ID A7I7B6_METB6 Unreviewed; 288 AA.
AC A7I7B6;
DT 11-SEP-2007, integrated into UniProtKB/TrEMBL.
DT 11-SEP-2007, sequence version 1.
DT 24-JAN-2024, entry version 91.
DE RecName: Full=malate dehydrogenase {ECO:0000256|ARBA:ARBA00012995};
DE EC=1.1.1.37 {ECO:0000256|ARBA:ARBA00012995};
GN OrderedLocusNames=Mboo_1109 {ECO:0000313|EMBL:ABS55627.1};
OS Methanoregula boonei (strain DSM 21154 / JCM 14090 / 6A8).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanomicrobiales; Methanoregulaceae; Methanoregula.
OX NCBI_TaxID=456442 {ECO:0000313|EMBL:ABS55627.1, ECO:0000313|Proteomes:UP000002408};
RN [1] {ECO:0000313|Proteomes:UP000002408}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21154 / JCM 14090 / 6A8
RC {ECO:0000313|Proteomes:UP000002408};
RX PubMed=25998264; DOI=10.1099/mic.0.000117;
RA Braeuer S., Cadillo-Quiroz H., Kyrpides N., Woyke T., Goodwin L.,
RA Detter C., Podell S., Yavitt J.B., Zinder S.H.;
RT "Genome of Methanoregula boonei 6A8 reveals adaptations to oligotrophic
RT peatland environments.";
RL Microbiology 161:1572-1581(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 -!- SIMILARITY: Belongs to the LDH/MDH superfamily.
CC {ECO:0000256|ARBA:ARBA00008104, ECO:0000256|RuleBase:RU003369}.
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DR EMBL; CP000780; ABS55627.1; -; Genomic_DNA.
DR RefSeq; WP_012106654.1; NC_009712.1.
DR AlphaFoldDB; A7I7B6; -.
DR STRING; 456442.Mboo_1109; -.
DR GeneID; 5411269; -.
DR KEGG; mbn:Mboo_1109; -.
DR eggNOG; arCOG00246; Archaea.
DR HOGENOM; CLU_045401_2_1_2; -.
DR OMA; CYIIVLT; -.
DR OrthoDB; 2596at2157; -.
DR Proteomes; UP000002408; Chromosome.
DR GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR GO; GO:0019752; P:carboxylic acid metabolic process; IEA:InterPro.
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; IPR036291; NAD(P)-bd_dom_sf.
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|PIRSR:PIRSR000102-3};
KW Oxidoreductase {ECO:0000256|RuleBase:RU003369};
KW Reference proteome {ECO:0000313|Proteomes:UP000002408}.
FT DOMAIN 3..135
FT /note="Lactate/malate dehydrogenase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00056"
FT DOMAIN 157..277
FT /note="Lactate/malate dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02866"
FT ACT_SITE 164
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000102-1"
FT BINDING 8..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|PIRSR:PIRSR000102-3"
FT BINDING 76
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000102-2"
FT BINDING 83
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000102-2"
FT BINDING 90
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
FT BINDING 111..113
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
FT BINDING 113
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000102-2"
FT BINDING 144
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000102-2"
SQ SEQUENCE 288 AA; 31135 MW; 949C75FC3311AEA2 CRC64;
MTRLAVMGVG RIGGEVASLA TLMGLADELV LYDQDPTFLR AQVLDISHTG LPVFLSTDPS
DIKDADICVF AAGLPRNPDI KTRADLLAAN LPVVRACAGL LDGFSGILVT VTNPMDINNY
LLHRLTGLPR ERCIGFGGQL DSARFALALH RRGLNGPAAV LGEHGEHQVP VFSRLKRPIE
ENLRLEILQE LQGSSMDVIK GKGGTVFGPA YHIITLLKML LSGTKETIPC SAVLKGEYQL
SDCSLGVPAR IGTDGIREIV TWDLDRWEQE KMADAGAFVR NLCRTVVP
//