ID   A0A0B2UWI4_TOXCA        Unreviewed;       702 AA.
AC   A0A0B2UWI4;
DT   04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT   04-MAR-2015, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   RecName: Full=Malate dehydrogenase, mitochondrial {ECO:0000256|ARBA:ARBA00016075};
DE            EC=1.1.1.37 {ECO:0000256|ARBA:ARBA00012995};
GN   Name=mdh-2 {ECO:0000313|EMBL:KHN73604.1};
GN   ORFNames=Tcan_06236 {ECO:0000313|EMBL:KHN73604.1};
OS   Toxocara canis (Canine roundworm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Spirurina; Ascaridomorpha; Ascaridoidea; Toxocaridae; Toxocara.
OX   NCBI_TaxID=6265 {ECO:0000313|EMBL:KHN73604.1, ECO:0000313|Proteomes:UP000031036};
RN   [1] {ECO:0000313|EMBL:KHN73604.1, ECO:0000313|Proteomes:UP000031036}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PN_DK_2014 {ECO:0000313|EMBL:KHN73604.1};
RA   Zhu X.-Q., Korhonen P.K., Cai H., Young N.D., Nejsum P.,
RA   von Samson-Himmelstjerna G., Boag P.R., Tan P., Li Q., Min J., Yang Y.,
RA   Wang X., Fang X., Hall R.S., Hofmann A., Sternberg P.W., Jex A.R.,
RA   Gasser R.B.;
RT   "Genetic blueprint of the zoonotic pathogen Toxocara canis.";
RL   Submitted (NOV-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC   -!- SIMILARITY: Belongs to the LDH/MDH superfamily. MDH type 1 family.
CC       {ECO:0000256|ARBA:ARBA00008824}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KHN73604.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; JPKZ01003101; KHN73604.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0B2UWI4; -.
DR   STRING; 6265.A0A0B2UWI4; -.
DR   Proteomes; UP000031036; Unassembled WGS sequence.
DR   GO; GO:0005763; C:mitochondrial small ribosomal subunit; IEA:InterPro.
DR   GO; GO:0030060; F:L-malate dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
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; IPR026299; MRP-S31.
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   Pfam; PF15433; MRP-S31; 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   Reference proteome {ECO:0000313|Proteomes:UP000031036};
KW   Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532}.
FT   DOMAIN          30..172
FT                   /note="Lactate/malate dehydrogenase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00056"
FT   DOMAIN          174..334
FT                   /note="Lactate/malate dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02866"
SQ   SEQUENCE   702 AA;  76738 MW;  ACE2935CDB5E662E CRC64;
     MALAAAKSVP TVVSNGIRII SQRANSSAPK VALLGAAGGI GQPLALLLKQ NSSIARLALY
     DLKGTPGVAA DLSHIDTRAQ VTGHTGTNEL KAALEGADVV VIPAGVPRKP GMTRDDLFNT
     NAGIVRDLCD AAAKTCPKAL LAIITNPVNS TVPIACEVFR KNGVLDTNRI FGVTMLDILR
     SQTFVAELKG LDVTKTHVPV IGGHSGVTII PLLSQTKPSC KFTEEEAKNL TTRIQDAGTE
     VVKAKAGAGS ATLSMALAGA RFVEGLVNGL KGQKNVLCAY IASDAMKGLD YFSTPVELGP
     NGVEKILGTG KLSAYEQSLV EKAIPELKKN ITKALFSKKE EKRPKQPKSV ELLGEKLLEA
     VENVAGELHR DDADAKKSTK RDLIAKLTEH EKETFHAATD SQVEEMLSDK NIVNILSGAS
     KQKAIPASRA AEVRHARRGL LLLRREIFYQ AKQSGYSASD ARAIAERAVA AAEARSIAQH
     TEKETKRTTE LEERIAAERA ANEKEQKFYD YAFRMADKML YPEDYRTGAA GERAEVTIQP
     DPKVKNIFSL DQPRLGIFNE DNLSKLKDHS LQFWADWDAH AARTWNQSFG PTNGFEEMID
     LTEKGKMWPY PIDNEYLLGE EEDVGFHEHI FLERTLSQYK LPKSGPIAHF MELVCVGLSK
     NPYMTAEKKR SHIQWFADYF NEKKTAEIEQ LHKQEQIAAG SA
//