ID A0A091C3J8_9ENTE Unreviewed; 313 AA.
AC A0A091C3J8;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 37.
DE SubName: Full=L-lactate dehydrogenase {ECO:0000313|EMBL:KFN92376.1};
DE EC=1.-.-.- {ECO:0000313|EMBL:KFN92376.1};
DE EC=1.1.1.- {ECO:0000313|EMBL:KFN92376.1};
DE EC=1.1.1.27 {ECO:0000313|EMBL:KFN92376.1};
GN ORFNames=TMU3MR103_0505 {ECO:0000313|EMBL:KFN92376.1};
OS Tetragenococcus muriaticus 3MR10-3.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae;
OC Tetragenococcus.
OX NCBI_TaxID=1302648 {ECO:0000313|EMBL:KFN92376.1, ECO:0000313|Proteomes:UP000029381};
RN [1] {ECO:0000313|EMBL:KFN92376.1, ECO:0000313|Proteomes:UP000029381}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3MR10-3 {ECO:0000313|EMBL:KFN92376.1,
RC ECO:0000313|Proteomes:UP000029381};
RA Chuea-nongthon C., Rodtong S., Yongsawatdigul J., Steele J.L., Liu X.-y.,
RA Speers J., Glasner J.D., Neeno-Eckwall E.C.;
RT "Genome sequence of Tetragenococcus muriaticus.";
RL Submitted (AUG-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the LDH/MDH superfamily. LDH family.
CC {ECO:0000256|ARBA:ARBA00006054}.
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:KFN92376.1}.
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DR EMBL; JPVT01000050; KFN92376.1; -; Genomic_DNA.
DR RefSeq; WP_028790597.1; NZ_JPVT01000050.1.
DR AlphaFoldDB; A0A091C3J8; -.
DR PATRIC; fig|1302648.3.peg.491; -.
DR Proteomes; UP000029381; Unassembled WGS sequence.
DR GO; GO:0004459; F:L-lactate dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0019752; P:carboxylic acid metabolic process; IEA:InterPro.
DR CDD; cd05291; HicDH_like; 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 InterPro; IPR001557; L-lactate/malate_DH.
DR InterPro; IPR018177; L-lactate_DH_AS.
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:SF31; 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.
DR PROSITE; PS00064; L_LDH; 1.
PE 3: Inferred from homology;
KW NAD {ECO:0000256|PIRSR:PIRSR000102-3};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003369};
KW Reference proteome {ECO:0000313|Proteomes:UP000029381}.
FT DOMAIN 4..146
FT /note="Lactate/malate dehydrogenase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00056"
FT DOMAIN 149..306
FT /note="Lactate/malate dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02866"
FT ACT_SITE 179
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000102-1"
FT BINDING 9..14
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
FT BINDING 34
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
FT BINDING 122..124
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
SQ SEQUENCE 313 AA; 33968 MW; 067852C69DDF7C71 CRC64;
MTRKIGVIGM GNVGSTVAHD IIAKGLADDL VLIDTNEAKV NADALDFADA MANASFHVNL
TVNDYAALKD ADVVISAIGN IQMLQNNTNN DRFVELSFTS KQAANVALKI KESGFNGVLV
VITNPCDVIT LIYQELTELP KNQVIGTGTL LDSARMKRAV GKVFNIDPRS VGGYNLGEHG
NSQFTAWSTV TVLGKSINEI AKEQTVDFAE LDEIARAGGF TVLHGKNYTN YGIATAAVRL
ASLIINDARA ELPVSNFRYE YNTYLSYPAI VGKNGIIKSL QLDLTEEEEQ KLAQSAQYIQ
AKFEETKTDL QIN
//