LDHB_SCEWO
ID LDHB_SCEWO Reviewed; 333 AA.
AC P79913;
DT 16-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 111.
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 Sceloporus woodi (Florida scrub lizard).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Iguania; Phrynosomatidae; Phrynosomatinae; Sceloporus.
OX NCBI_TaxID=59726;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8666293; DOI=10.1016/0378-1119(96)00180-1;
RA Mannen H., Tsoi S.C.-M., Pickford D.B., Donald J.A., Guillette L.J.,
RA Li S.S.-L.;
RT "Sequences of the lizard cDNAs encoding lactate dehydrogenase (LDH)
RT isozymes A (muscle) and B (heart).";
RL Gene 171:303-304(1996).
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}.
CC -!- CAUTION: Was originally thought to originate from S.undulatus.
CC {ECO:0000305|PubMed:8666293}.
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DR EMBL; U28411; AAB53026.1; -; mRNA.
DR AlphaFoldDB; P79913; -.
DR SMR; P79913; -.
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_0000168472"
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; 36114 MW; F8E64CF57E225FF2 CRC64;
MASLKDKLIT PVAQPATQPT SKVTVVGVGQ VGMACAISVL EKGLCDELAL VDVLEDKLKG
EMMDLQHGSL FLKTNKIVAG KDYAVTANSK VVVVTAGVRQ QEGESRLDLV QRNVNVFKFI
IPQVVKYSPD CIILVVSNPV DILTYVTWKL SGLPKHRVIG SGCNLDSARF RFLMGERLGI
HPSSCHGWIL GEHGDSSVAV WSGVNVAGVS LQELNPAMGS DQDSEGWKQV HKQVVDSAYE
VIKLKGYTNW AIGLSVADLL ETIMKNLCRV HPVSTMVKGM YGIENEVFLS LPCVLGSVGL
TSVINQKLKD SEVAQLQTSA TTLWNVQKDL KDL
