ID MDH_PYRIL Reviewed; 309 AA.
AC A1RS58;
DT 13-APR-2016, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 27-MAR-2024, entry version 92.
DE RecName: Full=Malate dehydrogenase {ECO:0000303|PubMed:17487443};
DE EC=1.1.1.37 {ECO:0000269|PubMed:17487443};
GN Name=mdh {ECO:0000303|PubMed:17487443};
GN OrderedLocusNames=Pisl_0612 {ECO:0000312|EMBL:ABL87790.1};
OS Pyrobaculum islandicum (strain DSM 4184 / JCM 9189 / GEO3).
OC Archaea; Thermoproteota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC Pyrobaculum.
OX NCBI_TaxID=384616;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 4184 / JCM 9189 / GEO3;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Dalin E., Tice H., Pitluck S., Meincke L., Brettin T.,
RA Bruce D., Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Mikhailova N., Lowe T., Richardson P.;
RT "Complete sequence of Pyrobaculum islandicum DSM 4184.";
RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RC STRAIN=DSM 4184 / JCM 9189 / GEO3;
RX PubMed=17487443; DOI=10.1007/s00792-007-0081-2;
RA Yennaco L.J., Hu Y., Holden J.F.;
RT "Characterization of malate dehydrogenase from the hyperthermophilic
RT archaeon Pyrobaculum islandicum.";
RL Extremophiles 11:741-746(2007).
CC -!- FUNCTION: Catalyzes the reversible oxidation of malate to oxaloacetate.
CC Exhibits higher specific activity for oxaloacetate reduction than for
CC malate oxidation in vitro. Has a strong preference for NAD. Can use
CC NADPH for oxaloacetate reduction, but activity decreases more than 90%.
CC No activity detected with NADP(+) and malate.
CC {ECO:0000269|PubMed:17487443}.
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:0000269|PubMed:17487443};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.015 mM for oxaloacetate {ECO:0000269|PubMed:17487443};
CC KM=0.086 mM for NADH {ECO:0000269|PubMed:17487443};
CC KM=0.5 mM for malate {ECO:0000269|PubMed:17487443};
CC KM=0.028 mM for NAD(+) {ECO:0000269|PubMed:17487443};
CC pH dependence:
CC Optimum pH is 10.0. {ECO:0000269|PubMed:17487443};
CC Temperature dependence:
CC Optimum temperature is above 92 degrees Celsius.
CC {ECO:0000269|PubMed:17487443};
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:17487443}.
CC -!- SIMILARITY: Belongs to the LDH/MDH superfamily. {ECO:0000305}.
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DR EMBL; CP000504; ABL87790.1; -; Genomic_DNA.
DR RefSeq; WP_011762366.1; NC_008701.1.
DR AlphaFoldDB; A1RS58; -.
DR SMR; A1RS58; -.
DR STRING; 384616.Pisl_0612; -.
DR GeneID; 4617605; -.
DR KEGG; pis:Pisl_0612; -.
DR eggNOG; arCOG00246; Archaea.
DR HOGENOM; CLU_045401_2_1_2; -.
DR OrthoDB; 2596at2157; -.
DR Proteomes; UP000002595; Chromosome.
DR GO; GO:0030060; F:L-malate dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0019752; P:carboxylic acid metabolic process; IEA:InterPro.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-KW.
DR CDD; cd01339; LDH-like_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; IPR011275; Malate_DH_type3.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR43128; L-2-HYDROXYCARBOXYLATE DEHYDROGENASE (NAD(P)(+)); 1.
DR PANTHER; PTHR43128:SF34; L-LACTATE DEHYDROGENASE; 1.
DR Pfam; PF02866; Ldh_1_C; 1.
DR Pfam; PF00056; Ldh_1_N; 1.
DR PIRSF; PIRSF000102; Lac_mal_DH; 1.
DR PRINTS; PR00086; LLDHDRGNASE.
DR SUPFAM; SSF56327; LDH C-terminal domain-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE 1: Evidence at protein level;
KW NAD; Oxidoreductase; Tricarboxylic acid cycle.
FT CHAIN 1..309
FT /note="Malate dehydrogenase"
FT /id="PRO_0000436036"
FT ACT_SITE 173
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P61889"
FT BINDING 6..11
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:O08349"
FT BINDING 31
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:O08349"
FT BINDING 80
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P61889"
FT BINDING 86
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P61889"
FT BINDING 93
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:O08349"
FT BINDING 116..118
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:O08349"
FT BINDING 118
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P61889"
FT BINDING 149
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P61889"
SQ SEQUENCE 309 AA; 33532 MW; D2B35CCC1CF0E671 CRC64;
MITIIGSGRV GTAAAVIMGL LKIDTKILLI DIIKGLPQGE ALDMNHMSSI LGLDVEYFGS
NEYKDMEGSD LVIVTAGLPR KPGMTREQLL EANAKIVSEI GKEIKRYAPN SVVILTTNPL
DAMTYVMWKS TGFPRERVIG FSGVLDAGRL AYYAAKKLGV SPASILPIVL GQHGESMFPV
PSKSFIHGVP LSRLLTEEQL KEVVEETVKA GARITELRGF SSNWGPGAGL ALMAEAVKRD
TKRSLIASVV LQGEYDVRDV PVEVPVILGR SGVLKVLEIE LSAEERQKFM QSVEAIRKLI
ASIPSNYLQ
//
