ID   MDH_METFV               Reviewed;         339 AA.
AC   P16142; E3GY09;
DT   01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1990, sequence version 2.
DT   27-MAR-2024, entry version 110.
DE   RecName: Full=Malate/(S)-sulfolactate dehydrogenase;
DE            EC=1.1.1.310;
DE            EC=1.1.1.37;
DE            EC=1.1.1.82;
GN   Name=mdh; OrderedLocusNames=Mfer_0389;
OS   Methanothermus fervidus (strain ATCC 43054 / DSM 2088 / JCM 10308 / V24 S).
OC   Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC   Methanobacteriales; Methanothermaceae; Methanothermus.
OX   NCBI_TaxID=523846;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-24.
RC   STRAIN=ATCC 43054 / DSM 2088 / JCM 10308 / V24 S;
RX   PubMed=2110059; DOI=10.1111/j.1432-1033.1990.tb15443.x;
RA   Honka E., Fabry S., Niermann T., Palm P., Hensel R.;
RT   "Properties and primary structure of the L-malate dehydrogenase from the
RT   extremely thermophilic archaebacterium Methanothermus fervidus.";
RL   Eur. J. Biochem. 188:623-632(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43054 / DSM 2088 / JCM 10308 / V24 S;
RX   PubMed=21304736; DOI=10.4056/sigs.1283367;
RA   Anderson I., Djao O.D., Misra M., Chertkov O., Nolan M., Lucas S.,
RA   Lapidus A., Del Rio T.G., Tice H., Cheng J.F., Tapia R., Han C.,
RA   Goodwin L., Pitluck S., Liolios K., Ivanova N., Mavromatis K.,
RA   Mikhailova N., Pati A., Brambilla E., Chen A., Palaniappan K., Land M.,
RA   Hauser L., Chang Y.J., Jeffries C.D., Sikorski J., Spring S., Rohde M.,
RA   Eichinger K., Huber H., Wirth R., Goker M., Detter J.C., Woyke T.,
RA   Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Klenk H.P.,
RA   Kyrpides N.C.;
RT   "Complete genome sequence of Methanothermus fervidus type strain (V24S).";
RL   Stand. Genomic Sci. 3:315-324(2010).
RN   [3]
RP   FUNCTION.
RX   PubMed=10850983; DOI=10.1128/jb.182.13.3688-3692.2000;
RA   Graupner M., Xu H., White R.H.;
RT   "Identification of an archaeal 2-hydroxy acid dehydrogenase catalyzing
RT   reactions involved in coenzyme biosynthesis in methanoarchaea.";
RL   J. Bacteriol. 182:3688-3692(2000).
CC   -!- FUNCTION: Acts on oxaloacetate, sulfopyruvate but not on pyruvate. Has
CC       a higher selectivity for the coenzyme NADH than for NADPH.
CC       {ECO:0000269|PubMed:10850983}.
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   -!- CATALYTIC ACTIVITY:
CC       Reaction=(S)-malate + NADP(+) = H(+) + NADPH + oxaloacetate;
CC         Xref=Rhea:RHEA:10824, ChEBI:CHEBI:15378, ChEBI:CHEBI:15589,
CC         ChEBI:CHEBI:16452, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.82;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2S)-3-sulfolactate + NAD(+) = 3-sulfopyruvate + H(+) + NADH;
CC         Xref=Rhea:RHEA:28194, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540,
CC         ChEBI:CHEBI:57940, ChEBI:CHEBI:57945, ChEBI:CHEBI:61289;
CC         EC=1.1.1.310;
CC   -!- SUBUNIT: Homodimer.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the LDH2/MDH2 oxidoreductase family.
CC       {ECO:0000305}.
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DR   EMBL; X51714; CAA36010.1; -; Genomic_DNA.
DR   EMBL; X51840; CAA36133.1; -; Genomic_DNA.
DR   EMBL; CP002278; ADP77191.1; -; Genomic_DNA.
DR   PIR; S08981; S08981.
DR   RefSeq; WP_013413469.1; NC_014658.1.
DR   AlphaFoldDB; P16142; -.
DR   SMR; P16142; -.
DR   STRING; 523846.Mfer_0389; -.
DR   GeneID; 9962106; -.
DR   KEGG; mfv:Mfer_0389; -.
DR   HOGENOM; CLU_040452_3_1_2; -.
DR   OrthoDB; 40552at2157; -.
DR   BRENDA; 1.1.1.337; 3286.
DR   SABIO-RK; P16142; -.
DR   Proteomes; UP000002315; 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:0046554; F:malate dehydrogenase (NADP+) activity; IEA:UniProtKB-EC.
DR   GO; GO:0102155; F:S-sulfolactate dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.1530.10; -; 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   NCBIfam; NF040650; sulfolac_dhydr; 1.
DR   PANTHER; PTHR11091:SF0; HYDROXYCARBOXYLATE DEHYDROGENASE B-RELATED; 1.
DR   PANTHER; PTHR11091; OXIDOREDUCTASE-RELATED; 1.
DR   Pfam; PF02615; Ldh_2; 1.
DR   SUPFAM; SSF89733; L-sulfolactate dehydrogenase-like; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Direct protein sequencing; NAD; NADP; Oxidoreductase;
KW   Reference proteome; Tricarboxylic acid cycle.
FT   CHAIN           1..339
FT                   /note="Malate/(S)-sulfolactate dehydrogenase"
FT                   /id="PRO_0000083827"
SQ   SEQUENCE   339 AA;  36762 MW;  2319D822DB275835 CRC64;
     MIISPEEERS LIIKILNALG VSEEHAKITA DVIVDADLKG FTSHGIGRFP QYVEGIKLGT
     IKTSGNIEIE KETDSVALIN GNHLLGQVVA YKGMKLAIEK AKNTGVGIVG IHDSNHFGIA
     GYYSDMAMKN DMIGITMTNT EPAVAPLGGK IPVLGTNPIA ISIPSNEYYV AVDMSTAAVA
     RGKLLEAARK NEKIPEGIAV DKNGNPTTDP NEALNGSILP FGGHKGYALC FMIEILAGPL
     VKAEFGSKVK GTVDPSQMCT KGDLLIAIDP SKFYDIEEFK RNVDEFVKEI KSTGKDVLIP
     GDRERMNIKK REKEGIELDK KLVEKLKEIA DELNIELTW
//