LDHB_PANTR
ID LDHB_PANTR Reviewed; 334 AA.
AC A5A6N7;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-2007, sequence version 1.
DT 03-AUG-2022, entry version 83.
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 Pan troglodytes (Chimpanzee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9598;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Skin;
RX PubMed=17574350; DOI=10.1016/j.gene.2007.04.013;
RA Sakate R., Suto Y., Imanishi T., Tanoue T., Hida M., Hayasaka I.,
RA Kusuda J., Gojobori T., Hashimoto K., Hirai M.;
RT "Mapping of chimpanzee full-length cDNAs onto the human genome unveils
RT large potential divergence of the transcriptome.";
RL Gene 399:1-10(2007).
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. Interacts with PTEN upstream reading frame
CC protein MP31; the interaction leads to inhibition of mitochondrial
CC lactate dehydrogenase activity, preventing conversion of lactate to
CC pyruvate in mitochondria. {ECO:0000250|UniProtKB:P07195}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Mitochondrion inner
CC membrane {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; AB222165; BAF62410.1; -; mRNA.
DR RefSeq; NP_001092031.1; NM_001098561.1.
DR AlphaFoldDB; A5A6N7; -.
DR SMR; A5A6N7; -.
DR STRING; 9598.ENSPTRP00000008129; -.
DR PaxDb; A5A6N7; -.
DR PRIDE; A5A6N7; -.
DR GeneID; 465337; -.
DR KEGG; ptr:465337; -.
DR CTD; 3945; -.
DR eggNOG; KOG1495; Eukaryota.
DR InParanoid; A5A6N7; -.
DR OrthoDB; 1204514at2759; -.
DR UniPathway; UPA00554; UER00611.
DR Proteomes; UP000002277; 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 2: Evidence at transcript level;
KW Acetylation; Cytoplasm; Membrane; Mitochondrion;
KW Mitochondrion inner membrane; NAD; Oxidoreductase; Phosphoprotein;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P07195"
FT CHAIN 2..334
FT /note="L-lactate dehydrogenase B chain"
FT /id="PRO_0000295286"
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:0000250|UniProtKB:P07195"
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"
SQ SEQUENCE 334 AA; 36653 MW; 1F350FE07AAE530B CRC64;
MATLKEKLIA PVAEEEATIP NNKITVVGVG QVGMACAISI LGKSLADELA LVDVLEDKLK
GEMMDLQHGS LFLQTPKIVA DKDYSVTANS KIVVVTAGVR QQEGESRLNL VQRNVNVFKF
IIPQIVKYSP DCIIIVVSNP VDILTYVTWK LSGLPKHRVI GSGCNLDSAR FRYLMAEKLG
IHPSSCHGWI LGEHGDSSVA VWSGVNVAGV SLQELNPEMG TDNDSENWKE VHKMVVESAY
EVIKLKGYTN WAIGLSVADL IESMLKNLSR IHPVSTMVKG MYGIENEVFL SLPCILNARG
LTSVINQKLK DDEVAQLKKS ADTLWDIQKD LKDL
