MDH_ARCFU
ID MDH_ARCFU Reviewed; 294 AA.
AC O08349;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Malate dehydrogenase {ECO:0000303|PubMed:9211715};
DE EC=1.1.1.37 {ECO:0000269|PubMed:19555779};
GN Name=mdh; OrderedLocusNames=AF_0855;
OS Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC
OS 100126 / VC-16).
OC Archaea; Euryarchaeota; Archaeoglobi; Archaeoglobales; Archaeoglobaceae;
OC Archaeoglobus.
OX NCBI_TaxID=224325;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CHARACTERIZATION.
RC STRAIN=ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16;
RX PubMed=9211715; DOI=10.1007/s002030050470;
RA Langelandsvik A.S., Steen I.H., Birkeland N.K., Lien T.;
RT "Properties and primary structure of a thermostable L-malate dehydrogenase
RT from Archaeoglobus fulgidus.";
RL Arch. Microbiol. 168:59-67(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16;
RX PubMed=9389475; DOI=10.1038/37052;
RA Klenk H.-P., Clayton R.A., Tomb J.-F., White O., Nelson K.E., Ketchum K.A.,
RA Dodson R.J., Gwinn M.L., Hickey E.K., Peterson J.D., Richardson D.L.,
RA Kerlavage A.R., Graham D.E., Kyrpides N.C., Fleischmann R.D.,
RA Quackenbush J., Lee N.H., Sutton G.G., Gill S.R., Kirkness E.F.,
RA Dougherty B.A., McKenney K., Adams M.D., Loftus B.J., Peterson S.N.,
RA Reich C.I., McNeil L.K., Badger J.H., Glodek A., Zhou L., Overbeek R.,
RA Gocayne J.D., Weidman J.F., McDonald L.A., Utterback T.R., Cotton M.D.,
RA Spriggs T., Artiach P., Kaine B.P., Sykes S.M., Sadow P.W., D'Andrea K.P.,
RA Bowman C., Fujii C., Garland S.A., Mason T.M., Olsen G.J., Fraser C.M.,
RA Smith H.O., Woese C.R., Venter J.C.;
RT "The complete genome sequence of the hyperthermophilic, sulphate-reducing
RT archaeon Archaeoglobus fulgidus.";
RL Nature 390:364-370(1997).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=19555779; DOI=10.1016/j.bbapap.2009.06.014;
RA Kawakami R., Sakuraba H., Goda S., Tsuge H., Ohshima T.;
RT "Refolding, characterization and crystal structure of (S)-malate
RT dehydrogenase from the hyperthermophilic archaeon Aeropyrum pernix.";
RL Biochim. Biophys. Acta 1794:1496-1504(2009).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.79 ANGSTROMS) IN COMPLEX WITH NAD, AND SUBUNIT.
RX PubMed=14659762; DOI=10.1016/j.jmb.2003.10.054;
RA Irimia A., Vellieux F.M.D., Madern D., Zaccai G., Karshikoff A.,
RA Tibbelin G., Ladenstein R., Lien T., Birkeland N.-K.;
RT "The 2.9A resolution crystal structure of malate dehydrogenase from
RT Archaeoglobus fulgidus: mechanisms of oligomerisation and thermal
RT stabilisation.";
RL J. Mol. Biol. 335:343-356(2004).
CC -!- FUNCTION: Catalyzes the reversible oxidation of malate to oxaloacetate.
CC Can also oxidize tartrate. {ECO:0000269|PubMed:19555779}.
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:0000269|PubMed:19555779};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.074 mM for S-malate {ECO:0000269|PubMed:19555779};
CC KM=0.63 mM for (2S,3S)-tartrate {ECO:0000269|PubMed:19555779};
CC KM=0.40 mM for (2S,3R)-tartrate {ECO:0000269|PubMed:19555779};
CC Note=kcat is 5.7 sec(-1) for NAD-dependent malate oxidation.
CC {ECO:0000269|PubMed:19555779};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:14659762}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
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; Z85985; CAB06654.1; -; Genomic_DNA.
DR EMBL; AE000782; AAB90384.1; -; Genomic_DNA.
DR PIR; G69356; G69356.
DR RefSeq; WP_010878358.1; NC_000917.1.
DR PDB; 2X0I; X-ray; 2.90 A; A=1-294.
DR PDB; 2X0J; X-ray; 2.79 A; A=1-294.
DR PDBsum; 2X0I; -.
DR PDBsum; 2X0J; -.
DR AlphaFoldDB; O08349; -.
DR SMR; O08349; -.
DR STRING; 224325.AF_0855; -.
DR EnsemblBacteria; AAB90384; AAB90384; AF_0855.
DR GeneID; 24794453; -.
DR KEGG; afu:AF_0855; -.
