ID A0A0G4IYT0_PLABS Unreviewed; 531 AA.
AC A0A0G4IYT0;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=Malic enzyme {ECO:0008006|Google:ProtNLM};
GN ORFNames=PBRA_001572 {ECO:0000313|EMBL:CEP00518.1};
OS Plasmodiophora brassicae (Clubroot disease agent).
OC Eukaryota; Sar; Rhizaria; Endomyxa; Phytomyxea; Plasmodiophorida;
OC Plasmodiophoridae; Plasmodiophora.
OX NCBI_TaxID=37360 {ECO:0000313|EMBL:CEP00518.1, ECO:0000313|Proteomes:UP000039324};
RN [1] {ECO:0000313|EMBL:CEP00518.1, ECO:0000313|Proteomes:UP000039324}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=E3 {ECO:0000313|EMBL:CEP00518.1};
RA Chooi Y.-H.;
RL Submitted (FEB-2015) 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}.
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DR EMBL; CDSF01000101; CEP00518.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G4IYT0; -.
DR STRING; 37360.A0A0G4IYT0; -.
DR EnsemblProtists; CEP00518; CEP00518; PBRA_001572.
DR OMA; YYRMLME; -.
DR OrthoDB; 1069499at2759; -.
DR Proteomes; UP000039324; 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; 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:SF90; MALIC ENZYME-RELATED; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000039324}.
FT DOMAIN 50..233
FT /note="Malic enzyme N-terminal"
FT /evidence="ECO:0000259|SMART:SM01274"
FT DOMAIN 243..498
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 144
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-1"
FT BINDING 126
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
FT BINDING 218
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT BINDING 219
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT BINDING 242
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT BINDING 385
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
FT BINDING 429
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
SQ SEQUENCE 531 AA; 58021 MW; 60B1ACDA693B4F37 CRC64;
MSVPDREDRR LVGLVAPAVQ SRALQVQRCL RYLDAIDDRL QRFAFMQRLH SSDVDLFYML
LMTHPDTILP IVYTPAVGLA CQQWSHMYFE PQGLYVPISA RGAVRKVVDN WPGDEVDVVV
FTDGGRILGL GDLGANGMGI PIGKLALYVA FAGISPRRVL PVCLDVGTDN EQLLNDDLYI
GLKQRRSATS FEEYDAFVGE FMDAMADRFG RTTLMQFEDF GTQTALYLLG KYRSRFTTFN
DDVQGTAVMT LAGVMSSLPL LASPHLHEQR IVFFGAGSAG IGIADMISKA ISVSGGISFE
EARRRVWAVD SRGLIVANRP GRPLEPYKQG YAHEHEHIKD LLDIVNAIRP SILIGVSSQA
GAFNEQILAA MAMINKRPVV FALSNPTSQS ECTAEMAIVH TEGRALFASG SPFPPVTYRG
KEFDTSQANN VYVFPGIGLG ALASQALQIS DDMMVVAAKA LSSLVTDADR ERGNLFPPMD
GLRRVSARIG TAVAEAAFRS GLASIPRPDD VSLAVRRTMV YDPTQCLVSK M
//
