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Database: UniProt
Entry: MDH_NITMS
LinkDB: MDH_NITMS
Original site: MDH_NITMS 
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
//
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