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MDH_METEA
ID   MDH_METEA               Reviewed;         320 AA.
AC   Q84FY8; C5B049;
DT   16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   22-SEP-2009, sequence version 2.
DT   03-AUG-2022, entry version 123.
DE   RecName: Full=Malate dehydrogenase {ECO:0000255|HAMAP-Rule:MF_00487};
DE            EC=1.1.1.37 {ECO:0000255|HAMAP-Rule:MF_00487};
GN   Name=mdh {ECO:0000255|HAMAP-Rule:MF_00487};
GN   OrderedLocusNames=MexAM1_META1p1537;
OS   Methylorubrum extorquens (strain ATCC 14718 / DSM 1338 / JCM 2805 / NCIMB
OS   9133 / AM1) (Methylobacterium extorquens).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Methylobacteriaceae; Methylorubrum.
OX   NCBI_TaxID=272630;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=12730156; DOI=10.1128/jb.185.10.2980-2987.2003;
RA   Chistoserdova L., Chen S.-W., Lapidus A., Lidstrom M.E.;
RT   "Methylotrophy in Methylobacterium extorquens AM1 from a genomic point of
RT   view.";
RL   J. Bacteriol. 185:2980-2987(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 14718 / DSM 1338 / JCM 2805 / NCIMB 9133 / AM1;
RX   PubMed=19440302; DOI=10.1371/journal.pone.0005584;
RA   Vuilleumier S., Chistoserdova L., Lee M.-C., Bringel F., Lajus A., Zhou Y.,
RA   Gourion B., Barbe V., Chang J., Cruveiller S., Dossat C., Gillett W.,
RA   Gruffaz C., Haugen E., Hourcade E., Levy R., Mangenot S., Muller E.,
RA   Nadalig T., Pagni M., Penny C., Peyraud R., Robinson D.G., Roche D.,
RA   Rouy Z., Saenampechek C., Salvignol G., Vallenet D., Wu Z., Marx C.J.,
RA   Vorholt J.A., Olson M.V., Kaul R., Weissenbach J., Medigue C.,
RA   Lidstrom M.E.;
RT   "Methylobacterium genome sequences: a reference blueprint to investigate
RT   microbial metabolism of C1 compounds from natural and industrial sources.";
RL   PLoS ONE 4:E5584-E5584(2009).
CC   -!- FUNCTION: Catalyzes the reversible oxidation of malate to oxaloacetate.
CC       {ECO:0000255|HAMAP-Rule:MF_00487}.
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:0000255|HAMAP-Rule:MF_00487};
CC   -!- SIMILARITY: Belongs to the LDH/MDH superfamily. MDH type 3 family.
CC       {ECO:0000255|HAMAP-Rule:MF_00487}.
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DR   EMBL; AY181040; AAO24626.1; -; Genomic_DNA.
DR   EMBL; CP001510; ACS39399.1; -; Genomic_DNA.
DR   RefSeq; WP_003599890.1; NC_012808.1.
DR   PDB; 5UJK; X-ray; 1.53 A; A=1-320.
DR   PDB; 5ULV; X-ray; 1.66 A; A=1-320.
DR   PDBsum; 5UJK; -.
DR   PDBsum; 5ULV; -.
DR   AlphaFoldDB; Q84FY8; -.
DR   SMR; Q84FY8; -.
DR   STRING; 272630.MexAM1_META1p1537; -.
DR   EnsemblBacteria; ACS39399; ACS39399; MexAM1_META1p1537.
DR   KEGG; mea:Mex_1p1537; -.
DR   eggNOG; COG0039; Bacteria.
DR   HOGENOM; CLU_045401_2_1_5; -.
DR   OMA; MGWTSQA; -.
DR   OrthoDB; 870724at2; -.
DR   BioCyc; MetaCyc:MON-4226; -.
DR   BRENDA; 1.1.1.37; 3296.
DR   Proteomes; UP000009081; Chromosome.
DR   GO; GO:0030060; F:L-malate dehydrogenase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0019752; P:carboxylic acid metabolic process; IEA:InterPro.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-UniRule.
DR   CDD; cd01339; LDH-like_MDH; 1.
DR   Gene3D; 3.90.110.10; -; 1.
DR   HAMAP; MF_00487; Malate_dehydrog_3; 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   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.
DR   TIGRFAMs; TIGR01763; MalateDH_bact; 1.
PE   1: Evidence at protein level;
KW   3D-structure; NAD; Oxidoreductase; Tricarboxylic acid cycle.
