MDH_RALPJ
ID MDH_RALPJ Reviewed; 328 AA.
AC B2U705;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-2008, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=Malate dehydrogenase {ECO:0000255|HAMAP-Rule:MF_01517};
DE EC=1.1.1.37 {ECO:0000255|HAMAP-Rule:MF_01517};
GN Name=mdh {ECO:0000255|HAMAP-Rule:MF_01517}; OrderedLocusNames=Rpic_2153;
OS Ralstonia pickettii (strain 12J).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Ralstonia.
OX NCBI_TaxID=402626;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=12J;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Meincke L., Brettin T., Detter J.C.,
RA Han C., Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L.,
RA Kyrpides N., Mikhailova N., Marsh T., Richardson P.;
RT "Complete sequence of chromosome 1 of Ralstonia pickettii 12J.";
RL Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the reversible oxidation of malate to oxaloacetate.
CC {ECO:0000255|HAMAP-Rule:MF_01517}.
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_01517};
CC -!- SIMILARITY: Belongs to the LDH/MDH superfamily. MDH type 2 family.
CC {ECO:0000255|HAMAP-Rule:MF_01517}.
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DR EMBL; CP001068; ACD27287.1; -; Genomic_DNA.
DR RefSeq; WP_012436029.1; NC_010682.1.
DR AlphaFoldDB; B2U705; -.
DR SMR; B2U705; -.
DR STRING; 402626.Rpic_2153; -.
DR PRIDE; B2U705; -.
DR EnsemblBacteria; ACD27287; ACD27287; Rpic_2153.
DR KEGG; rpi:Rpic_2153; -.
DR PATRIC; fig|402626.5.peg.3301; -.
DR eggNOG; COG0039; Bacteria.
DR HOGENOM; CLU_040727_2_0_4; -.
DR OMA; TKGMERG; -.
DR OrthoDB; 870724at2; -.
DR GO; GO:0030060; F:L-malate dehydrogenase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006108; P:malate metabolic process; IEA:InterPro.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-UniRule.
DR Gene3D; 3.90.110.10; -; 1.
DR HAMAP; MF_01517; Malate_dehydrog_2; 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; IPR010945; Malate_DH_type2.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR23382; PTHR23382; 1.
DR Pfam; PF02866; Ldh_1_C; 1.
DR Pfam; PF00056; Ldh_1_N; 1.
DR PIRSF; PIRSF000102; Lac_mal_DH; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR SUPFAM; SSF56327; SSF56327; 1.
DR TIGRFAMs; TIGR01759; MalateDH-SF1; 1.
PE 3: Inferred from homology;
KW NAD; Oxidoreductase; Tricarboxylic acid cycle.
FT CHAIN 1..328
FT /note="Malate dehydrogenase"
FT /id="PRO_1000191628"
FT ACT_SITE 190
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01517"
FT BINDING 12..18
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01517"
FT BINDING 95
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01517"
FT BINDING 101
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01517"
FT BINDING 108
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01517"
FT BINDING 115
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01517"
FT BINDING 132..134
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01517"
FT BINDING 134
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01517"
FT BINDING 165
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01517"
SQ SEQUENCE 328 AA; 35247 MW; B37874A02F8F76B4 CRC64;
MAKAPMRVAV TGAAGQIGYA LLFRIAAGEM LGKDQPVILQ LLEIPDEKAQ KALKGVMMEI
EDCAFPLLAG MQAHSDPMTA FKDVDVALLV GARPRGPGME RADLLSANAQ IFTAQGRALN
AVASRNVKVL VVGNPANTNA YIAMKSAPDL PRENFTAMLR LDHNRALSQI AAKTGKPVSS
IEKLFVWGNH SPTMYADYRY ATIDGKSVKD MINDPVWNND VFLPTVGKRG AAIIEARGLS
SAASAANAAI DHVRDWVLGT NGKIVTMGIP SNGEYGIPKD VMFGFPVTTE NGKYKIVEGL
EIDEYSQGKI KITLDELEGE RAGVQHLL
