LDHB_PIG
ID LDHB_PIG Reviewed; 334 AA.
AC P00336;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=L-lactate dehydrogenase B chain;
DE Short=LDH-B;
DE EC=1.1.1.27 {ECO:0000250|UniProtKB:P07195};
DE AltName: Full=LDH heart subunit;
DE Short=LDH-H;
GN Name=LDHB;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Muscle;
RX PubMed=7937776; DOI=10.1073/pnas.91.20.9392;
RA Tsuji S., Qureshi M.A., Hou E.W., Fitch W.M., Li S.S.-L.;
RT "Evolutionary relationships of lactate dehydrogenases (LDHs) from mammals,
RT birds, an amphibian, fish, barley, and bacteria: LDH cDNA sequences from
RT Xenopus, pig, and rat.";
RL Proc. Natl. Acad. Sci. U.S.A. 91:9392-9396(1994).
RN [2]
RP PROTEIN SEQUENCE OF 2-334, AND ACETYLATION AT ALA-2.
RX PubMed=838465; DOI=10.1515/bchm2.1977.358.1.123;
RA Kiltz H.-H., Keil W., Griesbach M., Petry K., Meyer H.;
RT "The primary structure of porcine lactate dehydrogenase: isoenzymes M4 and
RT H4.";
RL Hoppe-Seyler's Z. Physiol. Chem. 358:123-127(1977).
RN [3]
RP SEQUENCE REVISION TO 22; 148; 216 AND 218.
RA Kiltz H.-H.;
RL Submitted (OCT-1977) to the PIR data bank.
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS).
RX PubMed=7338899; DOI=10.1016/0022-2836(81)90516-7;
RA Grau U.M., Trommer W.E., Rossmann M.G.;
RT "Structure of the active ternary complex of pig heart lactate dehydrogenase
RT with S-lac-NAD at 2.7-A resolution.";
RL J. Mol. Biol. 151:289-307(1981).
CC -!- FUNCTION: Interconverts simultaneously and stereospecifically pyruvate
CC and lactate with concomitant interconversion of NADH and NAD(+).
CC {ECO:0000250|UniProtKB:P07195}.
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:0000250|UniProtKB:P07195};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23445;
CC Evidence={ECO:0000250|UniProtKB:P07195};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:23446;
CC Evidence={ECO:0000250|UniProtKB:P07195};
CC -!- PATHWAY: Fermentation; pyruvate fermentation to lactate; (S)-lactate
CC from pyruvate: step 1/1. {ECO:0000250|UniProtKB:P07195}.
CC -!- SUBUNIT: Homotetramer (PubMed:7338899). Interacts with PTEN upstream
CC reading frame protein MP31; the interaction leads to inhibition of
CC mitochondrial lactate dehydrogenase activity, preventing conversion of
CC lactate to pyruvate in mitochondria (By similarity).
CC {ECO:0000250|UniProtKB:P07195, ECO:0000269|PubMed:7338899}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Mitochondrion inner membrane
CC {ECO:0000250|UniProtKB:P07195}; Peripheral membrane protein
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the LDH/MDH superfamily. LDH family.
CC {ECO:0000305}.
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DR EMBL; U07180; AAA50438.1; -; mRNA.
DR PIR; A91671; DEPGLH.
DR RefSeq; NP_001106758.1; NM_001113287.1.
DR PDB; 5LDH; X-ray; 2.70 A; A/B=2-334.
DR PDB; 5YTA; X-ray; 2.10 A; A/B=2-333.
DR PDB; 6CEP; X-ray; 2.00 A; A/B/C/D=1-334.
DR PDBsum; 5LDH; -.
DR PDBsum; 5YTA; -.
DR PDBsum; 6CEP; -.
DR AlphaFoldDB; P00336; -.
DR SMR; P00336; -.
DR CORUM; P00336; -.
DR STRING; 9823.ENSSSCP00000024847; -.
DR BindingDB; P00336; -.
DR ChEMBL; CHEMBL3823; -.
DR iPTMnet; P00336; -.
DR PaxDb; P00336; -.
DR PeptideAtlas; P00336; -.
DR PRIDE; P00336; -.
DR GeneID; 100621540; -.
DR KEGG; ssc:100621540; -.
DR CTD; 3945; -.
DR eggNOG; KOG1495; Eukaryota.
DR InParanoid; P00336; -.
DR OrthoDB; 1204514at2759; -.
DR BRENDA; 1.1.1.27; 6170.
DR SABIO-RK; P00336; -.
DR UniPathway; UPA00554; UER00611.
DR EvolutionaryTrace; P00336; -.
DR PRO; PR:P00336; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR GO; GO:0005743; C:mitochondrial inner membrane; ISS:UniProtKB.
DR GO; GO:0004459; F:L-lactate dehydrogenase activity; ISS:UniProtKB.
