH_04425; -.
DR eggNOG; KOG2614; Eukaryota.
DR HOGENOM; CLU_009665_6_3_1; -.
DR InParanoid; K2RU69; -.
DR OrthoDB; 2684451at2759; -.
DR Proteomes; UP000007129; Unassembled WGS sequence.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR InterPro; IPR002938; FAD-bd.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR PANTHER; PTHR46720; HYDROXYLASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_3G01460)-RELATED; 1.
DR PANTHER; PTHR46720:SF3; HYDROXYLASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_3G01460)-RELATED; 1.
DR Pfam; PF01494; FAD_binding_3; 1.
DR PRINTS; PR00420; RNGMNOXGNASE.
DR SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Monooxygenase {ECO:0000313|EMBL:EKG18343.1};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000007129}.
FT DOMAIN 18..396
FT /note="FAD-binding"
FT /evidence="ECO:0000259|Pfam:PF01494"
SQ SEQUENCE 446 AA; 47956 MW; A7241444ECE65840 CRC64;
MIDPASELPG AQPPKPFSVA VVGGGLGGVV LAIALLVHRV PVHIYESAKS FGEIGAGVAF
GPNSVRALAL ISPQLREAIA RHATCNATPG LEDVFLSFRR GQASDGGMVD GRKAGSPGEW
LFDLKNEQSA DNLTGLPLRC CVHRAKFLDE VIKLVPEGAA SFNKSLTAID ELTTEEGGGV
RLHFSDGTSA VASAAIGCDG IKSKARQYVH GLEAQPTFTG CYAIRAMVSS AAFEKAMGRE
STFNGQMYAG RGGYIITYPV DHGKLINVLA SRSHPGSTWS QEAWLSPSTK EEMVEELHGW
HPVLVEFLAQ YGTMEKWALF DYHHDRKYWR GRVCLLGDAA HATTPHLGAG AGQAMEDAYV
LSNLLGKAET AEDLPNVFQA YDAVRRPRTQ QVVEFSRQSG LALAGLEEGV GTDYAKLEAV
SVERFRWVWN EDLQKELDEA AGAMAA
//
