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Database: UniProt
Entry: A0A067N4F4_PLEOS
LinkDB: A0A067N4F4_PLEOS
Original site: A0A067N4F4_PLEOS 
ID   A0A067N4F4_PLEOS        Unreviewed;       323 AA.
AC   A0A067N4F4;
DT   03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT   03-SEP-2014, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   RecName: Full=L-lactate dehydrogenase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=PLEOSDRAFT_62446 {ECO:0000313|EMBL:KDQ22883.1};
OS   Pleurotus ostreatus PC15.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Pleurotineae; Pleurotaceae; Pleurotus.
OX   NCBI_TaxID=1137138 {ECO:0000313|EMBL:KDQ22883.1, ECO:0000313|Proteomes:UP000027073};
RN   [1] {ECO:0000313|Proteomes:UP000027073}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PC15 {ECO:0000313|Proteomes:UP000027073};
RX   PubMed=24958869; DOI=10.1073/pnas.1400592111;
RA   Riley R., Salamov A.A., Brown D.W., Nagy L.G., Floudas D., Held B.W.,
RA   Levasseur A., Lombard V., Morin E., Otillar R., Lindquist E.A., Sun H.,
RA   LaButti K.M., Schmutz J., Jabbour D., Luo H., Baker S.E., Pisabarro A.G.,
RA   Walton J.D., Blanchette R.A., Henrissat B., Martin F., Cullen D.,
RA   Hibbett D.S., Grigoriev I.V.;
RT   "Extensive sampling of basidiomycete genomes demonstrates inadequacy of the
RT   white-rot/brown-rot paradigm for wood decay fungi.";
RL   Proc. Natl. Acad. Sci. U.S.A. 111:9923-9928(2014).
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; KL198014; KDQ22883.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A067N4F4; -.
DR   STRING; 1137138.A0A067N4F4; -.
DR   VEuPathDB; FungiDB:PLEOSDRAFT_62446; -.
DR   HOGENOM; CLU_045401_1_2_1; -.
DR   InParanoid; A0A067N4F4; -.
DR   OrthoDB; 5344346at2759; -.
DR   Proteomes; UP000027073; 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; cd00300; LDH_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   NAD {ECO:0000256|PIRSR:PIRSR000102-3};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU003369};
KW   Reference proteome {ECO:0000313|Proteomes:UP000027073}.
FT   DOMAIN          16..158
FT                   /note="Lactate/malate dehydrogenase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00056"
FT   DOMAIN          161..320
FT                   /note="Lactate/malate dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02866"
FT   ACT_SITE        191
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-1"
FT   BINDING         21..26
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
FT   BINDING         46
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
FT   BINDING         111
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
FT   BINDING         134..136
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
SQ   SEQUENCE   323 AA;  34356 MW;  E551FE2EBD53F509 CRC64;
     MDPPAMDPNV LSSRSRIAIL GAGSVGSSIA LCLILNPVAS EVILVDPKVE LRDAQVKDLG
     DATTYHGAVG GGGVKIRSGT HKDAGQCDVI VISAGAKQRH GESRTDLLGR NLHILRSAIN
     DMKPFREDAV ILIVANPVDV LTYFARKFSG LPEGQVLGSG TFLDSARLRG ILAEKLDVDA
     GSVDGYVLGE HGETQMVAWS CVTIGAVPLE QCLLPNTVLD RKAIAKETRE KAGKIIQAKG
     ATAYGIGALT GSICKSILFD QRNVRPISHW IEEMECCLSL PVVLGRKGVL RTLRMPLNEE
     EQASLAESAS ALRGFISDAE KIP
//
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