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 3D-structure; Acetylation; Cytoplasm; Direct protein sequencing; Membrane;
KW Mitochondrion; Mitochondrion inner membrane; NAD; Oxidoreductase;
KW Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:838465"
FT CHAIN 2..334
FT /note="L-lactate dehydrogenase B chain"
FT /id="PRO_0000168462"
FT ACT_SITE 194
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 30..58
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 100
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 107
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 139
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 139
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 170
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 249
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|PubMed:838465"
FT MOD_RES 7
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P07195"
FT MOD_RES 44
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P07195"
FT MOD_RES 58
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P07195"
FT MOD_RES 119
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P07195"
FT MOD_RES 240
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P07195"
FT MOD_RES 329
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P07195"
FT CONFLICT 14..15
FT /note="EE -> QQ (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 81
FT /note="D -> N (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 131
FT /note="D -> N (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 214
FT /note="E -> Q (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT HELIX 4..8
FT /evidence="ECO:0007829|PDB:6CEP"
FT STRAND 9..13
FT /evidence="ECO:0007829|PDB:6CEP"
FT STRAND 24..27
FT /evidence="ECO:0007829|PDB:6CEP"
FT HELIX 31..42
FT /evidence="ECO:0007829|PDB:6CEP"
FT STRAND 47..52
FT /evidence="ECO:0007829|PDB:6CEP"
FT HELIX 56..67
FT /evidence="ECO:0007829|PDB:6CEP"
FT HELIX 68..72
FT /evidence="ECO:0007829|PDB:6CEP"
FT STRAND 76..80
FT /evidence="ECO:0007829|PDB:6CEP"
FT HELIX 84..87
FT /evidence="ECO:0007829|PDB:6CEP"
FT STRAND 91..95
FT /evidence="ECO:0007829|PDB:6CEP"
FT STRAND 103..106
FT /evidence="ECO:0007829|PDB:5LDH"
FT HELIX 107..110
FT /evidence="ECO:0007829|PDB:6CEP"
FT HELIX 111..128
FT /evidence="ECO:0007829|PDB:6CEP"
FT STRAND 133..136
FT /evidence="ECO:0007829|PDB:6CEP"
FT STRAND 138..140
FT /evidence="ECO:0007829|PDB:6CEP"
FT HELIX 141..152
FT /evidence="ECO:0007829|PDB:6CEP"
FT HELIX 156..158
FT /evidence="ECO:0007829|PDB:6CEP"
FT STRAND 159..161
FT /evidence="ECO:0007829|PDB:6CEP"
FT HELIX 165..179
FT /evidence="ECO:0007829|PDB:6CEP"
FT HELIX 183..185
FT /evidence="ECO:0007829|PDB:6CEP"
FT STRAND 190..192
FT /evidence="ECO:0007829|PDB:6CEP"
FT HELIX 202..204
FT /evidence="ECO:0007829|PDB:6CEP"
FT STRAND 208..211
FT /evidence="ECO:0007829|PDB:5LDH"
FT HELIX 212..215
FT /evidence="ECO:0007829|PDB:6CEP"
FT TURN 217..220
FT /evidence="ECO:0007829|PDB:6CEP"
FT STRAND 221..223
FT /evidence="ECO:0007829|PDB:6CEP"
FT HELIX 228..246
FT /evidence="ECO:0007829|PDB:6CEP"
FT HELIX 251..265
FT /evidence="ECO:0007829|PDB:6CEP"
FT STRAND 270..277
FT /evidence="ECO:0007829|PDB:6CEP"
FT STRAND 280..282
FT /evidence="ECO:0007829|PDB:5LDH"
FT STRAND 285..287
FT /evidence="ECO:0007829|PDB:5LDH"
FT STRAND 289..297
FT /evidence="ECO:0007829|PDB:6CEP"
FT STRAND 300..305
FT /evidence="ECO:0007829|PDB:6CEP"
FT HELIX 311..329
FT /evidence="ECO:0007829|PDB:6CEP"
SQ SEQUENCE 334 AA; 36612 MW; A0A2389BAB8FFD73 CRC64;
MATLKEKLIA PVAEEETTIP NNKITVVGVG QVGMACAISI LGKSLTDELA LVDVLEDKLK
GEMMDLQHGS LFLQTPKIVA DKDYSVTANS KIVVVTAGVR QQEGESRLNL VQRNVNVFKF
IIPQIVKYSP DCIIIVVSNP VDILTYVTWK LSGLPKHRVI GSGCNLDSAR FRYLMAEKLG
VHPSSCHGWI LGEHGDSSVA VWSGVNVAGV SLQELNPEMG TDNDSENWKE VHKMVVESAY
EVIKLKGYTN WAIGLSVADL IESMLKNLSR IHPVSTMVQG MYGIENEVFL SLPCVLNARG
LTSVINQKLK DDEVAQLKNS ADTLWGIQKD LKDL
