ID F9MQB5_9FIRM Unreviewed; 316 AA.
AC F9MQB5;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 24-JAN-2024, entry version 46.
DE SubName: Full=Putative L-lactate dehydrogenase {ECO:0000313|EMBL:EGS32626.1};
GN ORFNames=HMPREF1040_1067 {ECO:0000313|EMBL:EGS32626.1};
OS Megasphaera sp. UPII 135-E.
OC Bacteria; Bacillota; Negativicutes; Veillonellales; Veillonellaceae;
OC Megasphaera.
OX NCBI_TaxID=1000569 {ECO:0000313|EMBL:EGS32626.1, ECO:0000313|Proteomes:UP000004137};
RN [1] {ECO:0000313|EMBL:EGS32626.1, ECO:0000313|Proteomes:UP000004137}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UPII 135-E {ECO:0000313|EMBL:EGS32626.1,
RC ECO:0000313|Proteomes:UP000004137};
RA Harkins D.M., Madupu R., Durkin A.S., Torralba M., Methe B., Sutton G.G.,
RA Nelson K.E.;
RL Submitted (JUN-2011) 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:EGS32626.1}.
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DR EMBL; AFUG01000038; EGS32626.1; -; Genomic_DNA.
DR RefSeq; WP_007393000.1; NZ_AFUG01000038.1.
DR AlphaFoldDB; F9MQB5; -.
DR eggNOG; COG0039; Bacteria.
DR OrthoDB; 9802969at2; -.
DR Proteomes; UP000004137; 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 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: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.
PE 3: Inferred from homology;
KW NAD {ECO:0000256|PIRSR:PIRSR000102-3};
KW Oxidoreductase {ECO:0000256|RuleBase:RU003369};
KW Reference proteome {ECO:0000313|Proteomes:UP000004137}.
FT DOMAIN 8..146
FT /note="Lactate/malate dehydrogenase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00056"
FT DOMAIN 149..314
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 12..17
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
FT BINDING 37
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 316 AA; 34438 MW; 6827AE5C8BD3EB58 CRC64;
MGLKKRIVGV VGLGHVGAHV AFNLGMMGIA DAVYLCDKNE QKVLSEVQDL NDAAPFMPNH
TVYTVVDYAG LKDCDIIVNA VGNIALLATH DRDKELENSV KEVADFIPKI MAAGFDGIFV
NITNPCDVIT NLIREKSGLP TQRVVGTGTL LDSARLIAVI SKHTGLDARG FTAFMIGEHG
NAQMAAWSCI SFYGKPLREL TNKKEFQFTK EESQAMAIKG AWVTYVGKQC TEYGVASAGA
TLVRTILRDE KRIIPVSAYL NGEYGEKGIY CGIPAIISAK GVESIIEYEL TDEEKVEFKQ
CCDAIRKNIE KSHALL
//