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Database: UniProt
Entry: A0A0R3WCB6_TAEAS
LinkDB: A0A0R3WCB6_TAEAS
Original site: A0A0R3WCB6_TAEAS 
ID   A0A0R3WCB6_TAEAS        Unreviewed;       582 AA.
AC   A0A0R3WCB6;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   RecName: Full=Malic enzyme {ECO:0000256|RuleBase:RU003426};
GN   ORFNames=TASK_LOCUS8340 {ECO:0000313|EMBL:VDK40066.1};
OS   Taenia asiatica (Asian tapeworm).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Cestoda;
OC   Eucestoda; Cyclophyllidea; Taeniidae; Taenia.
OX   NCBI_TaxID=60517 {ECO:0000313|Proteomes:UP000046400, ECO:0000313|WBParaSite:TASK_0000833901-mRNA-1};
RN   [1] {ECO:0000313|WBParaSite:TASK_0000833901-mRNA-1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (FEB-2017) to UniProtKB.
RN   [2] {ECO:0000313|EMBL:VDK40066.1, ECO:0000313|Proteomes:UP000282613}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG   Pathogen Informatics;
RL   Submitted (NOV-2018) 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; UYRS01018779; VDK40066.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0R3WCB6; -.
DR   STRING; 60517.A0A0R3WCB6; -.
DR   WBParaSite; TASK_0000833901-mRNA-1; TASK_0000833901-mRNA-1; TASK_0000833901.
DR   Proteomes; UP000046400; Unplaced.
DR   Proteomes; UP000282613; 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: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.
DR   PROSITE; PS00331; MALIC_ENZYMES; 1.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils};
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:UP000282613}.
FT   DOMAIN          86..267
FT                   /note="Malic enzyme N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01274"
FT   DOMAIN          277..535
FT                   /note="Malic enzyme NAD-binding"
FT                   /evidence="ECO:0000259|SMART:SM00919"
FT   COILED          55..82
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   ACT_SITE        109
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-1"
FT   ACT_SITE        180
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-1"
FT   BINDING         162
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
FT   BINDING         252
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT   BINDING         253
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT   BINDING         276
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT   BINDING         418
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
FT   BINDING         466
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
SQ   SEQUENCE   582 AA;  65259 MW;  817E9F4724022A3C CRC64;
     MRRSFVQFIS RRFLASEIHC YGVGVLRNPV TNKGTAFTIR ERQLLGIHGL LPPAVSDLDA
     QVKKMMNNLR RLEDDLQRYM FLIGLQDRNE TLFYKVVTEH TEYCMPLIYT PTVGLACQKY
     GLVFRRPRGL YITIHDRYNI DDILKNWPEP IVRTIVVTDG ERILGLGDLG AYGMGIPVGK
     LSLYSALAGV NPRHCLPIVL DVGSDNHDLL NDTHYLGISH KRIRDARYEE LLDNFMRAVV
     RRYGNNCLVQ FEDFGNRNAY RILERYRHDY CTFNDDIQGT ASVTVAGLIA AGRLTSRRLS
     DDTYLFVGAG EAASGIAHLL KTAMVMHGVP ECDAINKIYM FDKDGLLVQG RPEGNLDEHN
     STFARTDVEP MRNLEEIVRK LKPTVLIGAS GVGGLFTHRI LQQMKRNIDR PIIFALSNPT
     DKAECTAEAA YSTTGGACIF ASGSPFGEVT MNVGGQVKTF KPGQCNNSYI FPGVGLAITA
     CKLRPIPDEC FAVAADSLAD QVKEEDLALG RVFPPLSQIR PVSLAIAHRV AEFAYEQDVA
     HLIPKPENLE AYIQDQMYVP QYDSALPEFY EWPEEAIHKP YE
//
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