ID D8LY89_BLAHO Unreviewed; 338 AA.
AC D8LY89;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 24-JAN-2024, entry version 54.
DE RecName: Full=Malate dehydrogenase {ECO:0008006|Google:ProtNLM};
GN ORFNames=GSBLH_T00000858001 {ECO:0000313|EMBL:CBK20544.2};
OS Blastocystis hominis.
OC Eukaryota; Sar; Stramenopiles; Bigyra; Opalozoa; Opalinata; Blastocystidae;
OC Blastocystis.
OX NCBI_TaxID=12968 {ECO:0000313|EMBL:CBK20544.2};
RN [1] {ECO:0000313|EMBL:CBK20544.2}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Singapore isolate B {ECO:0000313|EMBL:CBK20544.2};
RA Wincker P.;
RT "Sequencing and annotation of the Blastocystis hominis genome.";
RL Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the LDH/MDH superfamily. MDH type 2 family.
CC {ECO:0000256|ARBA:ARBA00009613}.
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DR EMBL; FN668639; CBK20544.2; -; Genomic_DNA.
DR RefSeq; XP_012894592.1; XM_013039138.1.
DR AlphaFoldDB; D8LY89; -.
DR EnsemblProtists; CBK20544; CBK20544; GSBLH_T00000858001.
DR GeneID; 24918146; -.
DR InParanoid; D8LY89; -.
DR OMA; CATLANQ; -.
DR OrthoDB; 501358at2759; -.
DR Proteomes; UP000008312; Unassembled WGS sequence.
DR GO; GO:0016615; F:malate dehydrogenase activity; 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:0006108; P:malate metabolic process; IEA:InterPro.
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 PANTHER; PTHR23382; MALATE DEHYDROGENASE; 1.
DR PANTHER; PTHR23382:SF3; MALATE DEHYDROGENASE, CYTOPLASMIC; 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 Reference proteome {ECO:0000313|Proteomes:UP000008312}.
FT DOMAIN 5..150
FT /note="Lactate/malate dehydrogenase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00056"
FT DOMAIN 183..326
FT /note="Lactate/malate dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02866"
FT ACT_SITE 191
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000102-1"
FT BINDING 10..16
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
FT BINDING 41
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
FT BINDING 103
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
FT BINDING 127..129
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
SQ SEQUENCE 338 AA; 37196 MW; E6A20C71D6491696 CRC64;
MKCLRVVVSG AAGLIGYSLS GLLGDGTVFG TDRLVELVLH DIPRCEQKLV ALKAELEDCA
FPYVSSIEFF TDPLNAFRDA DIVFFLASLP LTGPDRASLL EKNINIYIEF GKALEQVASR
TCKSIVVANP ANTLAYVLMQ TAPSIPRSNF AALNRTDHNR TRSLTLDACR KAYDASLQLS
DLSDTFVWGN HGNTMFADLT HAKIRGIPLM EAIPDRELWE KTLPEQVERR GWVLMELRGG
VSSVLSVARA SVDVARDWCL GTNGKRITMA VCSDGNCYGV EEGLIFGMPV VCENGEWKCV
EGLKIAENVR KHIEITTQDL KKEVEIADAA IERAKNNN
//