ID A0A136WI16_9FIRM Unreviewed; 313 AA.
AC A0A136WI16;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=L-lactate dehydrogenase {ECO:0000256|ARBA:ARBA00012967, ECO:0000256|HAMAP-Rule:MF_00488};
DE Short=L-LDH {ECO:0000256|HAMAP-Rule:MF_00488};
DE EC=1.1.1.27 {ECO:0000256|ARBA:ARBA00012967, ECO:0000256|HAMAP-Rule:MF_00488};
GN Name=ldhB {ECO:0000313|EMBL:KXL54083.1};
GN Synonyms=ldh {ECO:0000256|HAMAP-Rule:MF_00488};
GN ORFNames=CLNEO_01790 {ECO:0000313|EMBL:KXL54083.1};
OS Anaerotignum neopropionicum.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC Anaerotignum.
OX NCBI_TaxID=36847 {ECO:0000313|EMBL:KXL54083.1, ECO:0000313|Proteomes:UP000070539};
RN [1] {ECO:0000313|EMBL:KXL54083.1, ECO:0000313|Proteomes:UP000070539}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM-3847 {ECO:0000313|EMBL:KXL54083.1,
RC ECO:0000313|Proteomes:UP000070539};
RA Poehlein A., Beck M.H., Bengelsdorf F.R., Daniel R., Duerre P.;
RT "Genome sequence of Clostridium neopropionicum X4, DSM-3847.";
RL Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the conversion of lactate to pyruvate.
CC {ECO:0000256|HAMAP-Rule:MF_00488}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(S)-lactate + NAD(+) = H(+) + NADH + pyruvate;
CC Xref=Rhea:RHEA:23444, ChEBI:CHEBI:15361, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16651, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.27;
CC Evidence={ECO:0000256|ARBA:ARBA00001763, ECO:0000256|HAMAP-
CC Rule:MF_00488};
CC -!- PATHWAY: Fermentation; pyruvate fermentation to lactate; (S)-lactate
CC from pyruvate: step 1/1. {ECO:0000256|ARBA:ARBA00004843,
CC ECO:0000256|HAMAP-Rule:MF_00488}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_00488}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00488}.
CC -!- SIMILARITY: Belongs to the LDH/MDH superfamily. LDH family.
CC {ECO:0000256|ARBA:ARBA00006054, ECO:0000256|HAMAP-Rule:MF_00488}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00488}.
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:KXL54083.1}.
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DR EMBL; LRVM01000001; KXL54083.1; -; Genomic_DNA.
DR RefSeq; WP_066083557.1; NZ_LRVM01000001.1.
DR AlphaFoldDB; A0A136WI16; -.
DR STRING; 36847.CLNEO_01790; -.
DR PATRIC; fig|36847.3.peg.222; -.
DR OrthoDB; 9802969at2; -.
DR UniPathway; UPA00554; UER00611.
DR Proteomes; UP000070539; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004459; F:L-lactate dehydrogenase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniRule.
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 HAMAP; MF_00488; Lactate_dehydrog; 1.
DR InterPro; IPR001557; L-lactate/malate_DH.
DR InterPro; IPR011304; L-lactate_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 NCBIfam; TIGR01771; L-LDH-NAD; 1.
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 Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00488};
KW NAD {ECO:0000256|HAMAP-Rule:MF_00488, ECO:0000256|PIRSR:PIRSR000102-3};
KW Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_00488,
KW ECO:0000256|RuleBase:RU003369};
KW Reference proteome {ECO:0000313|Proteomes:UP000070539}.
FT DOMAIN 6..142
FT /note="Lactate/malate dehydrogenase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00056"
FT DOMAIN 145..309
FT /note="Lactate/malate dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02866"
FT ACT_SITE 175
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00488,
FT 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 14
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00488"
FT BINDING 35
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00488,
FT ECO:0000256|PIRSR:PIRSR000102-3"
FT BINDING 40
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00488"
FT BINDING 66
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00488"
FT BINDING 80..81
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00488"
FT BINDING 88
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00488"
FT BINDING 101
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00488"
FT BINDING 118..120
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00488,
FT ECO:0000256|PIRSR:PIRSR000102-3"
FT BINDING 120..123
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00488"
FT BINDING 143
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00488"
FT BINDING 148..151
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00488"
FT BINDING 228
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00488"
SQ SEQUENCE 313 AA; 34148 MW; 8D4CAC47D57F2A34 CRC64;
MKTRSVGIIG VGHVGAHCAY SLAVQGIVDE LVLVDINEQK AISECQDLRD SVAYLPHRVE
VRTGGYADVK DCDVVVISVG VITKSNNRLD ELNVSIGMVN SFVKQVVDAG FDGIFVNITN
PCDIIARQVH KLSGFDKSRV FGTGTGLDSS RFKAVLAREM GIDHKSLVAY TMGEHGDSQM
APWSHVTVNG KPLPELMEKD KKYDVDKEAV LTEAIRGGWV TFAGKGCTEY GIASTLARIV
NVIFHDEKAV MPCSTQLNGE YGQNDLFIST PCVIGKNGVE EVYEMNLTEE EMAAFHHSCD
VIRTNIGYIN EEA
//
