ID G9IYH2_EDWTA Unreviewed; 213 AA.
AC G9IYH2;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE RecName: Full=Malate dehydrogenase {ECO:0000256|ARBA:ARBA00020382, ECO:0000256|RuleBase:RU000422};
DE EC=1.1.1.37 {ECO:0000256|ARBA:ARBA00012995, ECO:0000256|RuleBase:RU000422};
DE Flags: Fragment;
GN Name=mdh {ECO:0000313|EMBL:AEW46514.1};
OS Edwardsiella tarda.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Hafniaceae; Edwardsiella.
OX NCBI_TaxID=636 {ECO:0000313|EMBL:AEW46514.1};
RN [1] {ECO:0000313|EMBL:AEW46514.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=EIB107 {ECO:0000313|EMBL:AEW46514.1};
RX PubMed=22590641; DOI=10.1371/journal.pone.0036987;
RA Yang M., Lv Y., Xiao J., Wu H., Zheng H., Liu Q., Zhang Y., Wang Q.;
RT "Edwardsiella comparative phylogenomics reveal the new intra/inter-species
RT taxonomic relationships, virulence evolution and niche adaptation
RT mechanisms.";
RL PLoS ONE 7:e36987-E36987(2012).
CC -!- FUNCTION: Catalyzes the reversible oxidation of malate to oxaloacetate.
CC {ECO:0000256|ARBA:ARBA00003966}.
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:0000256|RuleBase:RU000422};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC -!- SIMILARITY: Belongs to the LDH/MDH superfamily. MDH type 1 family.
CC {ECO:0000256|ARBA:ARBA00008824}.
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DR EMBL; JN709570; AEW46514.1; -; Genomic_DNA.
DR AlphaFoldDB; G9IYH2; -.
DR GO; GO:0030060; F:L-malate dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0006108; P:malate metabolic process; IEA:InterPro.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-KW.
DR Gene3D; 3.90.110.10; Lactate dehydrogenase/glycoside hydrolase, family 4, C-terminal; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
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; IPR001252; Malate_DH_AS.
DR InterPro; IPR010097; Malate_DH_type1.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR NCBIfam; TIGR01772; MDH_euk_gproteo; 1.
DR PANTHER; PTHR11540; MALATE AND LACTATE DEHYDROGENASE; 1.
DR PANTHER; PTHR11540:SF16; MALATE DEHYDROGENASE, MITOCHONDRIAL; 1.
DR Pfam; PF02866; Ldh_1_C; 1.
DR Pfam; PF00056; Ldh_1_N; 1.
DR SUPFAM; SSF56327; LDH C-terminal domain-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS00068; MDH; 1.
PE 3: Inferred from homology;
KW NAD {ECO:0000256|RuleBase:RU000422};
KW Oxidoreductase {ECO:0000256|RuleBase:RU003369};
KW Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532,
KW ECO:0000256|RuleBase:RU000422}.
FT DOMAIN 2..80
FT /note="Lactate/malate dehydrogenase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00056"
FT DOMAIN 82..212
FT /note="Lactate/malate dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02866"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AEW46514.1"
FT NON_TER 213
FT /evidence="ECO:0000313|EMBL:AEW46514.1"
SQ SEQUENCE 213 AA; 22334 MW; 326C62A8B52BF0E1 CRC64;
ALEGADIVLI SAGVARKPGM DRSDLFNINA GIIRNLIGQV ARTSPNACIG IITNPVNTMV
PIAAEVLKKA GVYNPNKLFG VTTLDIIRSN TFVGELKHLD PTTLDIPVIG GHSGVTILPL
LSQIPGVSLS EQEVADLTKR IQNAGTEVVE AKAGGGSATL AMGQAAARFA LSLVRAMQGD
ENVVECGYVE SDGEYARFFA QPLLLGKEGL VQR
//
