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Database: UniProt
Entry: A0A0G4GKF7_VITBC
LinkDB: A0A0G4GKF7_VITBC
Original site: A0A0G4GKF7_VITBC 
ID   A0A0G4GKF7_VITBC        Unreviewed;       317 AA.
AC   A0A0G4GKF7;
DT   16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT   16-SEP-2015, sequence version 1.
DT   24-JAN-2024, entry version 35.
DE   RecName: Full=L-lactate dehydrogenase {ECO:0000256|ARBA:ARBA00016495};
GN   ORFNames=Vbra_18101 {ECO:0000313|EMBL:CEM30509.1};
OS   Vitrella brassicaformis (strain CCMP3155).
OC   Eukaryota; Sar; Alveolata; Colpodellida; Vitrellaceae; Vitrella.
OX   NCBI_TaxID=1169540 {ECO:0000313|EMBL:CEM30509.1, ECO:0000313|Proteomes:UP000041254};
RN   [1] {ECO:0000313|EMBL:CEM30509.1, ECO:0000313|Proteomes:UP000041254}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Zhu J., Qi W., Song R.;
RL   Submitted (NOV-2014) 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   -!- SIMILARITY: Belongs to the LDH/MDH superfamily.
CC       {ECO:0000256|RuleBase:RU003369}.
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DR   EMBL; CDMY01000698; CEM30509.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G4GKF7; -.
DR   STRING; 1169540.A0A0G4GKF7; -.
DR   VEuPathDB; CryptoDB:Vbra_18101; -.
DR   InParanoid; A0A0G4GKF7; -.
DR   OMA; IVSHYDD; -.
DR   OrthoDB; 5059897at2759; -.
DR   PhylomeDB; A0A0G4GKF7; -.
DR   Proteomes; UP000041254; 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; cd01339; LDH-like_MDH; 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_00487; Malate_dehydrog_3; 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; IPR011275; Malate_DH_type3.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   NCBIfam; TIGR01763; MalateDH_bact; 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.
PE   3: Inferred from homology;
KW   NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|PIRSR:PIRSR000102-3};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU003369};
KW   Reference proteome {ECO:0000313|Proteomes:UP000041254}.
FT   DOMAIN          5..143
FT                   /note="Lactate/malate dehydrogenase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00056"
FT   DOMAIN          148..307
FT                   /note="Lactate/malate dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02866"
FT   ACT_SITE        176
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-1"
FT   BINDING         10..15
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
FT   BINDING         34
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
FT   BINDING         83
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-2"
FT   BINDING         89
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-2"
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"
FT   BINDING         121
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-2"
FT   BINDING         152
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-2"
SQ   SEQUENCE   317 AA;  33963 MW;  75DDC90B44867335 CRC64;
     MPRPKIALVG SGAIGATLAH ISGIKELGDV VLFDIVEGMP QGKALDLSQL SPVEGFDTKY
     TGTQDYSAMK DADVVIVTAG VPRKPGMSRD DLLAINAKII REVATNIKTF CPNAFVICIT
     NPLDAMVQLL QSASGLPTNK VCGMAGVLDA SRFRYFIAEK LNVSVEDVSA LVMGGHGDTM
     VPLVRYTTVA GIPLPDLVSM GWLTQEDIDK LVERTRFGGG EIVQLLKTGS AFYAPAASAI
     AMAESYLRDK KRLLPCAAYL TGQYGVNGFY CGVPCIIGKD GVEKVVELKL TAEEDKMFRQ
     SVESVRQLVE ATPNARL
//
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