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Database: UniProt
Entry: A0A059CH86_EUCGR
LinkDB: A0A059CH86_EUCGR
Original site: A0A059CH86_EUCGR 
ID   A0A059CH86_EUCGR        Unreviewed;       351 AA.
AC   A0A059CH86;
DT   09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT   09-JUL-2014, sequence version 1.
DT   27-MAR-2024, entry version 51.
DE   RecName: Full=L-lactate dehydrogenase {ECO:0000256|ARBA:ARBA00012967, ECO:0000256|RuleBase:RU000496};
DE            EC=1.1.1.27 {ECO:0000256|ARBA:ARBA00012967, ECO:0000256|RuleBase:RU000496};
GN   ORFNames=EUGRSUZ_D02046 {ECO:0000313|EMBL:KCW77752.1};
OS   Eucalyptus grandis (Flooded gum).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Myrtales; Myrtaceae; Myrtoideae; Eucalypteae; Eucalyptus.
OX   NCBI_TaxID=71139 {ECO:0000313|EMBL:KCW77752.1};
RN   [1] {ECO:0000313|EMBL:KCW77752.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Leaf extractions {ECO:0000313|EMBL:KCW77752.1};
RA   Schmutz J., Hayes R., Myburg A., Tuskan G., Grattapaglia D., Rokhsar D.S.;
RT   "The genome of Eucalyptus grandis.";
RL   Submitted (JUL-2013) 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         ECO:0000256|RuleBase:RU000496};
CC   -!- PATHWAY: Fermentation; pyruvate fermentation to lactate; (S)-lactate
CC       from pyruvate: step 1/1. {ECO:0000256|ARBA:ARBA00004843,
CC       ECO:0000256|RuleBase:RU000496}.
CC   -!- SIMILARITY: Belongs to the LDH/MDH superfamily. LDH family.
CC       {ECO:0000256|ARBA:ARBA00006054}.
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DR   EMBL; KK198756; KCW77752.1; -; Genomic_DNA.
DR   RefSeq; XP_010053454.1; XM_010055152.2.
DR   AlphaFoldDB; A0A059CH86; -.
DR   STRING; 71139.A0A059CH86; -.
DR   EnsemblPlants; KCW77752; KCW77752; EUGRSUZ_D02046.
DR   GeneID; 104441897; -.
DR   Gramene; KCW77752; KCW77752; EUGRSUZ_D02046.
DR   KEGG; egr:104441897; -.
DR   eggNOG; KOG1495; Eukaryota.
DR   InParanoid; A0A059CH86; -.
DR   OMA; VDELVIC; -.
DR   OrthoDB; 5344346at2759; -.
DR   UniPathway; UPA00554; UER00611.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0004459; F:L-lactate dehydrogenase activity; IBA:GO_Central.
DR   GO; GO:0006089; P:lactate metabolic process; IBA:GO_Central.
DR   GO; GO:0006090; P:pyruvate metabolic process; IBA:GO_Central.
DR   CDD; cd05293; LDH_1; 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   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, ECO:0000256|RuleBase:RU000496};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000496}.
FT   DOMAIN          39..178
FT                   /note="Lactate/malate dehydrogenase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00056"
FT   DOMAIN          181..344
FT                   /note="Lactate/malate dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02866"
FT   ACT_SITE        211
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-1"
FT   BINDING         44..49
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
FT   BINDING         69
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
FT   BINDING         131
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
FT   BINDING         154..156
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
SQ   SEQUENCE   351 AA;  37972 MW;  C1C2574868E94CE5 CRC64;
     MHKTYSASSL GPDGLDLSQA FFRPIHNTAP PSQTNRHAKI TVVGAGNVGM AIAQTVLTQD
     LVDEIALVDP MADKLRGEML DLQHAAAFLP RTTILSSSSD YAVTSGSDLI VVTAGARQNP
     GESRLNLLQR NVALFRSIIP ELAKHSPDAI LMVVSNPVDI LTYVAWKISG FPPNRVIGSG
     TNLDTSRFRF LLADHLEVNA QDVQAYVVGE HGDSSVALWS SISVGGVPIL SFLERQQIPY
     EEEMLENIHK TVVEGAYEVI NLKGYTSWAI GYSVASLART LLRDQRRIHP VSVLARGFYG
     IEGGDVFLSL PAQLGHGGVV GVTNVHLTDE EMQKLRASAE TLLELQSQLG I
//
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