MDH_METTM
ID MDH_METTM Reviewed; 325 AA.
AC D9PVI7;
DT 13-APR-2016, integrated into UniProtKB/Swiss-Prot.
DT 05-OCT-2010, sequence version 1.
DT 03-AUG-2022, entry version 63.
DE RecName: Full=Malate dehydrogenase {ECO:0000303|PubMed:9639601};
DE EC=1.1.1.299 {ECO:0000269|PubMed:9639601};
DE AltName: Full=MdhII {ECO:0000303|PubMed:9639601};
GN Name=mdh {ECO:0000312|EMBL:ADL58235.1};
GN OrderedLocusNames=MTBMA_c06400 {ECO:0000312|EMBL:ADL58235.1};
OS Methanothermobacter marburgensis (strain ATCC BAA-927 / DSM 2133 / JCM
OS 14651 / NBRC 100331 / OCM 82 / Marburg) (Methanobacterium
OS thermoautotrophicum).
OC Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC Methanobacteriales; Methanobacteriaceae; Methanothermobacter.
OX NCBI_TaxID=79929;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 /
RC Marburg;
RX PubMed=20802048; DOI=10.1128/jb.00844-10;
RA Liesegang H., Kaster A.K., Wiezer A., Goenrich M., Wollherr A., Seedorf H.,
RA Gottschalk G., Thauer R.K.;
RT "Complete genome sequence of Methanothermobacter marburgensis, a
RT methanoarchaeon model organism.";
RL J. Bacteriol. 192:5850-5851(2010).
RN [2]
RP PROTEIN SEQUENCE OF 1-20, FUNCTION, CATALYTIC ACTIVITY, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 /
RC Marburg;
RX PubMed=9639601; DOI=10.1007/s002030050612;
RA Thompson H., Tersteegen A., Thauer R.K., Hedderich R.;
RT "Two malate dehydrogenases in Methanobacterium thermoautotrophicum.";
RL Arch. Microbiol. 170:38-42(1998).
CC -!- FUNCTION: Catalyzes the reversible oxidation of malate to oxaloacetate.
CC Can use NAD(+) and NADP(+) with similar specific activity.
CC {ECO:0000269|PubMed:9639601}.
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;
CC EC=1.1.1.299; Evidence={ECO:0000269|PubMed:9639601};
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;
CC EC=1.1.1.299; Evidence={ECO:0000269|PubMed:9639601};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.030 mM for oxaloacetate {ECO:0000269|PubMed:9639601};
CC KM=0.09 mM for NADH {ECO:0000269|PubMed:9639601};
CC KM=0.02 mM for NADPH {ECO:0000269|PubMed:9639601};
CC KM=1 mM for malate {ECO:0000269|PubMed:9639601};
CC KM=0.5 mM for NAD(+) {ECO:0000269|PubMed:9639601};
CC -!- SIMILARITY: Belongs to the LDH/MDH superfamily. {ECO:0000305}.
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DR EMBL; CP001710; ADL58235.1; -; Genomic_DNA.
DR RefSeq; WP_013295459.1; NC_014408.1.
DR AlphaFoldDB; D9PVI7; -.
DR SMR; D9PVI7; -.
DR STRING; 79929.MTBMA_c06400; -.
DR EnsemblBacteria; ADL58235; ADL58235; MTBMA_c06400.
DR GeneID; 9704348; -.
DR KEGG; mmg:MTBMA_c06400; -.
DR PATRIC; fig|79929.8.peg.624; -.
DR HOGENOM; CLU_045401_2_2_2; -.
DR OMA; ASCAEYI; -.
DR OrthoDB; 69007at2157; -.
DR SABIO-RK; D9PVI7; -.
DR Proteomes; UP000000345; Chromosome.
DR GO; GO:0030060; F:L-malate dehydrogenase activity; IEA:RHEA.
DR GO; GO:0046554; F:malate dehydrogenase (NADP+) activity; IEA:RHEA.
DR GO; GO:0019752; P:carboxylic acid metabolic process; IEA:InterPro.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-KW.
DR Gene3D; 3.90.110.10; -; 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; 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.
PE 1: Evidence at protein level;
KW Direct protein sequencing; NAD; NADP; Oxidoreductase;
KW Tricarboxylic acid cycle.
FT CHAIN 1..325
FT /note="Malate dehydrogenase"
FT /id="PRO_0000436035"
FT ACT_SITE 177
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P61889"
FT BINDING 7..13
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q60176"
FT BINDING 84
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P61889"
FT BINDING 90
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P61889"
FT BINDING 97
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q60176"
FT BINDING 120..122
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q60176"
FT BINDING 122
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P61889"
FT BINDING 153
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P61889"
FT CONFLICT 1
FT /note="M -> H (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 19
FT /note="Missing (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 325 AA; 35860 MW; 1D4BB57775D4A236 CRC64;
MKVSIIGSTG RVGRATALCL AEEEAVKTLH LISRRESLEQ NIGEVLDMSD ALAAKGVSVK
LENSADIENV HGSRIVVITA GVPRTADMDR DDLAFQNGVI VAEYARQIAR FAPDSIILVV
TNPVDVMTYV ALKYSGFHPS RVFGLGNHLD SLRLKNYMAR HFNVHVSEVH TRVIGQHGPY
MVPLISSTSI GGIPIEHYAR RDYFSGYRRF DLKKTIEKVI NAGSNIISRK GATEYGPAFA
ISNIVTTILN DERRILTVST LMEGEIDGIR DVCLGVPVKL GKNGIEGVVP VLMDRDERET
FREAASHVRN STMKVMEFLD EELPL
