MDH_RALSO
ID MDH_RALSO Reviewed; 329 AA.
AC Q8XXW5;
DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 116.
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=RSc1998;
GN ORFNames=RS03566;
OS Ralstonia solanacearum (strain GMI1000) (Pseudomonas solanacearum).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Ralstonia.
OX NCBI_TaxID=267608;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GMI1000;
RX PubMed=11823852; DOI=10.1038/415497a;
RA Salanoubat M., Genin S., Artiguenave F., Gouzy J., Mangenot S., Arlat M.,
RA Billault A., Brottier P., Camus J.-C., Cattolico L., Chandler M.,
RA Choisne N., Claudel-Renard C., Cunnac S., Demange N., Gaspin C., Lavie M.,
RA Moisan A., Robert C., Saurin W., Schiex T., Siguier P., Thebault P.,
RA Whalen M., Wincker P., Levy M., Weissenbach J., Boucher C.A.;
RT "Genome sequence of the plant pathogen Ralstonia solanacearum.";
RL Nature 415:497-502(2002).
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; AL646052; CAD15700.1; -; Genomic_DNA.
DR RefSeq; WP_011001933.1; NC_003295.1.
DR AlphaFoldDB; Q8XXW5; -.
DR SMR; Q8XXW5; -.
DR STRING; 267608.RSc1998; -.
DR EnsemblBacteria; CAD15700; CAD15700; RSc1998.
DR GeneID; 60501514; -.
DR KEGG; rso:RSc1998; -.
DR eggNOG; COG0039; Bacteria.
DR HOGENOM; CLU_040727_2_0_4; -.
DR OMA; TKGMERG; -.
DR Proteomes; UP000001436; Chromosome.
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; Reference proteome; Tricarboxylic acid cycle.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..329
FT /note="Malate dehydrogenase"
FT /id="PRO_0000113391"
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 329 AA; 35423 MW; 24847844D1F18695 CRC64;
MAKAPMRVAV TGAAGQIGYA LLFRIAAGEM LGKDQPVILQ LLEIPDEKAQ KALKGVMMEI
EDCAFPLLAG MEAHADPMTA FKDVDVALLV GARPRGPGME RKDLLSANAQ IFTAQGKALN
AVASRNVKVL VVGNPANTNA YIAMKSAPDL PRENFTAMLR LDHNRALSQI AAKTGKPVSS
IEKLFVWGNH SPTMYADYRY ATIDGQSVKD MINDPVWNND VFLPTVGKRG AAIIEARGLS
SAASAANAAI DHVRDWVLGS NGKIVTMGIP SNGDYEIPQD VMFGFPVTTA NGKYEVVKGF
EVDAYSREKI NITLKELEEE RAGVQHLLG
