ID E2RU65_GIAIC Unreviewed; 331 AA.
AC E2RU65;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 64.
DE SubName: Full=Malate dehydrogenase {ECO:0000313|EMBL:EDO79444.1};
DE EC=1.1.1.37 {ECO:0000313|EMBL:EDO79444.1};
GN ORFNames=GL50803_003331 {ECO:0000313|EMBL:KAE8302233.1}, GL50803_3331
GN {ECO:0000313|EMBL:EDO79444.1};
OS Giardia intestinalis (strain ATCC 50803 / WB clone C6) (Giardia lamblia).
OC Eukaryota; Metamonada; Diplomonadida; Hexamitidae; Giardiinae; Giardia.
OX NCBI_TaxID=184922 {ECO:0000313|EMBL:EDO79444.1};
RN [1] {ECO:0000313|EMBL:EDO79444.1, ECO:0000313|Proteomes:UP000001548}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 50803 / WB clone C6 {ECO:0000313|Proteomes:UP000001548},
RC and WB C6 {ECO:0000313|EMBL:EDO79444.1};
RX PubMed=17901334; DOI=10.1126/science.1143837;
RA Morrison H.G., McArthur A.G., Gillin F.D., Aley S.B., Adam R.D.,
RA Olsen G.J., Best A.A., Cande W.Z., Chen F., Cipriano M.J., Davids B.J.,
RA Dawson S.C., Elmendorf H.G., Hehl A.B., Holder M.E., Huse S.M., Kim U.U.,
RA Lasek-Nesselquist E., Manning G., Nigam A., Nixon J.E., Palm D.,
RA Passamaneck N.E., Prabhu A., Reich C.I., Reiner D.S., Samuelson J.,
RA Svard S.G., Sogin M.L.;
RT "Genomic minimalism in the early diverging intestinal parasite Giardia
RT lamblia.";
RL Science 317:1921-1926(2007).
RN [2] {ECO:0000313|EMBL:KAE8302233.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=WB C6 {ECO:0000313|EMBL:KAE8302233.1};
RA Xu F., Jex A., Svard S.G.;
RT "New Giardia intestinalis WB genome in near-complete chromosomes.";
RL Submitted (JUL-2019) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the LDH/MDH superfamily. MDH type 2 family.
CC {ECO:0000256|ARBA:ARBA00009613}.
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:EDO79444.1}.
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DR EMBL; AACB02000016; EDO79444.1; -; Genomic_DNA.
DR EMBL; AACB03000004; KAE8302233.1; -; Genomic_DNA.
DR RefSeq; XP_001707118.1; XM_001707066.1.
DR AlphaFoldDB; E2RU65; -.
DR SMR; E2RU65; -.
DR STRING; 184922.E2RU65; -.
DR EnsemblProtists; EDO79444; EDO79444; GL50803_3331.
DR GeneID; 5700025; -.
DR KEGG; gla:GL50803_003331; -.
DR VEuPathDB; GiardiaDB:GL50803_3331; -.
DR HOGENOM; CLU_040727_2_0_1; -.
DR InParanoid; E2RU65; -.
DR OMA; DHMRDWT; -.
DR Proteomes; UP000001548; Chromosome 2.
DR GO; GO:0030060; F:L-malate dehydrogenase activity; IBA:GO_Central.
DR GO; GO:0006108; P:malate metabolic process; IBA:GO_Central.
DR GO; GO:0006734; P:NADH metabolic process; IBA:GO_Central.
DR GO; GO:0006107; P:oxaloacetate metabolic process; IBA:GO_Central.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IBA:GO_Central.
DR CDD; cd00704; MDH; 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; IPR001557; L-lactate/malate_DH.
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; IPR010945; Malate_DH_type2.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR NCBIfam; TIGR01759; MalateDH-SF1; 1.
DR PANTHER; PTHR23382; MALATE DEHYDROGENASE; 1.
DR PANTHER; PTHR23382:SF0; MALATE DEHYDROGENASE 2, MITOCHONDRIAL-RELATED; 1.
DR Pfam; PF02866; Ldh_1_C; 1.
DR Pfam; PF00056; Ldh_1_N; 1.
DR PIRSF; PIRSF000102; Lac_mal_DH; 1.
DR SUPFAM; SSF56327; LDH C-terminal domain-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE 3: Inferred from homology;
KW NAD {ECO:0000256|PIRSR:PIRSR000102-3};
KW Oxidoreductase {ECO:0000256|RuleBase:RU003369,
KW ECO:0000313|EMBL:EDO79444.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001548}.
FT DOMAIN 7..150
FT /note="Lactate/malate dehydrogenase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00056"
FT DOMAIN 158..328
FT /note="Lactate/malate dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02866"
FT ACT_SITE 188
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000102-1"
FT BINDING 93
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000102-2"
FT BINDING 99
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000102-2"
FT BINDING 106
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
FT BINDING 130..132
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
FT BINDING 132
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000102-2"
FT BINDING 163
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000102-2"
SQ SEQUENCE 331 AA; 35494 MW; 0969226853D09E1C CRC64;
MTKPVLRVCI SGAAGQICYS VLFRIAAGDM LGYDQPVHIV MLEVPAALKA AEGVAMELVD
CAFPLLSGFT LTSDNAEAFK DVDYCLLFGA FPRKAGMERA ELLSKNKGIF QIQGAAINEH
AKPTCRILVI GNPANTNALV LSTQLTKIPK TNVTAMSRLD HNRAVGQVAG KLGVRTNRIS
NVWVAGNHSN TMVPIVDCGV IYDEGLKDKQ PVKPMLPADW IKGEFVPCVR GRGTAVIEAR
GHSSSASAAN AAIDHVRDWH MGTKPGAFVS CSLLIEEGNP YGIAPGIFYS MPCSCVGGKW
QIVKLDLPKD VLDEMKLSEA ELMKEAADAL K
//
