ID A0A0D7ANH0_9AGAR Unreviewed; 528 AA.
AC A0A0D7ANH0;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Malic enzyme {ECO:0000256|RuleBase:RU003426};
GN ORFNames=FISHEDRAFT_63445 {ECO:0000313|EMBL:KIY53284.1};
OS Fistulina hepatica ATCC 64428.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Fistulinaceae; Fistulina.
OX NCBI_TaxID=1128425 {ECO:0000313|EMBL:KIY53284.1, ECO:0000313|Proteomes:UP000054144};
RN [1] {ECO:0000313|EMBL:KIY53284.1, ECO:0000313|Proteomes:UP000054144}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 64428 {ECO:0000313|EMBL:KIY53284.1,
RC ECO:0000313|Proteomes:UP000054144};
RX PubMed=25683379; DOI=10.1016/j.fgb.2015.02.002;
RA Floudas D., Held B.W., Riley R., Nagy L.G., Koehler G., Ransdell A.S.,
RA Younus H., Chow J., Chiniquy J., Lipzen A., Tritt A., Sun H., Haridas S.,
RA LaButti K., Ohm R.A., Kues U., Blanchette R.A., Grigoriev I.V., Minto R.E.,
RA Hibbett D.S.;
RT "Evolution of novel wood decay mechanisms in Agaricales revealed by the
RT genome sequences of Fistulina hepatica and Cylindrobasidium torrendii.";
RL Fungal Genet. Biol. 76:78-92(2015).
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 -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|ARBA:ARBA00001936};
CC -!- SIMILARITY: Belongs to the malic enzymes family.
CC {ECO:0000256|ARBA:ARBA00008785, ECO:0000256|RuleBase:RU003426}.
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DR EMBL; KN881627; KIY53284.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0D7ANH0; -.
DR OrthoDB; 1069499at2759; -.
DR Proteomes; UP000054144; 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; IPR015884; Malic_enzyme_CS.
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.
DR PROSITE; PS00331; MALIC_ENZYMES; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR000106-3};
KW Oxidoreductase {ECO:0000256|RuleBase:RU003426};
KW Reference proteome {ECO:0000313|Proteomes:UP000054144}.
FT DOMAIN 50..231
FT /note="Malic enzyme N-terminal"
FT /evidence="ECO:0000259|SMART:SM01274"
FT DOMAIN 241..499
FT /note="Malic enzyme NAD-binding"
FT /evidence="ECO:0000259|SMART:SM00919"
FT ACT_SITE 73
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-1"
FT ACT_SITE 145
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-1"
FT BINDING 127
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
FT BINDING 216
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT BINDING 217
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT BINDING 240
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT BINDING 386
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
FT BINDING 430
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
SQ SEQUENCE 528 AA; 58369 MW; 6F83C7FCBFC56C85 CRC64;
MSSLTVRRPE LKRGLTPPML DEKLHIERCL EQLHSKDKPI EKYIYLSSLK ERDQSMFYKL
CLAHMSEFTP IIYTPVVGDA CLQFSHIYRR PEGLFVSIED KGRIGKVLSN WPAIDNARIS
VVTDGSRILG LGDLGVNGMP IAVGKLSLYV AGAGIDPAST LPICLDLGTN TQKFLDDPLY
LGARRKRPAT AEMDEFMDEF MHEMATRFPK LVVQFEDFST DNAFRYLARY RNKYATFNDD
IQGTGAVVLS GFLNAAKLSA AASGRALGDQ RILFFGAGSA GVGVAMQLMS FFRLQGMSEE
EARNRVWLVD SQGLVYDARG RLPEHKKYFS RRDYTGPPMK NLLEIVEYVK PTALLGLSTI
ANAFTPAVLA KLAEINPRPI VFPLSNPVRL SECSFEDAVA NTNGSVLFAS GSPFDEIKRN
GKTLYPGQGN NMYIFPGLGL GSILSEASAI TDAMVEAASY GLAESLTKEE RAQDLLYPRI
ERIREISAFI AAQVIATAQK AGVAHNEKLR GKPLSELVDY AKGKMWYP
//
