ID M7U9Q0_BOTF1 Unreviewed; 686 AA.
AC M7U9Q0;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE SubName: Full=Putative nadp-dependent malic enzyme protein {ECO:0000313|EMBL:EMR83353.1};
GN ORFNames=BcDW1_8040 {ECO:0000313|EMBL:EMR83353.1};
OS Botryotinia fuckeliana (strain BcDW1) (Noble rot fungus) (Botrytis
OS cinerea).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Sclerotiniaceae; Botrytis.
OX NCBI_TaxID=1290391 {ECO:0000313|EMBL:EMR83353.1, ECO:0000313|Proteomes:UP000012045};
RN [1] {ECO:0000313|Proteomes:UP000012045}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BcDW1 {ECO:0000313|Proteomes:UP000012045};
RX PubMed=23704180; DOI=10.1128/genomea.00252-13;
RA Blanco-Ulate B., Allen G., Powell A.L., Cantu D.;
RT "Draft genome sequence of Botrytis cinerea BcDW1, inoculum for noble rot of
RT grape berries.";
RL Genome Announc. 1:E0025213-E0025213(2013).
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|PIRSR:PIRSR000106-3};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|PIRSR:PIRSR000106-3};
CC Note=Divalent metal cations. Prefers magnesium or manganese.
CC {ECO:0000256|PIRSR:PIRSR000106-3};
CC -!- SIMILARITY: Belongs to the malic enzymes family.
CC {ECO:0000256|ARBA:ARBA00008785}.
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DR EMBL; KB708011; EMR83353.1; -; Genomic_DNA.
DR AlphaFoldDB; M7U9Q0; -.
DR STRING; 1290391.M7U9Q0; -.
DR HOGENOM; CLU_011405_2_1_1; -.
DR Proteomes; UP000012045; Unassembled WGS sequence.
DR GO; GO:0004470; F:malic enzyme activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR CDD; cd05312; NAD_bind_1_malic_enz; 1.
DR Gene3D; 3.40.50.10380; Malic enzyme, N-terminal domain; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR046346; Aminoacid_DH-like_N_sf.
DR InterPro; IPR012301; Malic_N_dom.
DR InterPro; IPR037062; Malic_N_dom_sf.
DR InterPro; IPR012302; Malic_NAD-bd.
DR InterPro; IPR001891; Malic_OxRdtase.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR23406; MALIC ENZYME-RELATED; 1.
DR PANTHER; PTHR23406:SF32; NAD-DEPENDENT MALIC ENZYME, MITOCHONDRIAL; 1.
DR Pfam; PF00390; malic; 1.
DR Pfam; PF03949; Malic_M; 1.
DR PIRSF; PIRSF000106; ME; 1.
DR PRINTS; PR00072; MALOXRDTASE.
DR SMART; SM01274; malic; 1.
DR SMART; SM00919; Malic_M; 1.
DR SUPFAM; SSF53223; Aminoacid dehydrogenase-like, N-terminal domain; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|PIRSR:PIRSR000106-3}.
FT DOMAIN 188..368
FT /note="Malic enzyme N-terminal"
FT /evidence="ECO:0000259|SMART:SM01274"
FT DOMAIN 377..650
FT /note="Malic enzyme NAD-binding"
FT /evidence="ECO:0000259|SMART:SM00919"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 211
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-1"
FT ACT_SITE 282
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-1"
FT BINDING 264
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
FT BINDING 353
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT BINDING 354
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT BINDING 376
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT BINDING 525
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
FT BINDING 581
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
SQ SEQUENCE 686 AA; 75574 MW; 7208330E9BA109C1 CRC64;
MASSYNYSTS SSEVGTPYTP RSSSPTYSVA SRSSSTTISK RISISTSRRN TAMNPIGGID
IAAIEAAMKQ SSLDHLKGYS QTNYPTVTQS NDTEYISQES AQGYQVLREP AWNKGTFSSS
LSLAFPTLQI SDSQKGTSFT PEDRVNKNLT GLIPHVLESL ETQCIRAMRM INSRTTPIDK
YLYLSNIKAQ NTDLFYRLLI DNIATLMPLV YTPTIGDVCL QYSTLYTRPE ALYISIKQRK
SMTTILRNWP YPNPSICVVT DGSRILGLGD LGVNGVGISI GKLALYTGAA GIHPSQTLPI
VLDCGTANEE NLRDPLYLGL RMKRPGPEIE QQFMDEFMAA VKEVYPDMLV QFEDFESEKA
FKYLDRYKKE KMFNDDIQGT GAVVLAGYIG AVNLSGVPIE DQRLVFMGAG SAGVGVAKQV
MEYYTRRGLS EKDARDKFWL VDTKGLVTTD RGDKLAAHKK IFARDDNHGH QFATLEEVIE
YVKPTALIGL TATFGVFTES VVRALKGSVD AGGLGRRPIL FPLSNPLTKA ECTFEQAITW
TEGTVIFASG SPFSPVTIKH SDSSSSLSSE NSTTYYPNQG NNVYVFPGLG LGAILAKASR
VTDAMVYQSA EALSGCLNRE ELMMGLIYPK IGRVRDASVV VAREVMKAAR REGVSGLSEE
CWAVWEEWGD VALENWIKKQ VYDPRW
//
