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Database: UniProt
Entry: K2SIN9_MACPH
LinkDB: K2SIN9_MACPH
Original site: K2SIN9_MACPH 
ID   K2SIN9_MACPH            Unreviewed;       361 AA.
AC   K2SIN9;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   SubName: Full=Alcohol dehydrogenase superfamily zinc-containing {ECO:0000313|EMBL:EKG16695.1};
GN   ORFNames=MPH_06081 {ECO:0000313|EMBL:EKG16695.1};
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:EKG16695.1, ECO:0000313|Proteomes:UP000007129};
RN   [1] {ECO:0000313|EMBL:EKG16695.1, ECO:0000313|Proteomes:UP000007129}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MS6 {ECO:0000313|EMBL:EKG16695.1,
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:EKG16695.1}.
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DR   EMBL; AHHD01000264; EKG16695.1; -; Genomic_DNA.
DR   AlphaFoldDB; K2SIN9; -.
DR   STRING; 1126212.K2SIN9; -.
DR   VEuPathDB; FungiDB:MPH_06081; -.
DR   eggNOG; KOG1197; Eukaryota.
DR   HOGENOM; CLU_026673_3_1_1; -.
DR   InParanoid; K2SIN9; -.
DR   OrthoDB; 148501at2759; -.
DR   Proteomes; UP000007129; Unassembled WGS sequence.
DR   GO; GO:0003960; F:NADPH:quinone reductase activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   CDD; cd05286; QOR2; 1.
DR   Gene3D; 3.90.180.10; Medium-chain alcohol dehydrogenases, catalytic domain; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR013149; ADH-like_C.
DR   InterPro; IPR013154; ADH-like_N.
DR   InterPro; IPR011032; GroES-like_sf.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR020843; PKS_ER.
DR   InterPro; IPR047618; QOR-like.
DR   InterPro; IPR002364; Quin_OxRdtase/zeta-crystal_CS.
DR   PANTHER; PTHR48106; QUINONE OXIDOREDUCTASE PIG3-RELATED; 1.
DR   PANTHER; PTHR48106:SF13; QUINONE OXIDOREDUCTASE-RELATED; 1.
DR   Pfam; PF08240; ADH_N; 1.
DR   Pfam; PF00107; ADH_zinc_N; 1.
DR   SMART; SM00829; PKS_ER; 1.
DR   SUPFAM; SSF50129; GroES-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   PROSITE; PS01162; QOR_ZETA_CRYSTAL; 1.
PE   4: Predicted;
KW   NADP {ECO:0000256|ARBA:ARBA00022857};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007129}.
FT   DOMAIN          19..359
FT                   /note="Enoyl reductase (ER)"
FT                   /evidence="ECO:0000259|SMART:SM00829"
SQ   SEQUENCE   361 AA;  38984 MW;  B1D68E9C13F274B7 CRC64;
     MASTSLPSTM KGVIIEKTGG TEVLQYKTDL PVPQPKAGEV LVKNDFIGIN YIDTYFRTGL
     YPAPSFPYIL GREAAGLIVA TGSDGELHGL KTGDRIAWMG QGAYAEYTAI PVSHATKVPE
     GVSSDVAAAA LLQGLTALTL IREAHPVKKG DWVLVHAAAG GVGLWLCQLL KAVGARTIGT
     ASTEEKIELA KKNGAEVLIN YSKDDVVEKV KEVTGGQGVA AVFDGVGKAT FDISLESVAR
     KGSLISFGNA SGAVPPVTIA YVNLSPLPPP FSCYQWRWEH LLKVDCHSRL SAKNVKLLRP
     TLFNYLATRE EFNHYTKELF QFIEKDGIDV RIHEVYPLAE VARAHQDLEG RKTTGKLLLK
     P
//
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