FT   CHAIN           1..320
FT                   /note="Malate dehydrogenase"
FT                   /id="PRO_0000113457"
FT   ACT_SITE        176
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00487"
FT   BINDING         10..15
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00487"
FT   BINDING         34
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00487"
FT   BINDING         83
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00487"
FT   BINDING         89
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00487"
FT   BINDING         96
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00487"
FT   BINDING         119..121
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00487"
FT   BINDING         121
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00487"
FT   BINDING         152
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00487"
FT   CONFLICT        109
FT                   /note="E -> K (in Ref. 1; AAO24626)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        120
FT                   /note="T -> A (in Ref. 1; AAO24626)"
FT                   /evidence="ECO:0000305"
FT   STRAND          5..9
FT                   /evidence="ECO:0007829|PDB:5UJK"
FT   HELIX           13..24
FT                   /evidence="ECO:0007829|PDB:5UJK"
FT   STRAND          29..33
FT                   /evidence="ECO:0007829|PDB:5UJK"
FT   STRAND          35..38
FT                   /evidence="ECO:0007829|PDB:5ULV"
FT   HELIX           39..54
FT                   /evidence="ECO:0007829|PDB:5UJK"
FT   STRAND          60..65
FT                   /evidence="ECO:0007829|PDB:5UJK"
FT   HELIX           66..69
FT                   /evidence="ECO:0007829|PDB:5UJK"
FT   STRAND          73..77
FT                   /evidence="ECO:0007829|PDB:5UJK"
FT   HELIX           89..110
FT                   /evidence="ECO:0007829|PDB:5UJK"
FT   STRAND          115..118
FT                   /evidence="ECO:0007829|PDB:5UJK"
FT   HELIX           123..134
FT                   /evidence="ECO:0007829|PDB:5UJK"
FT   HELIX           138..140
FT                   /evidence="ECO:0007829|PDB:5UJK"
FT   STRAND          141..143
FT                   /evidence="ECO:0007829|PDB:5UJK"
FT   HELIX           146..161
FT                   /evidence="ECO:0007829|PDB:5UJK"
FT   HELIX           165..167
FT                   /evidence="ECO:0007829|PDB:5UJK"
FT   STRAND          172..174
FT                   /evidence="ECO:0007829|PDB:5UJK"
FT   HELIX           177..179
FT                   /evidence="ECO:0007829|PDB:5UJK"
FT   STRAND          180..182
FT                   /evidence="ECO:0007829|PDB:5UJK"
FT   HELIX           184..186
FT                   /evidence="ECO:0007829|PDB:5UJK"
FT   HELIX           194..199
FT                   /evidence="ECO:0007829|PDB:5UJK"
FT   HELIX           205..216
FT                   /evidence="ECO:0007829|PDB:5UJK"
FT   HELIX           218..226
FT                   /evidence="ECO:0007829|PDB:5UJK"
FT   STRAND          227..229
FT                   /evidence="ECO:0007829|PDB:5UJK"
FT   HELIX           233..247
FT                   /evidence="ECO:0007829|PDB:5UJK"
FT   STRAND          252..262
FT                   /evidence="ECO:0007829|PDB:5UJK"
FT   HELIX           263..265
FT                   /evidence="ECO:0007829|PDB:5UJK"
FT   STRAND          267..278
FT                   /evidence="ECO:0007829|PDB:5UJK"
FT   STRAND          281..285
FT                   /evidence="ECO:0007829|PDB:5UJK"
FT   HELIX           292..314
FT                   /evidence="ECO:0007829|PDB:5UJK"
SQ   SEQUENCE   320 AA;  33647 MW;  B2CF23AAA0F032EC CRC64;
     MARSKIALIG AGQIGGTLAH LAGLKELGDV VLFDIVDGVP QGKALDIAES APVDGFDAKY
     SGASDYSAIA GADVVIVTAG VPRKPGMSRD DLIGINLKVM EAVGAGIKEH APDAFVICIT
     NPLDAMVWAL QKFSGLPTNK VVGMAGVLDS ARFRHFLAEE FGVSVEDVTA FVLGGHGDDM
     VPLTRYSTVA GVPLTDLVKL GWTTQEKLDA MVERTRKGGG EIVNLLKTGS AFYAPAASAI
     AMAESYLRDK KRVLPCAAYL DGQYGIDGLY VGVPVVIGEN GVERVLEVTF NDDEKAMFEK
     SVNSVKGLIE ACKSVNDKLA
 
 
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