ID   MDH_PYRAB               Reviewed;         362 AA.
AC   Q9V0D5; G8ZH65;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   25-MAY-2022, entry version 106.
DE   RecName: Full=Malate dehydrogenase;
DE            EC=1.1.1.37;
GN   Name=mdh; OrderedLocusNames=PYRAB08550; ORFNames=PAB1791;
OS   Pyrococcus abyssi (strain GE5 / Orsay).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Pyrococcus.
OX   NCBI_TaxID=272844;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GE5 / Orsay;
RX   PubMed=12622808; DOI=10.1046/j.1365-2958.2003.03381.x;
RA   Cohen G.N., Barbe V., Flament D., Galperin M., Heilig R., Lecompte O.,
RA   Poch O., Prieur D., Querellou J., Ripp R., Thierry J.-C., Van der Oost J.,
RA   Weissenbach J., Zivanovic Y., Forterre P.;
RT   "An integrated analysis of the genome of the hyperthermophilic archaeon
RT   Pyrococcus abyssi.";
RL   Mol. Microbiol. 47:1495-1512(2003).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=GE5 / Orsay;
RX   PubMed=22057919; DOI=10.1007/s00284-011-0035-x;
RA   Gao J., Wang J.;
RT   "Re-annotation of two hyperthermophilic archaea Pyrococcus abyssi GE5 and
RT   Pyrococcus furiosus DSM 3638.";
RL   Curr. Microbiol. 64:118-129(2012).
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   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the LDH2/MDH2 oxidoreductase family.
CC       {ECO:0000305}.
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DR   EMBL; AJ248285; CAB49769.1; -; Genomic_DNA.
DR   EMBL; HE613800; CCE70260.1; -; Genomic_DNA.
DR   PIR; H75131; H75131.
DR   RefSeq; WP_010867978.1; NC_000868.1.
DR   AlphaFoldDB; Q9V0D5; -.
DR   SMR; Q9V0D5; -.
DR   STRING; 272844.PAB1791; -.
DR   EnsemblBacteria; CAB49769; CAB49769; PAB1791.
DR   GeneID; 1496204; -.
DR   KEGG; pab:PAB1791; -.
DR   PATRIC; fig|272844.11.peg.903; -.
DR   eggNOG; arCOG04874; Archaea.
DR   HOGENOM; CLU_040452_2_0_2; -.
DR   OMA; TNTEPAM; -.
DR   OrthoDB; 32318at2157; -.
DR   PhylomeDB; Q9V0D5; -.
DR   Proteomes; UP000000810; Chromosome.
DR   Proteomes; UP000009139; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0030060; F:L-malate dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.1530.10; -; 1.
DR   Gene3D; 3.30.1370.60; -; 1.
DR   InterPro; IPR043144; Mal/L-sulf/L-lact_DH-like_ah.
DR   InterPro; IPR043143; Mal/L-sulf/L-lact_DH-like_NADP.
DR   InterPro; IPR036111; Mal/L-sulfo/L-lacto_DH-like_sf.
DR   InterPro; IPR003767; Malate/L-lactate_DH-like.
DR   PANTHER; PTHR11091; PTHR11091; 1.
DR   Pfam; PF02615; Ldh_2; 1.
DR   SUPFAM; SSF89733; SSF89733; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; NAD; Oxidoreductase; Tricarboxylic acid cycle.
FT   CHAIN           1..362
FT                   /note="Malate dehydrogenase"
FT                   /id="PRO_0000083828"
SQ   SEQUENCE   362 AA;  39907 MW;  1E15C2E9E6BA5012 CRC64;
     MFEKGYVDEN YVRIPKDELF SFVVRVLTKL GTPEEDAKIV ADNLIMADLR GIESHGVQRL
     KRYVDGILSG GINLHPRIKI IREGPSYALL DGDEGFGQVV GYKAMKLAIE KARKTGIGIV
     AVRNSNHYGI AGYYALMAAE EGMIGISMTN SRPLVAPTGG VERILGTNPI ALAAPTKGKP
     FLLDMATSVV PIGKLEVYRR KGEEIPEGWA INSKGEITRS VEEVFNGGSL LPLGGFGELL
     GGHKGYGLSL MVDILSGILS GGTWSKHVKN TNEKNSNVCH FFMAINIEHF TPLEEFKGRM
     SEMINEIKNS RKHPDFERIW IHGEKGFLTM ETRLKLGIPI YKKVLDELNE IARRVGVKGL
     EV