ID S5TKW4_9CORY Unreviewed; 323 AA.
AC S5TKW4;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 24-JAN-2024, entry version 55.
DE RecName: Full=Malate dehydrogenase {ECO:0000256|HAMAP-Rule:MF_01517};
DE EC=1.1.1.37 {ECO:0000256|HAMAP-Rule:MF_01517};
GN Name=mdh {ECO:0000256|HAMAP-Rule:MF_01517};
GN ORFNames=B841_10120 {ECO:0000313|EMBL:AGS35496.1};
OS Corynebacterium maris DSM 45190.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=1224163 {ECO:0000313|EMBL:AGS35496.1, ECO:0000313|Proteomes:UP000015388};
RN [1] {ECO:0000313|EMBL:AGS35496.1, ECO:0000313|Proteomes:UP000015388}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Coryn-1 {ECO:0000313|Proteomes:UP000015388};
RA Schaffert L., Albersmeier A., Kalinowski J., Ruckert C.;
RT "The complete genome sequence of Corynebacterium maris Coryn-1 (=DSM
RT 45190).";
RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the reversible oxidation of malate to oxaloacetate.
CC {ECO:0000256|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:0000256|HAMAP-Rule:MF_01517};
CC -!- SIMILARITY: Belongs to the LDH/MDH superfamily. MDH type 2 family.
CC {ECO:0000256|ARBA:ARBA00009613, ECO:0000256|HAMAP-Rule:MF_01517}.
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DR EMBL; CP003924; AGS35496.1; -; Genomic_DNA.
DR RefSeq; WP_020935429.1; NC_021915.1.
DR AlphaFoldDB; S5TKW4; -.
DR STRING; 1224163.B841_10120; -.
DR KEGG; cmd:B841_10120; -.
DR PATRIC; fig|1224163.3.peg.2042; -.
DR eggNOG; COG0039; Bacteria.
DR HOGENOM; CLU_040727_2_0_11; -.
DR OrthoDB; 9802969at2; -.
DR Proteomes; UP000015388; 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 CDD; cd01338; MDH_choloroplast_like; 1.
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 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 NCBIfam; TIGR01759; MalateDH-SF1; 1.
DR PANTHER; PTHR23382; MALATE DEHYDROGENASE; 1.
DR PANTHER; PTHR23382:SF0; MALATE DEHYDROGENASE 2, MITOCHONDRIAL-RELATED; 1.
DR Pfam; PF02866; Ldh_1_C; 1.
DR Pfam; PF00056; Ldh_1_N; 1.
DR PIRSF; PIRSF000102; Lac_mal_DH; 1.
DR SUPFAM; SSF56327; LDH C-terminal domain-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE 3: Inferred from homology;
KW NAD {ECO:0000256|HAMAP-Rule:MF_01517, ECO:0000256|PIRSR:PIRSR000102-3};
KW Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_01517,
KW ECO:0000256|RuleBase:RU003369};
KW Reference proteome {ECO:0000313|Proteomes:UP000015388};
KW Tricarboxylic acid cycle {ECO:0000256|HAMAP-Rule:MF_01517}.
FT DOMAIN 5..144
FT /note="Lactate/malate dehydrogenase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00056"
FT DOMAIN 156..316
FT /note="Lactate/malate dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02866"
FT ACT_SITE 186
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01517,
FT ECO:0000256|PIRSR:PIRSR000102-1"
FT BINDING 10..16
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01517"
FT BINDING 91
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01517,
FT ECO:0000256|PIRSR:PIRSR000102-2"
FT BINDING 97
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01517,
FT ECO:0000256|PIRSR:PIRSR000102-2"
FT BINDING 104
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01517,
FT ECO:0000256|PIRSR:PIRSR000102-3"
FT BINDING 111
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01517"
FT BINDING 128..130
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01517,
FT ECO:0000256|PIRSR:PIRSR000102-3"
FT BINDING 130
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01517,
FT ECO:0000256|PIRSR:PIRSR000102-2"
FT BINDING 161
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01517,
FT ECO:0000256|PIRSR:PIRSR000102-2"
SQ SEQUENCE 323 AA; 34237 MW; 1D0FEF0886E26B84 CRC64;
MTTAKITVTG AAGNIAYSLL WRLAAGEVYG PDTPVELSLL EIPQATDAAE GVAMELADSA
FPLLRSITVT DDANTAFDGA NAAFLVGAKP RGKGMERADL LAANGGIFGP QGAAINEHAA
DDVRVLVVGN PANTNALIAQ SAAPDVPAER FTALMRLDHN RALGLLSTRL EVPTTDIEDV
VVWGNHSATQ FPDLTYATVD GRPALELVEQ EWYESEFIPR VAKRGAEIIE VRGKSSAASA
ASAAVDHMHD WIHGTEAWSS AAVVSDGSYG IDEGLVAGVP TVARNGKWEI VQGLELNDFQ
RGRIEESVQE LREERSAVQN LLG
//