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Database: UniProt
Entry: U3U7J9_9GAMM
LinkDB: U3U7J9_9GAMM
Original site: U3U7J9_9GAMM 
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
//
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