GenomeNet

Database: UniProt
Entry: A0A2V3VKT9_9BACI
LinkDB: A0A2V3VKT9_9BACI
Original site: A0A2V3VKT9_9BACI 
ID   A0A2V3VKT9_9BACI        Unreviewed;       316 AA.
AC   A0A2V3VKT9;
DT   12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT   12-SEP-2018, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   RecName: Full=Malate dehydrogenase {ECO:0000256|HAMAP-Rule:MF_00487};
DE            EC=1.1.1.37 {ECO:0000256|HAMAP-Rule:MF_00487};
GN   Name=mdh {ECO:0000256|HAMAP-Rule:MF_00487};
GN   ORFNames=DFR56_11816 {ECO:0000313|EMBL:PXW82442.1};
OS   Pseudogracilibacillus auburnensis.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae;
OC   Pseudogracilibacillus.
OX   NCBI_TaxID=1494959 {ECO:0000313|EMBL:PXW82442.1, ECO:0000313|Proteomes:UP000247978};
RN   [1] {ECO:0000313|EMBL:PXW82442.1, ECO:0000313|Proteomes:UP000247978}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 28556 {ECO:0000313|EMBL:PXW82442.1,
RC   ECO:0000313|Proteomes:UP000247978};
RA   Goeker M.;
RT   "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT   most valuable type-strain genomes for metagenomic binning, comparative
RT   biology and taxonomic classification.";
RL   Submitted (MAY-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the reversible oxidation of malate to oxaloacetate.
CC       {ECO:0000256|HAMAP-Rule:MF_00487}.
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_00487};
CC   -!- SIMILARITY: Belongs to the LDH/MDH superfamily. LDH family.
CC       {ECO:0000256|ARBA:ARBA00006054}.
CC   -!- SIMILARITY: Belongs to the LDH/MDH superfamily. MDH type 3 family.
CC       {ECO:0000256|HAMAP-Rule:MF_00487}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:PXW82442.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; QJJQ01000018; PXW82442.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2V3VKT9; -.
DR   OrthoDB; 9802969at2; -.
DR   Proteomes; UP000247978; Unassembled WGS sequence.
DR   GO; GO:0030060; F:L-malate dehydrogenase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0019752; P:carboxylic acid metabolic process; IEA:InterPro.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-UniRule.
DR   CDD; cd01339; LDH-like_MDH; 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_00487; Malate_dehydrog_3; 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; IPR011275; Malate_DH_type3.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   NCBIfam; TIGR01763; MalateDH_bact; 1.
DR   PANTHER; PTHR43128; L-2-HYDROXYCARBOXYLATE DEHYDROGENASE (NAD(P)(+)); 1.
DR   PANTHER; PTHR43128:SF16; L-LACTATE DEHYDROGENASE; 1.
DR   Pfam; PF02866; Ldh_1_C; 1.
DR   Pfam; PF00056; Ldh_1_N; 1.
DR   PIRSF; PIRSF000102; Lac_mal_DH; 1.
DR   PRINTS; PR00086; LLDHDRGNASE.
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|ARBA:ARBA00023027, ECO:0000256|HAMAP-Rule:MF_00487};
KW   Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_00487,
KW   ECO:0000256|RuleBase:RU003369};
KW   Phosphoprotein {ECO:0000256|HAMAP-Rule:MF_00487};
KW   Reference proteome {ECO:0000313|Proteomes:UP000247978};
KW   Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532, ECO:0000256|HAMAP-
KW   Rule:MF_00487}.
FT   DOMAIN          7..147
FT                   /note="Lactate/malate dehydrogenase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00056"
FT   DOMAIN          152..309
FT                   /note="Lactate/malate dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02866"
FT   ACT_SITE        180
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00487,
FT                   ECO:0000256|PIRSR:PIRSR000102-1"
FT   BINDING         12..17
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00487,
FT                   ECO:0000256|PIRSR:PIRSR000102-3"
FT   BINDING         36
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00487,
FT                   ECO:0000256|PIRSR:PIRSR000102-3"
FT   BINDING         87
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00487,
FT                   ECO:0000256|PIRSR:PIRSR000102-2"
FT   BINDING         93
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00487,
FT                   ECO:0000256|PIRSR:PIRSR000102-2"
FT   BINDING         100
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00487,
FT                   ECO:0000256|PIRSR:PIRSR000102-3"
FT   BINDING         123..125
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00487"
FT   BINDING         125
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00487,
FT                   ECO:0000256|PIRSR:PIRSR000102-2"
FT   BINDING         156
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00487,
FT                   ECO:0000256|PIRSR:PIRSR000102-2"
FT   MOD_RES         149
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00487"
SQ   SEQUENCE   316 AA;  33837 MW;  8964854C91974BF1 CRC64;
     MSFKRNKIAV IGAGYTGATT ALMLAQKELG DVVLLDLPNV ENPTKGKALD MLEASPIQRF
     NSNIIGTSSY EDIEGVNMVI ITAGIPRKPG MSRDDLVNTN VSVMKSVAEQ VKTYAPDSII
     LVLSNPVDAM TYVCHNVTGF PKNRVIGQSG ILDTARFNTF VAEELNISVE DISGFVLGGH
     GDEMVPLIRY SYAGGIPLQL LIPEKRLEEI IERTRKGGGE IVSLLGDGSA YYAPAAAIVE
     MAEAIILDKK KIIPSITLLE GEYGYHNLYL GVPTILGGNG VESVIELPLT NEEKDGLAVS
     ANAVQSVINI CDQVIS
//
DBGET integrated database retrieval system