ID MDH_NITMS Reviewed; 304 AA.
AC A9A450;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 1.
DT 13-SEP-2023, entry version 80.
DE RecName: Full=Malate dehydrogenase {ECO:0000250|UniProtKB:O08349};
DE EC=1.1.1.37 {ECO:0000250|UniProtKB:O08349};
GN Name=mdh; OrderedLocusNames=Nmar_0338;
OS Nitrosopumilus maritimus (strain SCM1).
OC Archaea; Nitrososphaerota; Nitrososphaeria; Nitrosopumilales;
OC Nitrosopumilaceae; Nitrosopumilus.
OX NCBI_TaxID=436308;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SCM1;
RX PubMed=20421470; DOI=10.1073/pnas.0913533107;
RA Walker C.B., de la Torre J.R., Klotz M.G., Urakawa H., Pinel N., Arp D.J.,
RA Brochier-Armanet C., Chain P.S., Chan P.P., Gollabgir A., Hemp J.,
RA Hugler M., Karr E.A., Konneke M., Shin M., Lawton T.J., Lowe T.,
RA Martens-Habbena W., Sayavedra-Soto L.A., Lang D., Sievert S.M.,
RA Rosenzweig A.C., Manning G., Stahl D.A.;
RT "Nitrosopumilus maritimus genome reveals unique mechanisms for
RT nitrification and autotrophy in globally distributed marine crenarchaea.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:8818-8823(2010).
CC -!- FUNCTION: Catalyzes the reversible oxidation of malate to oxaloacetate.
CC {ECO:0000250|UniProtKB:O08349}.
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:0000250|UniProtKB:O08349};
CC -!- SIMILARITY: Belongs to the LDH/MDH superfamily. {ECO:0000305}.
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DR EMBL; CP000866; ABX12234.1; -; Genomic_DNA.
DR AlphaFoldDB; A9A450; -.
DR SMR; A9A450; -.
DR STRING; 436308.Nmar_0338; -.
DR EnsemblBacteria; ABX12234; ABX12234; Nmar_0338.
DR KEGG; nmr:Nmar_0338; -.
DR eggNOG; arCOG00246; Archaea.
DR HOGENOM; CLU_045401_2_1_2; -.
DR InParanoid; A9A450; -.
DR OMA; ASCAEYI; -.
DR OrthoDB; 2596at2157; -.
DR PhylomeDB; A9A450; -.
DR Proteomes; UP000000792; Chromosome.
DR GO; GO:0004459; F:L-lactate dehydrogenase activity; IBA:GO_Central.
DR GO; GO:0030060; F:L-malate dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0006089; P:lactate metabolic process; IBA:GO_Central.
DR GO; GO:0006090; P:pyruvate metabolic process; IBA:GO_Central.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-KW.
DR CDD; cd01339; LDH-like_MDH; 1.
DR Gene3D; 3.90.110.10; Lactate dehydrogenase/glycoside hydrolase, family 4, C-terminal; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 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 PANTHER; PTHR43128; L-2-HYDROXYCARBOXYLATE DEHYDROGENASE (NAD(P)(+)); 1.
DR PANTHER; PTHR43128:SF16; L-LACTATE DEHYDROGENASE; 1.
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; SSF56327; LDH C-terminal domain-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE 3: Inferred from homology;
KW NAD; Oxidoreductase; Reference proteome; Tricarboxylic acid cycle.
FT CHAIN 1..304
FT /note="Malate dehydrogenase"
FT /id="PRO_1000126142"
FT ACT_SITE 173
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P61889"
FT BINDING 6..11
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:O08349"
FT BINDING 31
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:O08349"
FT BINDING 80
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P61889"
FT BINDING 86
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P61889"
FT BINDING 93
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:O08349"
FT BINDING 116..118
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:O08349"
FT BINDING 118
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P61889"
FT BINDING 149
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P61889"
SQ SEQUENCE 304 AA; 32783 MW; CCD4FA954CD3A944 CRC64;
MITIIGSGKV GGDAALFSAL KRLDDQILLL DVAEGLPQGE AMDINHMLSE QGIDVEVKGS
NNFEDMKGSN IVVVVAGSGR KPGMTRMDLL KINASIVKSV VENVKKYADD SMIIPVTNPL
DPMAYITYKV SGFDRSRVFG MGGMLDLSRF RQFIHEATGH SRDSIRALVI GEHGENMLPL
PRFSSVSGIP LPSLLPKEKL EELVQNTKQV AAKVIELKGA TVHAPGNAIS AIVEAVVRDR
KQVIPVATYL DGEYDHSDVT IGVPAVIGKN GVEKIIELDL NDEEKQVFNK AVENVKGALS
GVEI
//