MDH_WOLPP
ID MDH_WOLPP Reviewed; 314 AA.
AC B3CM44;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 22-JUL-2008, sequence version 1.
DT 03-AUG-2022, entry version 78.
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}; OrderedLocusNames=WP0855;
OS Wolbachia pipientis subsp. Culex pipiens (strain wPip).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC Anaplasmataceae; Wolbachieae; Wolbachia; unclassified Wolbachia.
OX NCBI_TaxID=570417;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=wPip;
RX PubMed=18550617; DOI=10.1093/molbev/msn133;
RA Klasson L., Walker T., Sebaihia M., Sanders M.J., Quail M.A., Lord A.,
RA Sanders S., Earl J., O'Neill S.L., Thomson N., Sinkins S.P., Parkhill J.;
RT "Genome evolution of Wolbachia strain wPip from the Culex pipiens group.";
RL Mol. Biol. Evol. 25:1877-1887(2008).
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; AM999887; CAQ54963.1; -; Genomic_DNA.
DR RefSeq; WP_007302259.1; NC_010981.1.
DR AlphaFoldDB; B3CM44; -.
DR SMR; B3CM44; -.
DR STRING; 570417.WP0855; -.
DR EnsemblBacteria; CAQ54963; CAQ54963; WP0855.
DR KEGG; wpi:WP0855; -.
DR eggNOG; COG0039; Bacteria.
DR HOGENOM; CLU_045401_2_1_5; -.
DR OMA; MGWTSQA; -.
DR OrthoDB; 870724at2; -.
DR Proteomes; UP000008814; 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 3: Inferred from homology;
KW NAD; Oxidoreductase; Tricarboxylic acid cycle.
FT CHAIN 1..314
FT /note="Malate dehydrogenase"
FT /id="PRO_1000126150"
FT ACT_SITE 178
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00487"
FT BINDING 12..17
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00487"
FT BINDING 36
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00487"
FT BINDING 85
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00487"
FT BINDING 91
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00487"
FT BINDING 98
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00487"
FT BINDING 121..123
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00487"
FT BINDING 123
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00487"
FT BINDING 154
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00487"
SQ SEQUENCE 314 AA; 33827 MW; 41D464E4A3BC5E90 CRC64;
MTAQRKKISL IGAGNIGGTL AHMIALRELG DVILLDVSDG IPQGKALDIT ESSPIDRSNV
NITGTNRYED IKNSDAIIIT AGIARKPGMS RDDLLQTNAA VMKEVGENIK KHSPNAFVIV
VTNPLDAMVS VVYKSSSLPT NMIVGMAGVL DSARFRYFLA SELNISVEDV SAFVLGGHGD
TMVPLINYAS IAGIPLTQII EMGVITRGKV DEIVERTRNG GKEIVDLLKS GSAYYAPASS
AISMLESYLK DKRRILPCAA YLNGEYGVKD LFIGVPTIIG KNGVEKVLEV KMNDSEQEMF
YKSVSAVKEL CQLN
