ID A0A0L6X069_9AGAR Unreviewed; 546 AA.
AC A0A0L6X069;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Malic enzyme {ECO:0000256|RuleBase:RU003426};
GN ORFNames=J132_03668 {ECO:0000313|EMBL:KNZ80968.1};
OS Termitomyces sp. J132.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Tricholomatineae; Lyophyllaceae;
OC Termitomyces.
OX NCBI_TaxID=1306850 {ECO:0000313|EMBL:KNZ80968.1, ECO:0000313|Proteomes:UP000053712};
RN [1] {ECO:0000313|Proteomes:UP000053712}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=J132 {ECO:0000313|Proteomes:UP000053712};
RA Hu H., Poulsen M.;
RT "The genome of Termitomyces.";
RL Submitted (JAN-2014) 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 -!- 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; KQ412216; KNZ80968.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0L6X069; -.
DR STRING; 1306850.A0A0L6X069; -.
DR OrthoDB; 1069499at2759; -.
DR Proteomes; UP000053712; 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:UP000053712}.
FT DOMAIN 48..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 71
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-1"
FT ACT_SITE 143
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-1"
FT BINDING 125
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 546 AA; 60609 MW; 9265BFC2839E54BA CRC64;
MTTIPYSSSP APRTPPYFFN TDHRQRCLEQ LRSKTDPLEK YIYLSGLKER DSNLFYEVLL
GNMLEIIPIL YTPTVGDACS QYSHIWRRPE GLYVGIQNRG RIRDVLRTWS GGVNSRIAVV
TDGSRILGLG DLGANGLPIS IGKLDLYIAG AGVSPATTVP ICLDLGTNTQ KFLDDPLYIG
ARRKRPGVEE ARMDLFMKEF MEAMKEVFPS LLVQFEDFST DNAFRYLDMF RSQYRCFNDD
IQGTGAVILS GFINAAKLSS AASGRPLTDH RILFFGAGSA GIGVAKQLTS FFKLLGMSED
EARSRIYTVD SKGLITADRK DLQEHKKYFA RTDYQGPPLK NLIDIIGYVK PTALLGLSTI
QNAFTEEVVR LMASVNTRPI IFPLSNPVSV CELGYTDAVQ WTNGSVIFAS GSPYKPVEHA
EKVYEPGQGN NMYIFPGIGL GTILSKARHV TDSMIEQASI ALSETLTEEE RSADLVYPRL
ARIREISALI ALAVIRAAQK DGVDENSSFR KMSDAALLDY VKTKQWQPHS TRPYENGNIN
GSTPRL
//
