LDHB_HORVU
ID LDHB_HORVU Reviewed; 344 AA.
AC P22989;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1991, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=L-lactate dehydrogenase B;
DE Short=LDH-B;
DE EC=1.1.1.27;
DE Flags: Fragment;
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; M55684; AAA62697.1; -; mRNA.
DR PIR; B36070; B36070.
DR AlphaFoldDB; P22989; -.
DR SMR; P22989; -.
DR UniPathway; UPA00554; UER00611.
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..344
FT /note="L-lactate dehydrogenase B"
FT /id="PRO_0000168490"
FT ACT_SITE 203
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 62..67
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 109
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 116
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 148
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 148
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 179
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 258
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT NON_TER 1
SQ SEQUENCE 344 AA; 36430 MW; 21F9BFDA80C8B251 CRC64;
AGDASSGFFR AVADGCPITH TSCSAPHRRL TKVSVIGAGN VGMAIAQTIL TQNLADEIAL
VDALPDKLRG EALDLQHAAA FLPRVRIVSG TDAAVTKNSD LIVVTAGARQ IPGETRLNLL
QRNVALYRKI VPPVAEHSPD ALLLVVSNPV DVLTYVAWKL SGFPASRVIG SGTNLDSSRF
RFLVAEHLDV SAQDVQAYMV GEHGDSSVAI WSSISVGGMP ALKSLRDSHR SFDEAALEGI
RRAVVGGAYE VIGLKGYTSW AIGYSVASLA TSLLRDQRRV HPVSVLAAGF HGISDGHEVF
LSLPARLGRA GVLGVAEMDL TEAEAAQLRR SAKTLWENCQ LLGL
