ID   LDHBB_DANRE             Reviewed;         334 AA.
AC   Q6DGK2;
DT   30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   03-AUG-2022, entry version 128.
DE   RecName: Full=L-lactate dehydrogenase B-B chain {ECO:0000250|UniProtKB:P07195};
DE            Short=LDH-B-B {ECO:0000250|UniProtKB:P07195};
DE            EC=1.1.1.27;
GN   Name=ldhbb {ECO:0000312|ZFIN:ZDB-GENE-040718-176}; ORFNames=zgc:92882;
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955;
RN   [1] {ECO:0000312|EMBL:AAH76340.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain {ECO:0000312|EMBL:AAH76340.1};
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
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   -!- PATHWAY: Fermentation; pyruvate fermentation to lactate; (S)-lactate
CC       from pyruvate: step 1/1. {ECO:0000250|UniProtKB:P07195}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:P07195}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P07195}.
CC   -!- SIMILARITY: Belongs to the LDH/MDH superfamily. LDH family.
CC       {ECO:0000255}.
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DR   EMBL; BC076340; AAH76340.1; -; mRNA.
DR   RefSeq; NP_001002474.1; NM_001002474.1.
DR   RefSeq; XP_005170716.1; XM_005170659.2.
DR   AlphaFoldDB; Q6DGK2; -.
DR   SMR; Q6DGK2; -.
DR   STRING; 7955.ENSDARP00000106067; -.
DR   Ensembl; ENSDART00000104866; ENSDARP00000095636; ENSDARG00000071076.
DR   Ensembl; ENSDART00000181143; ENSDARP00000154861; ENSDARG00000071076.
DR   GeneID; 436747; -.
DR   KEGG; dre:436747; -.
DR   CTD; 436747; -.
DR   ZFIN; ZDB-GENE-040718-176; ldhbb.
DR   eggNOG; KOG1495; Eukaryota.
DR   GeneTree; ENSGT00940000153525; -.
DR   InParanoid; Q6DGK2; -.
DR   OMA; CYIIVLT; -.
DR   OrthoDB; 1204514at2759; -.
DR   PhylomeDB; Q6DGK2; -.
DR   UniPathway; UPA00554; UER00611.
DR   PRO; PR:Q6DGK2; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Chromosome 25.
DR   Bgee; ENSDARG00000071076; Expressed in liver and 18 other tissues.
DR   ExpressionAtlas; Q6DGK2; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004459; F:L-lactate dehydrogenase activity; IBA:GO_Central.
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   Cytoplasm; NAD; Oxidoreductase; 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-B chain"
FT                   /evidence="ECO:0000250|UniProtKB:P07195"
FT                   /id="PRO_0000401128"
FT   ACT_SITE        194
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:P07195"
FT   BINDING         30..58
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:P00341"
FT   BINDING         100
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:P07195"
FT   BINDING         107
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P07195"
FT   BINDING         139
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:P07195"
FT   BINDING         139
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P07195"
FT   BINDING         170
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P07195"
FT   BINDING         249
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P07195"
SQ   SEQUENCE   334 AA;  36710 MW;  86D014E974F98541 CRC64;
     MASVLQKLIT PLFSGPLEPP RNKVTVVGVG QVGMACAVSV LLRELADELA LVDVVEDKLK
     GEMMDLQHGS LFLKTPKIVS GKDYSVTANS RIVVVTAGVR QQEGESRLNL VQRNVNIFKH
     IIPQIVKYSP NCILIVVSNP VDVLTYVTWK LSGLPKHRVI GSGTNLDSAR FRYLMAERLG
     IHPSSFNGWI LGEHGDSSVP VWSGANVAGV SLQKLNPDIG KDTDRENWKE THKKVVDSAY
     EVIRLKGYTN WAIGLSVADL TESIMKNLNR VHPVSTMVKG MYGISDEVYL SLPCVLNSAG
     VGSVVNMTLT VDEVSQLKKS ADMLWHIQRD LRDL