MDH_ACISJ
ID MDH_ACISJ Reviewed; 328 AA.
AC A1W9K7;
DT 26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 26-JUN-2007, sequence version 2.
DT 03-AUG-2022, entry version 78.
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=Ajs_2791;
OS Acidovorax sp. (strain JS42).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Acidovorax; unclassified Acidovorax.
OX NCBI_TaxID=232721;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JS42;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chertkov O., Brettin T.,
RA Bruce D., Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Kim E., Stahl D., Richardson P.;
RT "Complete sequence of chromosome 1 of Acidovorax sp. JS42.";
RL Submitted (DEC-2006) 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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABM42932.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; CP000539; ABM42932.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_041836045.1; NC_008782.1.
DR AlphaFoldDB; A1W9K7; -.
DR SMR; A1W9K7; -.
DR STRING; 232721.Ajs_2791; -.
DR PRIDE; A1W9K7; -.
DR EnsemblBacteria; ABM42932; ABM42932; Ajs_2791.
DR KEGG; ajs:Ajs_2791; -.
DR eggNOG; COG0039; Bacteria.
DR HOGENOM; CLU_040727_2_0_4; -.
DR Proteomes; UP000000645; 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..328
FT /note="Malate dehydrogenase"
FT /id="PRO_0000292367"
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; 34838 MW; A02967E44E7FA9BD CRC64;
MSKKPVRVAV TGAAGQIGYA LLFRIASGEM LGKDQPVILQ LLEIPDEKAQ NALKGVIMEL
EDCAFPLLAG IEAHSDPMTA FKDTDYALLV GARPRGPGME RADLLAANAQ IFTAQGKALN
AVASRNVKVL VVGNPANTNA YIAMKSAPDL PAKNFTAMLR LDHNRAASQL AAKGGFKVGD
IKKLTVWGNH SPTMYADYRF ATVDGKSVKD AINDPAWYKD VFLPTVGKRG AAIIAARGLS
SAASAANAAI DHMRDWALGS KGEWVTMGVP SNGEYGIPAG IVFGFPVTTE NGEYKIVEGL
PIDAFSQECI DKTLAELQGE QDGVKHLL
