ID A0A1U7MJF3_9FIRM Unreviewed; 301 AA.
AC A0A1U7MJF3;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=L-lactate dehydrogenase {ECO:0000313|EMBL:OLS57566.1};
DE EC=1.1.1.27 {ECO:0000313|EMBL:OLS57566.1};
GN Name=ldh {ECO:0000313|EMBL:OLS57566.1};
GN ORFNames=SPSPH_10820 {ECO:0000313|EMBL:OLS57566.1};
OS Sporomusa sphaeroides DSM 2875.
OC Bacteria; Bacillota; Negativicutes; Selenomonadales; Sporomusaceae;
OC Sporomusa.
OX NCBI_TaxID=1337886 {ECO:0000313|EMBL:OLS57566.1, ECO:0000313|Proteomes:UP000186950};
RN [1] {ECO:0000313|EMBL:OLS57566.1, ECO:0000313|Proteomes:UP000186950}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 2875 {ECO:0000313|EMBL:OLS57566.1,
RC ECO:0000313|Proteomes:UP000186950};
RA Poehlein A., Daniel R.;
RT "Genome sequence of Sporomusa sphaeroides DSM 2875.";
RL Submitted (FEB-2016) 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:OLS57566.1}.
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DR EMBL; LSLJ01000001; OLS57566.1; -; Genomic_DNA.
DR RefSeq; WP_075753995.1; NZ_LSLJ01000001.1.
DR AlphaFoldDB; A0A1U7MJF3; -.
DR STRING; 1337886.SPSPH_10820; -.
DR OrthoDB; 9802969at2; -.
DR Proteomes; UP000186950; 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 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 Oxidoreductase {ECO:0000256|RuleBase:RU003369,
KW ECO:0000313|EMBL:OLS57566.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000186950}.
FT DOMAIN 1..139
FT /note="Lactate/malate dehydrogenase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00056"
FT DOMAIN 142..297
FT /note="Lactate/malate dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02866"
FT ACT_SITE 172
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000102-1"
FT BINDING 7..12
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
FT BINDING 32
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
FT BINDING 79
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000102-2"
FT BINDING 85
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000102-2"
FT BINDING 92
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
FT BINDING 115..117
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
FT BINDING 117
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000102-2"
FT BINDING 148
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000102-2"
SQ SEQUENCE 301 AA; 31808 MW; 116BEC8686D11775 CRC64;
MKISFIGSGK VGVAAAYTAA LKGLAQEILL TDASADKAYG EALDLLQCQA FCPQARITHG
QIRDTANSDI VVISAGIPRR ADEPRVMLLS RNASLIAAIV KEAVALSPQC ILLIITNPLD
VMTHLAYQVS GLPAERVIGM GTVLDTARYR SYLAQHFSVD ARDIDAYVIG EHGETMVPLT
GNITIKGVPL ATLPAYDNTV ITRIGQEVEA ASGQVIALKG GTIYAPAASA CEILGAIVND
DRKVLPVSSF NSRYKTAVSL PTVVGRHGAG PVLNIPMSPS ETTAFAHSVA NIKRYVDELE
V
//
