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LDHB_RABIT
ID   LDHB_RABIT              Reviewed;         217 AA.
AC   P13490;
DT   01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1990, sequence version 1.
DT   03-AUG-2022, entry version 127.
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;
DE   Flags: Fragment;
GN   Name=LDHB;
OS   Oryctolagus cuniculus (Rabbit).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX   NCBI_TaxID=9986;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=2917988; DOI=10.1016/s0021-9258(19)84964-5;
RA   Sass C., Briand M., Benslimane S., Renaud M., Briand Y.;
RT   "Characterization of rabbit lactate dehydrogenase-M and lactate
RT   dehydrogenase-H cDNAs. Control of lactate dehydrogenase expression in
RT   rabbit muscle.";
RL   J. Biol. Chem. 264:4076-4081(1989).
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; M22584; AAA31381.1; -; mRNA.
DR   PIR; B32957; B32957.
DR   AlphaFoldDB; P13490; -.
DR   SMR; P13490; -.
DR   STRING; 9986.ENSOCUP00000022069; -.
DR   ChEMBL; CHEMBL4523187; -.
DR   eggNOG; KOG1495; Eukaryota.
DR   InParanoid; P13490; -.
DR   SABIO-RK; P13490; -.
DR   UniPathway; UPA00554; UER00611.
DR   Proteomes; UP000001811; 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   InterPro; IPR001557; L-lactate/malate_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   PRINTS; PR00086; LLDHDRGNASE.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   SUPFAM; SSF56327; SSF56327; 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   CHAIN           <1..217
FT                   /note="L-lactate dehydrogenase B chain"
FT                   /id="PRO_0000168463"
FT   ACT_SITE        77
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10002"
FT   BINDING         22
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         22
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         53
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         132
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         123
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:P07195"
FT   MOD_RES         212
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P07195"
FT   NON_TER         1
SQ   SEQUENCE   217 AA;  24134 MW;  FBCC3144CA889058 CRC64;
     GKFIIPQIVK YSPNCIIIVV SNPVDILTYV TWKLSGLPKH RVIGSGCNLD SARFRYLMAE
     KLGIHPSSCH GWILGEHGDS RLAVWSGVNV AGVSLQELNP EMGTDNDSEN WKEVHKMVVE
     SAYEVIKLKG YTNWAIGLSV ADLIESMLKN LSRIHPVSTM VRGMYGIESE VFLSLPCILN
     ARGLTSVINQ KLKDDEVAQL KKSADTLWDI QKDLKDL
 
 
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