ID   A0A1G4BJT9_9PEZI        Unreviewed;       611 AA.
AC   A0A1G4BJT9;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   SubName: Full=Malic enzyme {ECO:0000313|EMBL:OHF01573.1};
GN   ORFNames=CORC01_03063 {ECO:0000313|EMBL:OHF01573.1};
OS   Colletotrichum orchidophilum.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum.
OX   NCBI_TaxID=1209926 {ECO:0000313|EMBL:OHF01573.1, ECO:0000313|Proteomes:UP000176998};
RN   [1] {ECO:0000313|EMBL:OHF01573.1, ECO:0000313|Proteomes:UP000176998}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IMI 309357 {ECO:0000313|EMBL:OHF01573.1,
RC   ECO:0000313|Proteomes:UP000176998};
RA   Capua I., De Benedictis P., Joannis T., Lombin L.H., Cattoli G.;
RL   Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
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}.
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:OHF01573.1}.
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DR   EMBL; MJBS01000018; OHF01573.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G4BJT9; -.
DR   STRING; 1209926.A0A1G4BJT9; -.
DR   OrthoDB; 1069499at2759; -.
DR   Proteomes; UP000176998; 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   GO; GO:0008152; P:metabolic process; IEA:UniProt.
DR   CDD; cd05312; NAD_bind_1_malic_enz; 1.
DR   Gene3D; 3.40.50.10380; Malic enzyme, N-terminal domain; 2.
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; 2.
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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000176998}.
FT   DOMAIN          119..279
FT                   /note="Malic enzyme N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01274"
FT   DOMAIN          289..550
FT                   /note="Malic enzyme NAD-binding"
FT                   /evidence="ECO:0000259|SMART:SM00919"
FT   ACT_SITE        142
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-1"
FT   ACT_SITE        193
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-1"
FT   BINDING         264
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT   BINDING         265
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT   BINDING         288
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT   BINDING         431
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
FT   BINDING         481
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
SQ   SEQUENCE   611 AA;  67308 MW;  B1D2A418AB289C83 CRC64;
     MLPRIIVNPL RNTITRRYHP SRLSHIMAPA KDRKEPKFSH LPLSTSGPIS CAVTGSALLN
     TPYLNKGTAF PEDERREFNL TGLLPQSIHS LDQQMHRAYE QYKSRQDDLA KNTFLTSLKE
     QNEVLYYRLL QAHLPEMFSI VYTPTEGDAI QNFSRLFRRP DGCFLNINDV DHGEEILGIG
     DQGVGGVLIS VAKLVLTTLC AGVHPNRTLP VVLDCGTDNE ELLNDDLYLG LRQKRVRGHK
     YDRFVDEFVK AARRLYPRAY IHFEDFGLTN ARRILDQYRP HIPCFNDDVQ GTGCVTLAAI
     TAALHVSKQK LTDLRLVVFG AGSAGVGIAD QVRDAIAAEG NMSKEDASKQ IWLIDKPGLL
     TTDSEVSAAQ KGFAKDPADW KDKDGSLLSV IKNVKPNVLI GTSTKPKAFT EEIVRAMAAG
     VERPIILPLS NPTRLHEAVP EDIYKWTDGK ALVATGSPFK PVKGPWGDGG KEIEIEVAEC
     NNSVVFPGIG LGSVLCRARL VTDKMLVAAV EGVASLSPAL KDQTAPLLPG VDVVRDVSVR
     VARAVIKAAI EEGVATEEGI PEGDEELDEW VREQMWSPEY RPLKLVEFSE ASREAKGEMK
     VAGSFSRVGS W
//