ID L5NL42_9EURY Unreviewed; 320 AA.
AC L5NL42;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE RecName: Full=L-lactate dehydrogenase {ECO:0000256|ARBA:ARBA00012967};
DE EC=1.1.1.27 {ECO:0000256|ARBA:ARBA00012967};
GN ORFNames=D320_16340 {ECO:0000313|EMBL:ELK50808.1};
OS Haloferax sp. BAB-2207.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Haloferacaceae; Haloferax.
OX NCBI_TaxID=1296625 {ECO:0000313|EMBL:ELK50808.1, ECO:0000313|Proteomes:UP000010764};
RN [1] {ECO:0000313|EMBL:ELK50808.1, ECO:0000313|Proteomes:UP000010764}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BAB2207 {ECO:0000313|EMBL:ELK50808.1,
RC ECO:0000313|Proteomes:UP000010764};
RA Joshi M.N., Sharma A.C., Pandit A.S., Pandya R.V., Desai S.M.,
RA Jasmani F.P., Pandey A., Saxena A.K., Bagatharia S.B.;
RT "Whole genome sequencing of Haloferax sp. BAB-2207.";
RL Submitted (DEC-2012) to the EMBL/GenBank/DDBJ databases.
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};
CC -!- PATHWAY: Fermentation; pyruvate fermentation to lactate; (S)-lactate
CC from pyruvate: step 1/1. {ECO:0000256|ARBA:ARBA00004843}.
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:ELK50808.1}.
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DR EMBL; ANPG01000431; ELK50808.1; -; Genomic_DNA.
DR RefSeq; WP_004065537.1; NZ_ANPG01000431.1.
DR AlphaFoldDB; L5NL42; -.
DR GeneID; 79189746; -.
DR PATRIC; fig|1243180.4.peg.2861; -.
DR UniPathway; UPA00554; UER00611.
DR Proteomes; UP000010764; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
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 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:SF16; 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 NAD {ECO:0000256|PIRSR:PIRSR000102-3};
KW Oxidoreductase {ECO:0000256|RuleBase:RU003369}.
FT DOMAIN 10..148
FT /note="Lactate/malate dehydrogenase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00056"
FT DOMAIN 151..315
FT /note="Lactate/malate dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02866"
FT ACT_SITE 181
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000102-1"
FT BINDING 14..20
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
FT BINDING 40
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
FT BINDING 100
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
FT BINDING 124..126
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
SQ SEQUENCE 320 AA; 34600 MW; 4991A04DED202498 CRC64;
MSTERGKGTV AVVGGAGAVG SSTAFALMES SLVGEIILVD IAEERVEGEA MDLNHGAYFT
SPVRVRTGDY EDCWDADVVI VTAGASQKPD ETRLDLMERN ADIFADMIPQ ITEGLNDDAV
MLIVTNPVDV LSYVTWKVSD LPAERVIGSG TVLDTSRFRH SLSREFDLDP ANVHAYVVGE
HGDSEVLVWS SANLGGIPFE SYATSHGVDD IDALKARVEE EVREAAYEII ERKERTNYGV
ARSVAATTER ILGGDNSILT VSTLVSGEHG IDDVYMSLPC TVNQSGVRDV HEFDLSESET
AALRESAGVI RESIDRLDLE
//
