LDHB_CHICK
ID LDHB_CHICK Reviewed; 333 AA.
AC P00337; O93362; Q548X0;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 157.
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 Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Broiler; TISSUE=Heart;
RA Tsoi S.C.-M., Li J.Y., Mannen H., Li S.S.-L.;
RT "Molecular evolution of vertebrate lactate dehydrogenase isozymes by gene
RT duplication.";
RL Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Testis;
RA Martinez-Arias W., Mezquita C., Mezquita J.;
RT "Expression of lactate dehydrogenases A and B during chicken
RT spermatogenesis: characterization of testis specific transcripts.";
RL Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PROTEIN SEQUENCE OF 2-333.
RA Torff H.-J., Becker D., Schwarzwalder J.;
RL (In) Sund H. (eds.);
RL Pyridine nucleotide dependent dehydrogenases, pp.31-42, Walter de Gruyter,
RL Berlin (1977).
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.
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; AF069771; AAC27617.1; -; mRNA.
DR EMBL; AF218799; AAG48560.1; -; mRNA.
DR PIR; A00346; DECHLH.
DR RefSeq; NP_989508.1; NM_204177.2.
DR PDB; 5K0Z; EM; 2.80 A; A/B/C/D=2-332.
DR PDBsum; 5K0Z; -.
DR AlphaFoldDB; P00337; -.
DR SMR; P00337; -.
DR BioGRID; 675043; 2.
DR IntAct; P00337; 1.
DR STRING; 9031.ENSGALP00000041792; -.
DR PaxDb; P00337; -.
DR Ensembl; ENSGALT00000052417; ENSGALP00000049441; ENSGALG00000035836.
DR GeneID; 373997; -.
DR KEGG; gga:373997; -.
DR CTD; 3945; -.
DR VEuPathDB; HostDB:geneid_373997; -.
DR eggNOG; KOG1495; Eukaryota.
DR GeneTree; ENSGT00940000153525; -.
DR HOGENOM; CLU_045401_0_2_1; -.
DR InParanoid; P00337; -.
DR OMA; AFTRHCT; -.
DR OrthoDB; 1204514at2759; -.
DR PhylomeDB; P00337; -.
DR TreeFam; TF314963; -.
DR Reactome; R-GGA-373920; