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Database: UniProt
Entry: K2RTB1_MACPH
LinkDB: K2RTB1_MACPH
Original site: K2RTB1_MACPH 
ID   K2RTB1_MACPH            Unreviewed;       360 AA.
AC   K2RTB1;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   22-FEB-2023, entry version 29.
DE   SubName: Full=Fumarate reductase/succinate dehydrogenase flavoprotein {ECO:0000313|EMBL:EKG17983.1};
GN   ORFNames=MPH_04791 {ECO:0000313|EMBL:EKG17983.1};
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:EKG17983.1, ECO:0000313|Proteomes:UP000007129};
RN   [1] {ECO:0000313|EMBL:EKG17983.1, ECO:0000313|Proteomes:UP000007129}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MS6 {ECO:0000313|EMBL:EKG17983.1,
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   -!- 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:EKG17983.1}.
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DR   EMBL; AHHD01000219; EKG17983.1; -; Genomic_DNA.
DR   AlphaFoldDB; K2RTB1; -.
DR   STRING; 1126212.K2RTB1; -.
DR   VEuPathDB; FungiDB:MPH_04791; -.
DR   eggNOG; KOG2403; Eukaryota.
DR   HOGENOM; CLU_014312_4_0_1; -.
DR   InParanoid; K2RTB1; -.
DR   OrthoDB; 551958at2759; -.
DR   Proteomes; UP000007129; Unassembled WGS sequence.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR   Gene3D; 1.20.58.100; Fumarate reductase/succinate dehydrogenase flavoprotein-like, C-terminal domain; 1.
DR   Gene3D; 4.10.80.40; succinate dehydrogenase protein domain; 1.
DR   Gene3D; 3.90.700.10; Succinate dehydrogenase/fumarate reductase flavoprotein, catalytic domain; 1.
DR   InterPro; IPR003953; FAD-binding_2.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR037099; Fum_R/Succ_DH_flav-like_C_sf.
DR   InterPro; IPR015939; Fum_Rdtase/Succ_DH_flav-like_C.
DR   InterPro; IPR030664; SdhA/FrdA/AprA.
DR   InterPro; IPR027477; Succ_DH/fumarate_Rdtase_cat_sf.
DR   PANTHER; PTHR11632; SUCCINATE DEHYDROGENASE 2 FLAVOPROTEIN SUBUNIT; 1.
DR   PANTHER; PTHR11632:SF51; SUCCINATE DEHYDROGENASE [UBIQUINONE] FLAVOPROTEIN SUBUNIT, MITOCHONDRIAL; 1.
DR   Pfam; PF00890; FAD_binding_2; 1.
DR   Pfam; PF02910; Succ_DH_flav_C; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR   SUPFAM; SSF46977; Succinate dehydrogenase/fumarate reductase flavoprotein C-terminal domain; 1.
DR   SUPFAM; SSF56425; Succinate dehydrogenase/fumarate reductase flavoprotein, catalytic domain; 1.
PE   4: Predicted;
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007129}.
FT   DOMAIN          1..169
FT                   /note="FAD-dependent oxidoreductase 2 FAD binding"
FT                   /evidence="ECO:0000259|Pfam:PF00890"
FT   DOMAIN          225..360
FT                   /note="Fumarate reductase/succinate dehydrogenase
FT                   flavoprotein-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02910"
FT   ACT_SITE        51
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR630664-50"
SQ   SEQUENCE   360 AA;  39860 MW;  EF70692B7C337FE2 CRC64;
     MEFVQFHPSG IYGAGVLITE GARGEGGYLL NSQGERFMER YAPTAKDLAS RDVVSRSMNM
     EILEGRGCGP DKDHIHLQLS HLPRDIIMER LPGIAETASI FAGIDITKQP IPVLPTVHYC
     MGGIPTNYKG QVLDVSTDGK EKTVPGLYAA GETACVSVHG ANRLGANSLL DIIVFGRACA
     MDIVESHEKG MPHEKAPENV GLDSISELDS ILASDGDKLT AEIRGDMQRI MQTDAAVFRT
     GKSLDTGYER VKLVERDFKE RLAVRDKSMI WNSDLIETLE TRNLLTCAVQ TVAGAVERKE
     SRGSHAREDF PDRVDDEWMK HTLTWQKRVG EDVQVGYRDV IFDTLDPKEC PTIPPKKRSY
//
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