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Database: UniProt
Entry: A0A068Y1E9_ECHMU
LinkDB: A0A068Y1E9_ECHMU
Original site: A0A068Y1E9_ECHMU 
ID   A0A068Y1E9_ECHMU        Unreviewed;       375 AA.
AC   A0A068Y1E9;
DT   01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 48.
DE   RecName: Full=Malate dehydrogenase {ECO:0000256|RuleBase:RU003405};
DE            EC=1.1.1.37 {ECO:0000256|RuleBase:RU003405};
GN   ORFNames=EmuJ_001185100 {ECO:0000313|EMBL:CDS35894.1};
OS   Echinococcus multilocularis (Fox tapeworm).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Cestoda;
OC   Eucestoda; Cyclophyllidea; Taeniidae; Echinococcus.
OX   NCBI_TaxID=6211 {ECO:0000313|EMBL:CDS35894.1};
RN   [1] {ECO:0000313|EMBL:CDS35894.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=23485966; DOI=10.1038/nature12031;
RA   Tsai I.J., Zarowiecki M., Holroyd N., Garciarrubio A., Sanchez-Flores A.,
RA   Brooks K.L., Tracey A., Bobes R.J., Fragoso G., Sciutto E., Aslett M.,
RA   Beasley H., Bennett H.M., Cai J., Camicia F., Clark R., Cucher M.,
RA   De Silva N., Day T.A., Deplazes P., Estrada K., Fernandez C., Holland P.W.,
RA   Hou J., Hu S., Huckvale T., Hung S.S., Kamenetzky L., Keane J.A., Kiss F.,
RA   Koziol U., Lambert O., Liu K., Luo X., Luo Y., Macchiaroli N., Nichol S.,
RA   Paps J., Parkinson J., Pouchkina-Stantcheva N., Riddiford N., Rosenzvit M.,
RA   Salinas G., Wasmuth J.D., Zamanian M., Zheng Y., Cai X., Soberon X.,
RA   Olson P.D., Laclette J.P., Brehm K., Berriman M., Garciarrubio A.,
RA   Bobes R.J., Fragoso G., Sanchez-Flores A., Estrada K., Cevallos M.A.,
RA   Morett E., Gonzalez V., Portillo T., Ochoa-Leyva A., Jose M.V., Sciutto E.,
RA   Landa A., Jimenez L., Valdes V., Carrero J.C., Larralde C.,
RA   Morales-Montor J., Limon-Lason J., Soberon X., Laclette J.P.;
RT   "The genomes of four tapeworm species reveal adaptations to parasitism.";
RL   Nature 496:57-63(2013).
RN   [2] {ECO:0000313|EMBL:CDS35894.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Zhang Y., Guo Z.;
RL   Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(S)-malate + NAD(+) = H(+) + NADH + oxaloacetate;
CC         Xref=Rhea:RHEA:21432, ChEBI:CHEBI:15378, ChEBI:CHEBI:15589,
CC         ChEBI:CHEBI:16452, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.37;
CC         Evidence={ECO:0000256|RuleBase:RU003405};
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC   -!- SIMILARITY: Belongs to the LDH/MDH superfamily. MDH type 1 family.
CC       {ECO:0000256|ARBA:ARBA00008824}.
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DR   EMBL; LN902841; CDS35894.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A068Y1E9; -.
DR   STRING; 6211.A0A068Y1E9; -.
DR   eggNOG; KOG1494; Eukaryota.
DR   OMA; GIARCCP; -.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0030060; F:L-malate dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006108; P:malate metabolic process; IEA:InterPro.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-KW.
DR   CDD; cd01337; MDH_glyoxysomal_mitochondrial; 1.
DR   Gene3D; 3.90.110.10; Lactate dehydrogenase/glycoside hydrolase, family 4, C-terminal; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR022383; Lactate/malate_DH_C.
DR   InterPro; IPR001236; Lactate/malate_DH_N.
DR   InterPro; IPR015955; Lactate_DH/Glyco_Ohase_4_C.
DR   InterPro; IPR001252; Malate_DH_AS.
DR   InterPro; IPR010097; Malate_DH_type1.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   NCBIfam; TIGR01772; MDH_euk_gproteo; 1.
DR   PANTHER; PTHR11540; MALATE AND LACTATE DEHYDROGENASE; 1.
DR   PANTHER; PTHR11540:SF16; MALATE DEHYDROGENASE, MITOCHONDRIAL; 1.
DR   Pfam; PF02866; Ldh_1_C; 1.
DR   Pfam; PF00056; Ldh_1_N; 1.
DR   SUPFAM; SSF56327; LDH C-terminal domain-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   PROSITE; PS00068; MDH; 1.
PE   3: Inferred from homology;
KW   Membrane {ECO:0000256|SAM:Phobius}; NAD {ECO:0000256|RuleBase:RU003405};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU003369};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius};
KW   Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532,
KW   ECO:0000256|RuleBase:RU003405}.
FT   TRANSMEM        325..347
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        353..374
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          27..169
FT                   /note="Lactate/malate dehydrogenase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00056"
FT   DOMAIN          171..316
FT                   /note="Lactate/malate dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02866"
SQ   SEQUENCE   375 AA;  39756 MW;  A16833FACCBD5CC2 CRC64;
     MNCLRKIGFV LGRSAKLFST STQNPQKIAI LGASGGIGQP LALLMKQSLF VSEIALYDIA
     NAAGVAADLS HIETRAKVTG HTGPDNLKAA LDGAKVVIIP AGVPRKPGMT RDDLFSMNAS
     VVADLSRACG KYCSDAMICI VTNPVNSTVP IAAEILKKEG VYNPRRLFGV TTLDITRSNT
     FIAEAKGLDV SKVSCPVIGG HSGNTIVPVL SQCTPSVNFA QKAREELVAR IQNAGTEVVN
     AKAGAGSATL SMAYAGARFA NSLLHAMKGH ADIVECAFVE CDVAETEFFA SPVLLGPNGV
     EKVFGAGKLN ERASRKARSL RPPTSLYIVL LFFLIPSRTF SVLTPLWFLD TSILLLLPSY
     CDPIIISCAC FAFYN
//
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