ID K1XIV5_MARBU Unreviewed; 360 AA.
AC K1XIV5;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 24-JAN-2024, entry version 43.
DE SubName: Full=Zinc-binding transcription factor {ECO:0000313|EMBL:EKD12414.1};
GN ORFNames=MBM_09448 {ECO:0000313|EMBL:EKD12414.1};
OS Marssonina brunnea f. sp. multigermtubi (strain MB_m1) (Marssonina leaf
OS spot fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Drepanopezizaceae; Drepanopeziza.
OX NCBI_TaxID=1072389 {ECO:0000313|EMBL:EKD12414.1, ECO:0000313|Proteomes:UP000006753};
RN [1] {ECO:0000313|EMBL:EKD12414.1, ECO:0000313|Proteomes:UP000006753}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MB_m1 {ECO:0000313|EMBL:EKD12414.1,
RC ECO:0000313|Proteomes:UP000006753};
RX PubMed=22876864; DOI=10.1186/1471-2164-13-382;
RA Zhu S., Cao Y.-Z., Jiang C., Tan B.-Y., Wang Z., Feng S., Zhang L.,
RA Su X.-H., Brejova B., Vinar T., Xu M., Wang M.-X., Zhang S.-G.,
RA Huang M.-R., Wu R., Zhou Y.;
RT "Sequencing the genome of Marssonina brunnea reveals fungus-poplar co-
RT evolution.";
RL BMC Genomics 13:382-382(2012).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|RuleBase:RU361277};
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. {ECO:0000256|RuleBase:RU361277}.
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DR EMBL; JH921458; EKD12414.1; -; Genomic_DNA.
DR RefSeq; XP_007297337.1; XM_007297275.1.
DR AlphaFoldDB; K1XIV5; -.
DR STRING; 1072389.K1XIV5; -.
DR GeneID; 18765383; -.
DR KEGG; mbe:MBM_09448; -.
DR eggNOG; KOG0023; Eukaryota.
DR HOGENOM; CLU_026673_20_2_1; -.
DR InParanoid; K1XIV5; -.
DR OMA; GWGEQKF; -.
DR OrthoDB; 5353053at2759; -.
DR Proteomes; UP000006753; Unassembled WGS sequence.
DR GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd05283; CAD1; 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; IPR002328; ADH_Zn_CS.
DR InterPro; IPR047109; CAD-like.
DR InterPro; IPR011032; GroES-like_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020843; PKS_ER.
DR PANTHER; PTHR42683; ALDEHYDE REDUCTASE; 1.
DR PANTHER; PTHR42683:SF39; NADP-DEPENDENT ALCOHOL DEHYDROGENASE 6-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; PS00059; ADH_ZINC; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|RuleBase:RU361277};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000006753};
KW Zinc {ECO:0000256|RuleBase:RU361277}.
FT DOMAIN 16..345
FT /note="Enoyl reductase (ER)"
FT /evidence="ECO:0000259|SMART:SM00829"
SQ SEQUENCE 360 AA; 39116 MW; 6CAE77DC58E1C8C2 CRC64;
MVYPDTFEGF QIEDPKRWTD FKLNKLTPKP FGDFDVDVKI QACGVCASDL HTVSGGWGEQ
HFPLCVGHEI VGTALRVGPK VTLVKVGQRV GVGAQSYSCL DCRQCKNDNE TYCRHQLDTY
GAKWPDTGII SQGGYSSHVR THEHWVFPIP DGLSTAKAAP MLCAGLTAYS PLVRNGAGPG
KKVGVVGMGG IGHFGLLFSK ALGAETWAIS RTHSKEADAL KMGADGFLAT VDREWNKEHV
MTFDLIICTA SSTEGMDLGA YLQLLDVHGR FVSVGLPEGS GQEVKAQDFL SNGCLIGASH
LGSRKETLAM LQLAVEKGVE SWVEEIKISK EGLKEALTRV HNNDVKYRFT LTGYEEMFGA
//
