ID   MDH_HALSA               Reviewed;         304 AA.
AC   Q9HMV8;
DT   16-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 136.
DE   RecName: Full=Malate dehydrogenase {ECO:0000250|UniProtKB:O08349};
DE            EC=1.1.1.37 {ECO:0000250|UniProtKB:O08349};
GN   Name=mdh; Synonyms=mdhA; OrderedLocusNames=VNG_2367G;
OS   Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1)
OS   (Halobacterium halobium).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC   Halobacteriaceae; Halobacterium.
OX   NCBI_TaxID=64091;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700922 / JCM 11081 / NRC-1;
RX   PubMed=11016950; DOI=10.1073/pnas.190337797;
RA   Ng W.V., Kennedy S.P., Mahairas G.G., Berquist B., Pan M., Shukla H.D.,
RA   Lasky S.R., Baliga N.S., Thorsson V., Sbrogna J., Swartzell S., Weir D.,
RA   Hall J., Dahl T.A., Welti R., Goo Y.A., Leithauser B., Keller K., Cruz R.,
RA   Danson M.J., Hough D.W., Maddocks D.G., Jablonski P.E., Krebs M.P.,
RA   Angevine C.M., Dale H., Isenbarger T.A., Peck R.F., Pohlschroder M.,
RA   Spudich J.L., Jung K.-H., Alam M., Freitas T., Hou S., Daniels C.J.,
RA   Dennis P.P., Omer A.D., Ebhardt H., Lowe T.M., Liang P., Riley M., Hood L.,
RA   DasSarma S.;
RT   "Genome sequence of Halobacterium species NRC-1.";
RL   Proc. Natl. Acad. Sci. U.S.A. 97:12176-12181(2000).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AE004437; AAG20463.1; -; Genomic_DNA.
DR   PIR; C84387; C84387.
DR   RefSeq; WP_010903765.1; NC_002607.1.
DR   AlphaFoldDB; Q9HMV8; -.
DR   SMR; Q9HMV8; -.
DR   STRING; 64091.VNG_2367G; -.
DR   PaxDb; Q9HMV8; -.
DR   EnsemblBacteria; AAG20463; AAG20463; VNG_2367G.
DR   GeneID; 5953357; -.
DR   KEGG; hal:VNG_2367G; -.
DR   PATRIC; fig|64091.14.peg.1831; -.
DR   HOGENOM; CLU_045401_1_1_2; -.
DR   InParanoid; Q9HMV8; -.
DR   OMA; CYIIVLT; -.
DR   OrthoDB; 69007at2157; -.
DR   PhylomeDB; Q9HMV8; -.
DR   Proteomes; UP000000554; Chromosome.
DR   GO; GO:0030060; F:L-malate dehydrogenase activity; IEA:UniProtKB-EC.
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   3: Inferred from homology;
KW   NAD; Oxidoreductase; Reference proteome; Tricarboxylic acid cycle.
FT   CHAIN           1..304
FT                   /note="Malate dehydrogenase"
FT                   /id="PRO_0000113482"
FT   ACT_SITE        176
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:P61889"
FT   BINDING         8..14
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:O08349"
FT   BINDING         34
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:O08349"
FT   BINDING         83
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P61889"
FT   BINDING         89
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P61889"
FT   BINDING         96
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:O08349"
FT   BINDING         119..121
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:O08349"
FT   BINDING         121
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P61889"
FT   BINDING         152
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P61889"
SQ   SEQUENCE   304 AA;  32252 MW;  C357C0A9520CC649 CRC64;
     MTKVSIVGAA GTVGAAAGYN LALRDVVDEL VFVDIPDKEE ETIGQAADAN HGVAYDANTD
     VVQGDYADTA GSDVVVITAG IPRQPGQSRT DLAGDNAPIM EDIGSSLAEH NDDFVTVTTS
     NPVDLLNRHL YESGDRDRHS VVGFGGRLDS ARFRYVLGQR FDVPVQNVDA TILGEHGDAQ
     VPVFSKVRVN GTDPAFSADE REEILADLQE SAMNVIEKKG ATQWGPATGV AHMVEAILND
     TGEVLPGSMV LDGEYGLDDV GLGVPVKLGS DGVEEVVEWE LTADERDLLD EAAEKLSAQY
     DEIA