ID A0A086ZJN3_9BIFI Unreviewed; 325 AA.
AC A0A086ZJN3;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=L-lactate dehydrogenase {ECO:0000313|EMBL:KFI46733.1};
DE EC=1.1.1.27 {ECO:0000313|EMBL:KFI46733.1};
GN ORFNames=BBOH_0205 {ECO:0000313|EMBL:KFI46733.1};
OS Bifidobacterium bohemicum DSM 22767.
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=1437606 {ECO:0000313|EMBL:KFI46733.1, ECO:0000313|Proteomes:UP000029096};
RN [1] {ECO:0000313|EMBL:KFI46733.1, ECO:0000313|Proteomes:UP000029096}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22767 {ECO:0000313|EMBL:KFI46733.1,
RC ECO:0000313|Proteomes:UP000029096};
RA Ventura M., Milani C., Lugli G.A.;
RT "Genomics of Bifidobacteria.";
RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the LDH/MDH superfamily.
CC {ECO:0000256|RuleBase:RU003369}.
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:KFI46733.1}.
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DR EMBL; JGYP01000001; KFI46733.1; -; Genomic_DNA.
DR RefSeq; WP_033520259.1; NZ_JGYP01000001.1.
DR AlphaFoldDB; A0A086ZJN3; -.
DR STRING; 1437606.BBOH_0205; -.
DR eggNOG; COG0039; Bacteria.
DR OrthoDB; 9802969at2; -.
DR Proteomes; UP000029096; 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:KFI46733.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000029096}.
FT DOMAIN 6..146
FT /note="Lactate/malate dehydrogenase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00056"
FT DOMAIN 149..312
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 11..16
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
FT BINDING 36
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 325 AA; 35078 MW; D7B73C5F695246A2 CRC64;
MALIRKIGIV GQGHVGAHVA NRLLETGIPD ELYLCDINER KLAAEVQDLT DTLSFYPHNC
AIVGVGDEYE KLAGCDVIVN AAGDVLSSAK SRDGELFVTT DIARTFVHRI TDAGFQGIWV
SIANPCDVIA TEIWRLSGYD PKRIIGSGTA LDSARLRNVI SQHTGIDQHS INAYMLGEHG
FSEFAAFSAV TFGGKSLDAL TAEQPERFGF DRADANDHAV HNGYIAMEGK HCTEYSVASA
ACRIVQAVVS NEHYVTACST LLTGEYGHSG LFASIPCVIG ANGVEQTLPF ALTDEEQKAF
DASCAHIAGN IERLGDWWRS ESRVK
//
