ID U6F932_LACHE Unreviewed; 304 AA.
AC U6F932;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE SubName: Full=L-2-hydroxyisocaproate dehydrogenase {ECO:0000313|EMBL:CDI59550.1};
DE EC=1.1.1.- {ECO:0000313|EMBL:CDI59550.1};
GN ORFNames=LHCIRMBIA104_01633 {ECO:0000313|EMBL:CDI59550.1};
OS Lactobacillus helveticus CIRM-BIA 104.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lactobacillus.
OX NCBI_TaxID=1226333 {ECO:0000313|EMBL:CDI59550.1, ECO:0000313|Proteomes:UP000017247};
RN [1] {ECO:0000313|EMBL:CDI59550.1, ECO:0000313|Proteomes:UP000017247}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CIRM-BIA 104 {ECO:0000313|EMBL:CDI59550.1,
RC ECO:0000313|Proteomes:UP000017247};
RA Valence F., Chuat V., Ma L., Creno S., Falentin H., Lortal S., Bizet C.,
RA Clermont D., Loux V., Bouchier C., Cousin S.;
RT "Draft Genome Sequence of five Lactobacillus helveticus strains CIRM-BIA
RT 101T, 103, 104, 951 and 953 isolated from milk product.";
RL Submitted (SEP-2013) 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:CDI59550.1}.
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DR EMBL; CBUL010000011; CDI59550.1; -; Genomic_DNA.
DR RefSeq; WP_003627090.1; NZ_HG530983.1.
DR AlphaFoldDB; U6F932; -.
DR GeneID; 83724939; -.
DR HOGENOM; CLU_045401_1_2_9; -.
DR Proteomes; UP000017247; 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 Coiled coil {ECO:0000256|SAM:Coils}; NAD {ECO:0000256|PIRSR:PIRSR000102-3};
KW Oxidoreductase {ECO:0000256|RuleBase:RU003369,
KW ECO:0000313|EMBL:CDI59550.1}.
FT DOMAIN 4..143
FT /note="Lactate/malate dehydrogenase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00056"
FT DOMAIN 146..303
FT /note="Lactate/malate dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02866"
FT COILED 277..304
FT /evidence="ECO:0000256|SAM:Coils"
FT ACT_SITE 176
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000102-1"
FT BINDING 8..13
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
FT BINDING 33
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
FT BINDING 96
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 304 AA; 33765 MW; 95C374058353095E CRC64;
MRTVGIIGMG HVGATVAYTL FTHGMVDDLI LIDKNEDKVN AEYNDLHDTL ARNDTYVNVR
KQDWDGLEDA DIIITAFGDI AASVKTGDRF GEFELNAKNA REVGADIKES GFHGVLINIS
NPCDAITQIL QETTGLKKNR VFGTGTFLDT ARVQRIIGEK LGQDPRNVEG FVLGEHGSSQ
FTAWSTIRVN NKIAFQLFGE EEQEKISEQS NKNSFIVANG KGYTSYAIAT CAVRLVKAVF
SDARLYCPVS VYNPEYKTYI GYPAIIGRDG IEEEIELKLT SEEKEKLETA ADKIKEHLDQ
LKKK
//
