ID D3LTV8_9FIRM Unreviewed; 319 AA.
AC D3LTV8;
DT 20-APR-2010, integrated into UniProtKB/TrEMBL.
DT 20-APR-2010, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE SubName: Full=Lactate/malate dehydrogenase, NAD binding domain protein {ECO:0000313|EMBL:EFD94424.1};
GN ORFNames=HMPREF0889_1408 {ECO:0000313|EMBL:EFD94424.1};
OS Megasphaera genomosp. type_1 str. 28L.
OC Bacteria; Bacillota; Negativicutes; Veillonellales; Veillonellaceae;
OC Megasphaera.
OX NCBI_TaxID=699218 {ECO:0000313|EMBL:EFD94424.1, ECO:0000313|Proteomes:UP000003242};
RN [1] {ECO:0000313|Proteomes:UP000003242}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=28L {ECO:0000313|Proteomes:UP000003242};
RA Madupu R., Durkin A.S., Torralba M., Methe B., Sutton G.G.,
RA Strausberg R.L., Nelson K.E.;
RT "Sequence of Clostridiales genomosp. BVAB3 str. UPII9-5.";
RL Submitted (DEC-2009) 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:EFD94424.1}.
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DR EMBL; ADGP01000013; EFD94424.1; -; Genomic_DNA.
DR RefSeq; WP_007391476.1; NZ_ADGP01000013.1.
DR AlphaFoldDB; D3LTV8; -.
DR STRING; 699218.HMPREF0889_1408; -.
DR eggNOG; COG0039; Bacteria.
DR OrthoDB; 9802969at2; -.
DR Proteomes; UP000003242; Unassembled WGS sequence.
DR GO; GO:0004459; F:L-lactate dehydrogenase activity; IEA:InterPro.
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: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.
DR PROSITE; PS00064; L_LDH; 1.
PE 3: Inferred from homology;
KW NAD {ECO:0000256|PIRSR:PIRSR000102-3};
KW Oxidoreductase {ECO:0000256|RuleBase:RU003369}.
FT DOMAIN 5..145
FT /note="Lactate/malate dehydrogenase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00056"
FT DOMAIN 148..304
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 10..15
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
FT BINDING 35
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 121..123
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 319 AA; 35492 MW; 84C6A0BE9F921876 CRC64;
MERRKVVIIG AGHVGSHVAL SLTQSGIADE IVLLDIEKEK AAAQAMDIDD SLRGSICGHS
TVIRSGTYTD VEDAQILVTA FGRSRRPGEN RLDLFDDSIR MANEIIGRLK QHSFQGIMIS
VSNPADIVCE YIRRAMGWER QRCFGTGTSL ETYRLLRVLS RHLSVSRTSI QAFCMGEHGN
SGFIVWSHIF VNGKAFAHIL QEDKKYKELD LAALQEEVKM AGDVEIDGKG CTEFGIANVV
NMIITAVFHD QKLLWPCSVA LNGEYGEKDV AAGVPCIIGR RGIERVVEMT LHEEEKDKFK
HSCEVIRGFL VRARSLRKS
//
