ID   A0A161VML2_9PEZI        Unreviewed;       748 AA.
AC   A0A161VML2;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   SubName: Full=Malic enzyme {ECO:0000313|EMBL:KZL72235.1};
DE   Flags: Fragment;
GN   ORFNames=CT0861_00638 {ECO:0000313|EMBL:KZL72235.1};
OS   Colletotrichum tofieldiae.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC   Colletotrichum spaethianum species complex.
OX   NCBI_TaxID=708197 {ECO:0000313|EMBL:KZL72235.1, ECO:0000313|Proteomes:UP000076552};
RN   [1] {ECO:0000313|EMBL:KZL72235.1, ECO:0000313|Proteomes:UP000076552}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=0861 {ECO:0000313|EMBL:KZL72235.1,
RC   ECO:0000313|Proteomes:UP000076552};
RA   Hacquard S., Kracher B., Hiruma K., Weinman A., Muench P., Garrido Oter R.,
RA   Ver Loren van Themaat E., Dallerey J.-F., Damm U., Henrissat B.,
RA   Lespinet O., Thon M., Kemen E., McHardy A.C., Schulze-Lefert P.,
RA   O'Connell R.J.;
RT   "Survival trade-offs in plant roots during colonization by closely related
RT   pathogenic and mutualistic fungi.";
RL   Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the malic enzymes family.
CC       {ECO:0000256|ARBA:ARBA00008785}.
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:KZL72235.1}.
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DR   EMBL; LFIV01000062; KZL72235.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A161VML2; -.
DR   STRING; 708197.A0A161VML2; -.
DR   OrthoDB; 1069499at2759; -.
DR   Proteomes; UP000076552; Unassembled WGS sequence.
DR   GO; GO:0004470; F:malic enzyme activity; IEA:InterPro.
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   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   Reference proteome {ECO:0000313|Proteomes:UP000076552}.
FT   DOMAIN          249..429
FT                   /note="Malic enzyme N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01274"
FT   DOMAIN          439..705
FT                   /note="Malic enzyme NAD-binding"
FT                   /evidence="ECO:0000259|SMART:SM00919"
FT   REGION          1..26
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          89..134
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KZL72235.1"
SQ   SEQUENCE   748 AA;  83251 MW;  51471611D3868C68 CRC64;
     PRPHHTLNYS PAPSPKSAPS SPPHQRLITR PGRSHYTTIH TPHHARLLRL RAPTTTNCLV
     PSPTPASSFF SASLPPTHAP VMSMASYPFS SASSSDISTP RSASPSPSSV ASARSSRSSI
     SNKRMSMSSR RMTDFNPMSS VDISAIEEKM RMSALDQHRG YAQNTFGEVQ QYRTTEYVPK
     TQATAYQILR EPLWNKGLSF TPEERVTRNL TGLIPHTMES LQTQCQRAMK MINTRQTDVD
     KYLYLSSLKA QNFDLFYRLL IDNIRELMPL VYTPTIGDVC LQYSTLYTRP EALYISIKQR
     KSIRTMLRNW PYPNPQICVV TDGSRILGLG DLGVNGVGIS IGKLALYTGA AGIHPENTLP
     IVLDTGTNNE TNLKDPFYLG IRSKRVSVAE QQAFMDEFME AVTEVYPNMT VQFEDFESEK
     AFNYLDRYRN KYRCFNDDIQ GTGAVVLAGY INAVELSGVP LEEQRLVFMG AGSAGVGVAK
     QLVEYYTKRG LSEQVARDKF WLVDTKGLVT KDRGDKLAEH KKYFARTDNN GHQFRTLEEV
     IEYVKPTALV GLTATFGVFT ESVVRALKAS VDSGGLGRRP VLFPLSNPLT KAECTFEQAV
     QWTDGTVIFA SGSPFSPFTM KTPDGQAITY HPNQGNNVYV FPGLGLGAIL AKASKVTDDM
     VYTSAAALAA GLNADEIHKG LIYPRIERVR DASVIVAREV MKSARRDGVS TLPESQWVEW
     EEWGDVALDA WIKERIYDPV SFSEKSRI
//