ID E4LGE8_9FIRM Unreviewed; 315 AA.
AC E4LGE8;
DT 08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT 08-FEB-2011, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE SubName: Full=Putative L-lactate dehydrogenase {ECO:0000313|EMBL:EFR59260.1};
GN ORFNames=HMPREF9199_0537 {ECO:0000313|EMBL:EFR59260.1};
OS Veillonella sp. oral taxon 158 str. F0412.
OC Bacteria; Bacillota; Negativicutes; Veillonellales; Veillonellaceae;
OC Veillonella.
OX NCBI_TaxID=879309 {ECO:0000313|EMBL:EFR59260.1, ECO:0000313|Proteomes:UP000003565};
RN [1] {ECO:0000313|EMBL:EFR59260.1, ECO:0000313|Proteomes:UP000003565}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0412 {ECO:0000313|EMBL:EFR59260.1,
RC ECO:0000313|Proteomes:UP000003565};
RA Durkin A.S., Madupu R., Torralba M., Gillis M., Methe B., Sutton G.,
RA Nelson K.E.;
RL Submitted (NOV-2010) 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:EFR59260.1}.
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DR EMBL; AENU01000021; EFR59260.1; -; Genomic_DNA.
DR RefSeq; WP_009352685.1; NZ_AENU01000021.1.
DR AlphaFoldDB; E4LGE8; -.
DR STRING; 879309.HMPREF9199_0537; -.
DR eggNOG; COG0039; Bacteria.
DR OrthoDB; 9802969at2; -.
DR Proteomes; UP000003565; 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 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; 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}.
FT DOMAIN 5..142
FT /note="Lactate/malate dehydrogenase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00056"
FT DOMAIN 146..312
FT /note="Lactate/malate dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02866"
FT ACT_SITE 176
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 119..121
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
SQ SEQUENCE 315 AA; 34270 MW; 91D1ED3DD212E2A3 CRC64;
MKLRKVGIIG TGHVGSHVAF SLALQGEVDE LYMMDIDEKK AKAQAMDIND AVSYIPHKVI
ATAGPIEGCG DCDILVFSAG PLPNLYQDRL ESLGETVEVL KDVIPRIKQS GFDGFIISIS
NPADVVATYL CKHLNWNPKR IISTGTALDS ARLQKELAHI FNISNRSITA YCLGEHGGSA
MVPWSHVCVQ GKPLEQLQQE LPHRFPTLDH QQVLDDVKIG GYHVLAGKGS TEFGIASATT
ELIRAVFHDE KKVLPCSCYL DGQYGESGIF ASTPAVIGKD GIEDILELQL TVEELTLFKA
SCAIIREHAT KAETM
//
