ID U3U7J9_9GAMM Unreviewed; 311 AA.
AC U3U7J9;
DT 11-DEC-2013, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2013, sequence version 1.
DT 24-JAN-2024, entry version 52.
DE RecName: Full=Malate dehydrogenase {ECO:0000256|ARBA:ARBA00020382};
DE EC=1.1.1.37 {ECO:0000256|ARBA:ARBA00012995};
GN Name=mdh {ECO:0000313|EMBL:BAO00239.1};
GN ORFNames=BMSBPS_0741 {ECO:0000313|EMBL:AKC32512.1}, HHS_02690
GN {ECO:0000313|EMBL:BAO00239.1};
OS Candidatus Pantoea carbekii.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Pantoea.
OX NCBI_TaxID=1235990 {ECO:0000313|EMBL:BAO00239.1, ECO:0000313|Proteomes:UP000016900};
RN [1] {ECO:0000313|EMBL:BAO00239.1, ECO:0000313|Proteomes:UP000016900}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Kobayashi H., Fujii-Muramatsu R., Takeishi K., Noda H.;
RT "Genome sequence of the symbiont of the pentatomidae stink bug Halyomorpha
RT halys.";
RL Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AKC32512.1, ECO:0000313|Proteomes:UP000060036}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=US {ECO:0000313|EMBL:AKC32512.1,
RC ECO:0000313|Proteomes:UP000060036};
RX PubMed=25587021; DOI=10.1093/gbe/evv006;
RA Kenyon L.J., Meulia T., Sabree Z.L.;
RT "Habitat visualization and genomic analysis of "Candidatus Pantoea
RT carbekii," the primary symbiont of the brown marmorated stink bug.";
RL Genome Biol. Evol. 7:620-635(2015).
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|ARBA:ARBA00000774};
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; CP010907; AKC32512.1; -; Genomic_DNA.
DR EMBL; AP012554; BAO00239.1; -; Genomic_DNA.
DR RefSeq; WP_022564258.1; NZ_CP010907.1.
DR AlphaFoldDB; U3U7J9; -.
DR STRING; 1235990.BMSBPS_0741; -.
DR KEGG; hhs:HHS_02690; -.
DR KEGG; pck:BMSBPS_0741; -.
DR PATRIC; fig|1235990.3.peg.270; -.
DR eggNOG; COG0039; Bacteria.
DR OrthoDB; 9802969at2; -.
DR Proteomes; UP000016900; Chromosome.
DR Proteomes; UP000060036; Chromosome.
DR GO; GO:0030060; F:L-malate dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0019752; P:carboxylic acid metabolic process; IEA:InterPro.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-KW.
DR CDD; cd01337; MDH_glyoxysomal_mitochondrial; 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 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; 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 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|PIRSR:PIRSR000102-3};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003369};
KW Reference proteome {ECO:0000313|Proteomes:UP000016900};
KW Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532}.
FT DOMAIN 1..145
FT /note="Lactate/malate dehydrogenase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00056"
FT DOMAIN 148..310
FT /note="Lactate/malate dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02866"
FT ACT_SITE 177
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000102-1"
FT BINDING 7..13
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
FT BINDING 34
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
FT BINDING 81
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000102-2"
FT BINDING 87
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000102-2"
FT BINDING 94
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
FT BINDING 117..119
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
FT BINDING 119
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000102-2"
FT BINDING 153
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000102-2"
FT BINDING 227
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
SQ SEQUENCE 311 AA; 33380 MW; 2F97B82C3DE0BB12 CRC64;
MKITLLGAAG GIGQTLSLLL KIQLPSGSSL SLYDITSVIP GLAIDLNHIP TGVKVEGFNG
AYAIPALRDA NIVLISAGIA RKPGMDRADL FHVNAKIIYD LMNQVASIAP KALIGIITNP
INSMVVVAAK VLKKAGVYDK KRLFGISTLD IMRANTFVAQ CKNKQPTEIE VSVIGGHSGI
TILPLLSQIK NIHFSNQEVI DLTRRIQNAG SEVVKAKAGA GSATLSMSHA AARFSLSLVR
ALRGEKNIVE CAYVEGNGEY TNFFAQPLLL DENGIAEYLP IGVLSTFEQL TLNNMLETLK
KEIKQGEEFV R
//