LDHB_COLLI
ID LDHB_COLLI Reviewed; 333 AA.
AC Q9PW04;
DT 16-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 106.
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 testis subunit;
DE AltName: Full=LDH-C;
GN Name=LDHB;
OS Columba livia (Rock dove).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Columbiformes; Columbidae; Columba.
OX NCBI_TaxID=8932;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=White Carneau; TISSUE=Testis;
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; L79957; AAD46981.1; -; mRNA.
DR AlphaFoldDB; Q9PW04; -.
DR SMR; Q9PW04; -.
DR STRING; 8932.XP_005507114.1; -.
DR eggNOG; KOG1495; Eukaryota.
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_0000168467"
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; 36491 MW; 7F919CBCA204B131 CRC64;
MATVKEKLMT PLTAGIKVPN NKISIVGVGQ VGMASAISIL GKGLCDELAL VDVMEDRLKG
EMMDLQHGSL FPHTHKIVAD KDYAVTANSK IVVVTAGVRQ QEGESRLNLV QRNVNVFKFI
IPQIVKYSPN CTILVVSNPV DILTYVTWKL SGLPKHRVIG SGCNLDTARF RYLMSERLGI
HPDSCHGWIL GEHGDSSVAV WSGVNVAGVP LKELNPAMGT DKDSENWKEV HKQVVDSAYE
VIKLKGYTNW AIGLSVANLC ETILKDLYRV HSVSTLFKGM YGIENDVFLS LPSVLSAAGL
TSVINPKLKD DEVAQLKKSA ETLWNIQKDL QDL
