ID   LDHB_ALLMI              Reviewed;         333 AA.
AC   Q9PW05;
DT   16-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 105.
DE   RecName: Full=L-lactate dehydrogenase B chain;
DE            Short=LDH-B;
DE            EC=1.1.1.27 {ECO:0000250|UniProtKB:P07195};
GN   Name=LDHB;
OS   Alligator mississippiensis (American alligator).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Crocodylia; Alligatoridae; Alligatorinae;
OC   Alligator.
OX   NCBI_TaxID=8496;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Oviduct;
RX   PubMed=9364765; DOI=10.1093/oxfordjournals.molbev.a025717;
RA   Mannen H., Tsoi S.C.-M., Krushkal J.S., Li W.-H., Li S.S.-L.;
RT   "The cDNA cloning and molecular evolution of reptile and pigeon lactate
RT   dehydrogenase isozymes.";
RL   Mol. Biol. Evol. 14:1081-1087(1997).
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. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the LDH/MDH superfamily. LDH family.
CC       {ECO:0000305}.
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DR   EMBL; L79952; AAD46978.1; -; mRNA.
DR   RefSeq; NP_001274216.1; NM_001287287.1.
DR   AlphaFoldDB; Q9PW05; -.
DR   SMR; Q9PW05; -.
DR   STRING; 8496.XP_006263862.1; -.
DR   GeneID; 102573484; -.
DR   KEGG; amj:102573484; -.
DR   CTD; 3945; -.
DR   eggNOG; KOG1495; Eukaryota.
DR   OrthoDB; 1204514at2759; -.
DR   UniPathway; UPA00554; UER00611.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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   2: Evidence at transcript level;
KW   Cytoplasm; NAD; Oxidoreductase.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..333
FT                   /note="L-lactate dehydrogenase B chain"
FT                   /id="PRO_0000168468"
FT   ACT_SITE        193
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         29..57
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         99
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         106
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         138
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         138
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         169
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         248
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   333 AA;  36665 MW;  4856FDBD386E58D0 CRC64;
     MSTLKEKLIT QIASERTIPN SKVTVVGVGQ VGMACAISIL GKRLGDELAL VDVWEDKLKG
     EMMDLQHGSL FLQTHKIVAD KDYAVTANSK IVVVTAGVRQ QEGESRLNLV QRNVNVFKFI
     IPQIIKYSPD CTILVVSNPV DILTYVTWKL SGLPKHRVIG SGCNLDSARF RYLMSEKLGI
     HPSSCHGWIL GEHGDSSVAV WSGVNVAGVS LQELNPAMGT DRDSEKWKEV HKQVVESAYE
     VIKLKGYTNW AIGLSVADLL ETMMKNLCRV HPVSTMVKGM YGIENEVFLS LPCVLSASGL
     TSVINQKLKD DEVAQLRSSA DTLWSIQKDL KDL