ID A0A0A1N0J4_9BACI Unreviewed; 312 AA.
AC A0A0A1N0J4;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 27-MAR-2024, entry version 49.
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 ECO:0000313|EMBL:CEI84481.1};
GN ORFNames=BN997_04430 {ECO:0000313|EMBL:CEI84481.1};
OS Oceanobacillus oncorhynchi.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Oceanobacillus.
OX NCBI_TaxID=545501 {ECO:0000313|EMBL:CEI84481.1, ECO:0000313|Proteomes:UP000040453};
RN [1] {ECO:0000313|EMBL:CEI84481.1, ECO:0000313|Proteomes:UP000040453}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Oc5 {ECO:0000313|EMBL:CEI84481.1,
RC ECO:0000313|Proteomes:UP000040453};
RA Urmite Genomes Urmite Genomes;
RL Submitted (NOV-2014) 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 ---------------------------------------------------------------------------
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; CDGG01000001; CEI84481.1; -; Genomic_DNA.
DR RefSeq; WP_042535336.1; NZ_CDGG01000001.1.
DR AlphaFoldDB; A0A0A1N0J4; -.
DR STRING; 545501.BN997_04430; -.
DR OrthoDB; 9802969at2; -.
DR Proteomes; UP000040453; 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:SF34; 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|HAMAP-Rule:MF_00487, ECO:0000256|PIRSR:PIRSR000102-3};
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:UP000040453};
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 312 AA; 33481 MW; B71C77F002BFB6C2 CRC64;
MSSARKKISV IGSGFTGATT ALMVAQKELG DVVLVDIPDM ENPTKGKALD MAEAAPVQGF
DAKVTGTSDY AETKDSDLVI ITAGIARKPG MSRDDLVNTN AKIMNTITKE IVRYSADATI
IVLTNPVDAM TYSVYKASGL PKERVIGQSG VLDTARFRAF VAEELNISVK DITGFVLGGH
GDDMVPLIRY SYAGGIPLEK LISKERLQEI VQRTRTGGGE IVNLLGNGSA YYAPAASLTV
MAEAILKDQR RILPSIAYLE GEYGYDGIYL GVPTVLGGKG IEEVIELDLT EEEKQQLDKS
AKSVKKVIDI LE
//
