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LDHA_HORVU
ID   LDHA_HORVU              Reviewed;         356 AA.
AC   P22988;
DT   01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1991, sequence version 1.
DT   03-AUG-2022, entry version 120.
DE   RecName: Full=L-lactate dehydrogenase A;
DE            Short=LDH-A;
DE            EC=1.1.1.27;
OS   Hordeum vulgare (Barley).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Pooideae; Triticodae; Triticeae; Hordeinae; Hordeum.
OX   NCBI_TaxID=4513;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC   STRAIN=cv. Himalaya; TISSUE=Root;
RX   PubMed=1698294; DOI=10.1073/pnas.87.18.7300;
RA   Hondred D., Hanson A.D.;
RT   "Hypoxically inducible barley lactate dehydrogenase: cDNA cloning and
RT   molecular analysis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 87:7300-7304(1990).
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   -!- PATHWAY: Fermentation; pyruvate fermentation to lactate; (S)-lactate
CC       from pyruvate: step 1/1.
CC   -!- SUBUNIT: Tetramer that arise from random association of LDH-A and LDH-
CC       B.
CC   -!- INDUCTION: By hypoxia.
CC   -!- SIMILARITY: Belongs to the LDH/MDH superfamily. LDH family.
CC       {ECO:0000305}.
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DR   EMBL; M55685; AAA62696.1; -; mRNA.
DR   PIR; A36070; A36070.
DR   AlphaFoldDB; P22988; -.
DR   SMR; P22988; -.
DR   UniPathway; UPA00554; UER00611.
DR   ExpressionAtlas; P22988; baseline and differential.
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; -; 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   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; SSF51735; SSF51735; 1.
DR   SUPFAM; SSF56327; SSF56327; 1.
DR   TIGRFAMs; TIGR01771; L-LDH-NAD; 1.
DR   PROSITE; PS00064; L_LDH; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; NAD; Oxidoreductase; Stress response.
FT   CHAIN           1..356
FT                   /note="L-lactate dehydrogenase A"
FT                   /id="PRO_0000168489"
FT   ACT_SITE        215
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         75..80
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         121
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         128
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         160
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         160
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         191
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         270
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   356 AA;  37749 MW;  7B82D6F1D0BF5AD8 CRC64;
     MHKASSLSEL GFDAGGASSG FFRPVADGCP ATPTSSAVPH RRLTKISVIG AGNVGMAIAQ
     TILTQNLADE IALVDALPDK LRGEALDLQH AAAFLPRVRI SGTDAAVTKN SDLVIVTAGA
     RQIPGETRLN LLQRNVALYR KIVPPVAEHS PDALLLVVSN PVDVLTYVAW KLSGFPASRV
     IGSGTNLDSS RFRFLIAEHL DVNAQDVQAY MVGEHGDSSV AIWSSISVGG MPAFKSLRDS
     HRSFDEAALE GIRRAVVGGA YEVIGLKGYT SWAIGYSVAS LAASLLRDQR RVHPVSVLAS
     GFHGISDGHE VFLSLPARLG RGGILGVAEM DLTEAEAAQL RRSAKTLWEN CQLLDL
 
 
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