ID A0A345UFW0_9BACT Unreviewed; 317 AA.
AC A0A345UFW0;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-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=CYPRO_0073 {ECO:0000313|EMBL:AXI99361.1};
OS Cyclonatronum proteinivorum.
OC Bacteria; Balneolota; Balneolia; Balneolales; Cyclonatronaceae;
OC Cyclonatronum.
OX NCBI_TaxID=1457365 {ECO:0000313|EMBL:AXI99361.1, ECO:0000313|Proteomes:UP000254808};
RN [1] {ECO:0000313|EMBL:AXI99361.1, ECO:0000313|Proteomes:UP000254808}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Omega {ECO:0000313|EMBL:AXI99361.1,
RC ECO:0000313|Proteomes:UP000254808};
RA Toshchakov S.V., Korzhenkov A., Samarov N.I., Kublanov I.V., Muntyan M.S.,
RA Sorokin D.Y.;
RT "Phenotypic and genomic properties of Cyclonatronum proteinivorum gen.
RT nov., sp. nov., a haloalkaliphilic bacteroidete from soda lakes possessing
RT Na+-translocating rhodopsin.";
RL Submitted (MAR-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. MDH type 3 family.
CC {ECO:0000256|HAMAP-Rule:MF_00487}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00487}.
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DR EMBL; CP027806; AXI99361.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A345UFW0; -.
DR KEGG; cprv:CYPRO_0073; -.
DR OrthoDB; 9802969at2; -.
DR Proteomes; UP000254808; Chromosome.
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 Reference proteome {ECO:0000313|Proteomes:UP000254808};
KW Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532, ECO:0000256|HAMAP-
KW Rule:MF_00487}.
FT DOMAIN 1..149
FT /note="Lactate/malate dehydrogenase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00056"
FT DOMAIN 154..311
FT /note="Lactate/malate dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02866"
FT ACT_SITE 182
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00487,
FT 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 33
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 89
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00487,
FT ECO:0000256|PIRSR:PIRSR000102-2"
FT BINDING 95
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00487,
FT ECO:0000256|PIRSR:PIRSR000102-2"
FT BINDING 102
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 125..127
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 127
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00487,
FT ECO:0000256|PIRSR:PIRSR000102-2"
FT BINDING 158
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00487,
FT ECO:0000256|PIRSR:PIRSR000102-2"
SQ SEQUENCE 317 AA; 34046 MW; 70096F74371DB5CF CRC64;
MKITVVGAGG NVGSTAALTV AQRNFAKQVV AIDLEKKDGE KTFYPAKGRA LDQWQTAPIH
GFSTHLFGSS NYEDTKGSDI CIITAGVPRR PGMSRDDLLS INANIVKSVT EQLVAHSPDT
IIIVVSNPLD VMTYVAWKAS GLPSSKVMGM AGILDTARYC AFLAEELNVS PKDIQCQILG
GHGDTMVPLP RYTTVSGIPI RQLISDEKLN AIIERAKVGG GELVGLMGTS AWYAPGAAAA
QMAEAIALDE NRIFPCSAWL TGEFGHKDLY IGVPVKLNRQ GISEIVQIDL DADEQKLFDD
SVASVRTALE DLERIMK
//
