ID   MDH_PARUW               Reviewed;         330 AA.
AC   Q6MAA3;
DT   19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 108.
DE   RecName: Full=Malate dehydrogenase {ECO:0000255|HAMAP-Rule:MF_01517};
DE            EC=1.1.1.37 {ECO:0000255|HAMAP-Rule:MF_01517};
GN   Name=mdh {ECO:0000255|HAMAP-Rule:MF_01517}; OrderedLocusNames=pc1772;
OS   Protochlamydia amoebophila (strain UWE25).
OC   Bacteria; Chlamydiae; Parachlamydiales; Parachlamydiaceae;
OC   Candidatus Protochlamydia.
OX   NCBI_TaxID=264201;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UWE25;
RX   PubMed=15073324; DOI=10.1126/science.1096330;
RA   Horn M., Collingro A., Schmitz-Esser S., Beier C.L., Purkhold U.,
RA   Fartmann B., Brandt P., Nyakatura G.J., Droege M., Frishman D., Rattei T.,
RA   Mewes H.-W., Wagner M.;
RT   "Illuminating the evolutionary history of chlamydiae.";
RL   Science 304:728-730(2004).
CC   -!- FUNCTION: Catalyzes the reversible oxidation of malate to oxaloacetate.
CC       {ECO:0000255|HAMAP-Rule:MF_01517}.
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:0000255|HAMAP-Rule:MF_01517};
CC   -!- SIMILARITY: Belongs to the LDH/MDH superfamily. MDH type 2 family.
CC       {ECO:0000255|HAMAP-Rule:MF_01517}.
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DR   EMBL; BX908798; CAF24496.1; -; Genomic_DNA.
DR   RefSeq; WP_011176317.1; NC_005861.1.
DR   AlphaFoldDB; Q6MAA3; -.
DR   SMR; Q6MAA3; -.
DR   STRING; 264201.pc1772; -.
DR   EnsemblBacteria; CAF24496; CAF24496; PC_RS08490.
DR   KEGG; pcu:PC_RS08490; -.
DR   eggNOG; COG0039; Bacteria.
DR   HOGENOM; CLU_040727_2_0_0; -.
DR   OMA; TKGMERG; -.
DR   OrthoDB; 870724at2; -.
DR   Proteomes; UP000000529; Chromosome.
DR   GO; GO:0030060; F:L-malate dehydrogenase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006108; P:malate metabolic process; IEA:InterPro.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.90.110.10; -; 1.
DR   HAMAP; MF_01517; Malate_dehydrog_2; 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; IPR001252; Malate_DH_AS.
DR   InterPro; IPR010945; Malate_DH_type2.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   PANTHER; PTHR23382; PTHR23382; 1.
DR   Pfam; PF02866; Ldh_1_C; 1.
DR   Pfam; PF00056; Ldh_1_N; 1.
DR   PIRSF; PIRSF000102; Lac_mal_DH; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   SUPFAM; SSF56327; SSF56327; 1.
DR   TIGRFAMs; TIGR01759; MalateDH-SF1; 1.
DR   PROSITE; PS00068; MDH; 1.
PE   3: Inferred from homology;
KW   NAD; Oxidoreductase; Reference proteome; Tricarboxylic acid cycle.
FT   CHAIN           1..330
FT                   /note="Malate dehydrogenase"
FT                   /id="PRO_0000113384"
FT   ACT_SITE        187
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01517"
FT   BINDING         11..17
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01517"
FT   BINDING         92
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01517"
FT   BINDING         98
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01517"
FT   BINDING         105
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01517"
FT   BINDING         112
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01517"
FT   BINDING         129..131
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01517"
FT   BINDING         131
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01517"
FT   BINDING         162
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01517"
SQ   SEQUENCE   330 AA;  36250 MW;  BC04357B42C47F0B CRC64;
     MSQPIKIAIS GGAGQIAYSL LFRLASGELF GPNQLIELQV LEVPNALSAL EGVKMEIEDC
     AFPLLSSIKI CSDPYQAFED IDYALLIGAK SRGPGMERRD LLQENSKIFV NQGQALNAVA
     KSSAKIFVVG NPCNTNCLIA LNNAPSLKRE NFYAMTRLDQ NRATFFLSQK SQVSTKDVSC
     VTIWGNHSAT QVPDFVNAKI SQKPVETIIP DRQWLEKDFI ESVQKRGAAI IQARGKSSAA
     SAASALLDAM RDRILPTPTG QWFSTALLSD GNPYGIEEGL IFSFPCRVKK NGELSIVSGL
     KWDAFLEEKI KLTEQELKEE REMVSSILKI