ID A0A1X7CRX6_9BACI Unreviewed; 312 AA.
AC A0A1X7CRX6; A0A0H4L150;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 27-MAR-2024, entry version 32.
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:RJS66519.1};
GN ORFNames=B1B01_00815 {ECO:0000313|EMBL:OXS70886.1}, BEH_21145
GN {ECO:0000313|EMBL:AKO94383.1}, CJ485_18150
GN {ECO:0000313|EMBL:RJS66519.1}, SAMN06296056_101165
GN {ECO:0000313|EMBL:SMF01653.1};
OS Priestia filamentosa.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Priestia.
OX NCBI_TaxID=1402861 {ECO:0000313|EMBL:SMF01653.1, ECO:0000313|Proteomes:UP000192915};
RN [1] {ECO:0000313|EMBL:AKO94383.1, ECO:0000313|Proteomes:UP000036202}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hbe603 {ECO:0000313|EMBL:AKO94383.1,
RC ECO:0000313|Proteomes:UP000036202};
RX PubMed=26248285;
RA Jia N., Du J., Ding M.Z., Gao F., Yuan Y.J.;
RT "Genome Sequence of Bacillus endophyticus and Analysis of Its Companion
RT Mechanism in the Ketogulonigenium vulgare-Bacillus Strain Consortium.";
RL PLoS ONE 10:E0135104-E0135104(2015).
RN [2] {ECO:0000313|Proteomes:UP000036202}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hbe603 {ECO:0000313|Proteomes:UP000036202};
RA Jia N., Du J., Ding M.-Z., Gao F., Yuan Y.-J.;
RT "Genome Sequence of Bacillus endophyticus and Analysis of its Companion
RT Mechanism in the Ketogulonigenium vulgare-Bacillus strain Consortium.";
RL Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:AKO94383.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Hbe603 {ECO:0000313|EMBL:AKO94383.1};
RA Lavstsen T., Jespersen J.S.;
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|Proteomes:UP000215399}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 27955 {ECO:0000313|Proteomes:UP000215399};
RA Dastager S.G., Neurgaonkar P.S., Dharne M.S.;
RT "Bacillus sp. V-88(T) DSM27956, whole genome shotgun sequencing project.";
RL Submitted (MAR-2017) to the EMBL/GenBank/DDBJ databases.
RN [5] {ECO:0000313|EMBL:SMF01653.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 27955 {ECO:0000313|EMBL:OXS70886.1}, and SGD-14
RC {ECO:0000313|EMBL:SMF01653.1};
RA Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL Submitted (APR-2017) to the EMBL/GenBank/DDBJ databases.
RN [6] {ECO:0000313|Proteomes:UP000192915}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SGD-14 {ECO:0000313|Proteomes:UP000192915};
RA Varghese N., Submissions S.;
RL Submitted (APR-2017) to the EMBL/GenBank/DDBJ databases.
RN [7] {ECO:0000313|EMBL:RJS66519.1, ECO:0000313|Proteomes:UP000274910}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PK5_39 {ECO:0000313|EMBL:RJS66519.1,
RC ECO:0000313|Proteomes:UP000274910};
RA Bokhari A., Bougouffa S., Essack M., Andres-Barrao C., Saad M., Bajic V.B.,
RA Hirt H.;
RT "Complete genomes of four Endophytic plant-growth promoting Bacillus that
RT were isolated from a desert in Pakistan.";
RL Submitted (AUG-2017) 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; CP011974; AKO94383.1; -; Genomic_DNA.
DR EMBL; MWSI01000001; OXS70886.1; -; Genomic_DNA.
DR EMBL; NQYF01000001; RJS66519.1; -; Genomic_DNA.
DR EMBL; FXAJ01000001; SMF01653.1; -; Genomic_DNA.
DR RefSeq; WP_019391219.1; NZ_NQYF01000001.1.
DR AlphaFoldDB; A0A1X7CRX6; -.
DR KEGG; beo:BEH_21145; -.
DR PATRIC; fig|135735.6.peg.4474; -.
DR OrthoDB; 9802969at2; -.
DR Proteomes; UP000036202; Chromosome.
DR Proteomes; UP000192915; Unassembled WGS sequence.
DR Proteomes; UP000215399; Unassembled WGS sequence.
DR Proteomes; UP000274910; 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:UP000036202};
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..308
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; 33521 MW; 8F83B949604DD745 CRC64;
MTMRRKKISV IGAGFTGATT AFLLGQKELG DVVLVDIPNA EGPTKGKALD MLEASPIEGF
DSNIVGTSNY EDTANSDVVI ITAGIARKPG MSRDDLVTTN QKVMKSVTQE IVKYSPDCHI
IVLTNPVDAM TYTVYKESGF PKNRVIGQSG VLDTGRFRTF VAQELNVSVK DVTGFVLGGH
GDDMVPLVRY SYAGGIPLET LIPKERLDAI VERTRKGGGE IVGLLGNGSA YYAPAASLVE
MTEAIVKDQR RILPSIAYLE GEYGYQGIYL GVPTVLGGNG IEQVIELELT DPERAQLDQS
AESVKKVMSV LV
//
