ID A0A1D2WQA8_9EURY Unreviewed; 315 AA.
AC A0A1D2WQA8;
DT 30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Malate dehydrogenase {ECO:0000313|EMBL:OED01702.1};
GN ORFNames=A9505_02275 {ECO:0000313|EMBL:OED01702.1};
OS Methanobrevibacter sp. A27.
OC Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC Methanobacteriales; Methanobacteriaceae; Methanobrevibacter.
OX NCBI_TaxID=1860099 {ECO:0000313|EMBL:OED01702.1, ECO:0000313|Proteomes:UP000094786};
RN [1] {ECO:0000313|EMBL:OED01702.1, ECO:0000313|Proteomes:UP000094786}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A27 {ECO:0000313|EMBL:OED01702.1,
RC ECO:0000313|Proteomes:UP000094786};
RA Woodcroft B.J.;
RT "Validation of picogram- and femtogram-input DNA libraries for microscale
RT metagenomics.";
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the LDH/MDH superfamily.
CC {ECO:0000256|ARBA:ARBA00008104, ECO:0000256|RuleBase:RU003369}.
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:OED01702.1}.
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DR EMBL; LZPL01000003; OED01702.1; -; Genomic_DNA.
DR RefSeq; WP_069572821.1; NZ_LZPL01000003.1.
DR AlphaFoldDB; A0A1D2WQA8; -.
DR Proteomes; UP000094786; Unassembled WGS sequence.
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: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|PIRSR:PIRSR000102-3};
KW NADP {ECO:0000256|ARBA:ARBA00022857};
KW Oxidoreductase {ECO:0000256|RuleBase:RU003369}.
FT DOMAIN 2..145
FT /note="Lactate/malate dehydrogenase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00056"
FT DOMAIN 149..310
FT /note="Lactate/malate dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02866"
FT ACT_SITE 178
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000102-1"
FT BINDING 8..14
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
FT BINDING 85
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000102-2"
FT BINDING 91
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000102-2"
FT BINDING 98
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
FT BINDING 123
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000102-2"
FT BINDING 154
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000102-2"
SQ SEQUENCE 315 AA; 34523 MW; 005ECA1966CCA195 CRC64;
MVKVSIFGST GTIGKNVAFT LARMDTVDEI VMVSRPKSLD KVKGETYDMY DALAARDIDC
KLIPTCDFNE IRGSEIVLIA AGIHRQPGMN RLELAIPNAK IVRYYSKQIA KYAPDSIILV
ATNPVDVMTT IALEASGFNK MKVIGVGNHL DSLRLKNYFS RKININSSEV HTRVVGEHGN
HMVPLLSSTS IGGIPLKYFE FAKLDVDALV EQLKNAGNTI ISKKGATEYG PAFAISNLIS
TMITDSHKVL TVSFYLEGEV EGVRNVSLGV PAITSKNGIE MIVPIHMNDV EKESFIEAAN
VVRDTTYKVK ENLNI
//
