ID   MDH_THET7               Reviewed;         315 AA.
AC   A0A0S3QTC6;
DT   25-APR-2018, integrated into UniProtKB/Swiss-Prot.
DT   17-FEB-2016, sequence version 1.
DT   03-AUG-2022, entry version 32.
DE   RecName: Full=Malate dehydrogenase {ECO:0000255|HAMAP-Rule:MF_00487, ECO:0000303|PubMed:29420286};
DE            Short=MDH {ECO:0000303|PubMed:29420286};
DE            EC=1.1.1.37 {ECO:0000255|HAMAP-Rule:MF_00487, ECO:0000269|PubMed:29420286};
GN   Name=mdh {ECO:0000255|HAMAP-Rule:MF_00487};
GN   ORFNames=TST_0784 {ECO:0000312|EMBL:BAT71584.1};
OS   Thermosulfidibacter takaii (strain DSM 17441 / JCM 13301 / NBRC 103674 /
OS   ABI70S6).
OC   Bacteria; Aquificae; Aquificales.
OX   NCBI_TaxID=1298851;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], FUNCTION, CATALYTIC
RP   ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC   STRAIN=DSM 17441 / JCM 13301 / NBRC 103674 / ABI70S6;
RX   PubMed=29420286; DOI=10.1126/science.aao3407;
RA   Nunoura T., Chikaraishi Y., Izaki R., Suwa T., Sato T., Harada T., Mori K.,
RA   Kato Y., Miyazaki M., Shimamura S., Yanagawa K., Shuto A., Ohkouchi N.,
RA   Fujita N., Takaki Y., Atomi H., Takai K.;
RT   "A primordial and reversible TCA cycle in a facultatively
RT   chemolithoautotrophic thermophile.";
RL   Science 359:559-563(2018).
CC   -!- FUNCTION: Catalyzes the reversible oxidation of malate to oxaloacetate.
CC       {ECO:0000255|HAMAP-Rule:MF_00487, ECO:0000269|PubMed:29420286}.
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_00487,
CC         ECO:0000269|PubMed:29420286};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=20.1 uM for oxaloacetate {ECO:0000269|PubMed:29420286};
CC         Vmax=1550 umol/min/mg enzyme toward oxaloacetate
CC         {ECO:0000269|PubMed:29420286};
CC         Note=kcat is 871 sec(-1) with oxaloacetate as substrate.
CC         {ECO:0000269|PubMed:29420286};
CC   -!- SIMILARITY: Belongs to the LDH/MDH superfamily. MDH type 3 family.
CC       {ECO:0000255|HAMAP-Rule:MF_00487}.
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DR   EMBL; AP013035; BAT71584.1; -; Genomic_DNA.
DR   RefSeq; WP_068549586.1; NZ_AP013035.1.
DR   AlphaFoldDB; A0A0S3QTC6; -.
DR   SMR; A0A0S3QTC6; -.
DR   STRING; 1298851.TST_0784; -.
DR   EnsemblBacteria; BAT71584; BAT71584; TST_0784.
DR   KEGG; ttk:TST_0784; -.
DR   PATRIC; fig|1298851.3.peg.819; -.
DR   OMA; ASCAEYI; -.
DR   OrthoDB; 870724at2; -.
DR   Proteomes; UP000063234; Chromosome.
DR   GO; GO:0030060; F:L-malate dehydrogenase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0019752; P:carboxylic acid metabolic process; IEA:InterPro.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-UniRule.
DR   CDD; cd01339; LDH-like_MDH; 1.
DR   Gene3D; 3.90.110.10; -; 1.
DR   HAMAP; MF_00487; Malate_dehydrog_3; 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   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; SSF51735; SSF51735; 1.
DR   SUPFAM; SSF56327; SSF56327; 1.
DR   TIGRFAMs; TIGR01763; MalateDH_bact; 1.
PE   1: Evidence at protein level;
KW   NAD; Oxidoreductase; Reference proteome; Tricarboxylic acid cycle.
FT   CHAIN           1..315
FT                   /note="Malate dehydrogenase"
FT                   /id="PRO_0000443957"
FT   ACT_SITE        177
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00487"
FT   BINDING         11..16
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00487"
FT   BINDING         35
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00487"
FT   BINDING         84
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00487"
FT   BINDING         90
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00487"
FT   BINDING         97
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00487"
FT   BINDING         120..122
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00487"
FT   BINDING         122
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00487"
FT   BINDING         153
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00487"
SQ   SEQUENCE   315 AA;  33717 MW;  E3522A8D01A5E59C CRC64;
     MGKRAKITVV GAGHVGEHVA MFCAIKELGD VVLIDIVEDM PQGKALDMFE ATPLEGWDSR
     IVGTNDYADT ADSDIVVITA GSPRKPGMSR DDLLEINAKI IKAVTEQVAK YSPNAVIIVV
     TNPLDAMTQL AWNVSGFPKN RVLGQAGNLD SARFRAFIAM ELGVSVKEIS AMVLGGHGDD
     MVPLPRFTTV SGIPITELIP PDRIEALVQR TRVGGGEIVK LLKTGSAYYA PALATVEMVE
     AILKDQKRIQ PCAALCEGEY GINGVYCGVP CLLGANGVEK IIELKLTDDE LKALQASAGR
     VKGLIDKLTE WGYIK