DR eggNOG; arCOG00246; Archaea.
DR HOGENOM; CLU_045401_2_1_2; -.
DR OMA; ASCAEYI; -.
DR OrthoDB; 69007at2157; -.
DR PhylomeDB; O08349; -.
DR BRENDA; 1.1.1.37; 414.
DR BRENDA; 1.1.1.375; 414.
DR EvolutionaryTrace; O08349; -.
DR Proteomes; UP000002199; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004459; F:L-lactate dehydrogenase activity; IEA:InterPro.
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 CDD; cd01339; LDH-like_MDH; 1.
DR Gene3D; 3.90.110.10; -; 1.
DR InterPro; IPR001557; L-lactate/malate_DH.
DR InterPro; IPR018177; L-lactate_DH_AS.
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 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 3D-structure; Cytoplasm; NAD; Oxidoreductase; Reference proteome;
KW Tricarboxylic acid cycle.
FT CHAIN 1..294
FT /note="Malate dehydrogenase"
FT /id="PRO_0000113480"
FT ACT_SITE 172
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P61889"
FT BINDING 7..12
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:14659762"
FT BINDING 32
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:14659762"
FT BINDING 81
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P61889"
FT BINDING 87
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P61889"
FT BINDING 94
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:14659762"
FT BINDING 117..119
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:14659762"
FT BINDING 119
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P61889"
FT BINDING 150
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P61889"
FT STRAND 2..6
FT /evidence="ECO:0007829|PDB:2X0J"
FT HELIX 10..22
FT /evidence="ECO:0007829|PDB:2X0J"
FT STRAND 26..31
FT /evidence="ECO:0007829|PDB:2X0J"
FT HELIX 35..49
FT /evidence="ECO:0007829|PDB:2X0J"
FT HELIX 50..52
FT /evidence="ECO:0007829|PDB:2X0J"
FT STRAND 57..62
FT /evidence="ECO:0007829|PDB:2X0J"
FT HELIX 64..67
FT /evidence="ECO:0007829|PDB:2X0J"
FT STRAND 71..75
FT /evidence="ECO:0007829|PDB:2X0J"
FT STRAND 83..85
FT /evidence="ECO:0007829|PDB:2X0J"
FT HELIX 87..106
FT /evidence="ECO:0007829|PDB:2X0J"
FT STRAND 113..116
FT /evidence="ECO:0007829|PDB:2X0J"
FT STRAND 118..120
FT /evidence="ECO:0007829|PDB:2X0J"
FT HELIX 121..131
FT /evidence="ECO:0007829|PDB:2X0J"
FT STRAND 138..141
FT /evidence="ECO:0007829|PDB:2X0J"
FT HELIX 144..157
FT /evidence="ECO:0007829|PDB:2X0J"
FT STRAND 161..163
FT /evidence="ECO:0007829|PDB:2X0J"
FT STRAND 168..170
FT /evidence="ECO:0007829|PDB:2X0J"
FT HELIX 180..182
FT /evidence="ECO:0007829|PDB:2X0J"
FT STRAND 185..187
FT /evidence="ECO:0007829|PDB:2X0J"
FT HELIX 191..199
FT /evidence="ECO:0007829|PDB:2X0J"
FT HELIX 201..209
FT /evidence="ECO:0007829|PDB:2X0J"
FT HELIX 214..228
FT /evidence="ECO:0007829|PDB:2X0J"
FT STRAND 234..243
FT /evidence="ECO:0007829|PDB:2X0J"
FT HELIX 244..246
FT /evidence="ECO:0007829|PDB:2X0J"
FT STRAND 248..259
FT /evidence="ECO:0007829|PDB:2X0J"
FT STRAND 262..265
FT /evidence="ECO:0007829|PDB:2X0J"
FT HELIX 272..290
FT /evidence="ECO:0007829|PDB:2X0J"
FT TURN 291..293
FT /evidence="ECO:0007829|PDB:2X0J"
SQ SEQUENCE 294 AA; 31874 MW; 90389DBC189B944F CRC64;
MKLGFVGAGR VGSTSAFTCL LNLDVDEIAL VDIAEDLAVG EAMDLAHAAA GIDKYPKIVG
GADYSLLKGS EIIVVTAGLA RKPGMTRLDL AHKNAGIIKD IAKKIVENAP ESKILVVTNP
MDVMTYIMWK ESGKPRNEVF GMGNQLDSQR LKERLYNAGA RNIRRAWIIG EHGDSMFVAK
SLADFDGEVD WEAVENDVRF VAAEVIKRKG ATIFGPAVAI YRMVKAVVED TGEIIPTSMI
LQGEYGIENV AVGVPAKLGK NGAEVADIKL SDEEIEKLRN SAKILRERLE ELGY
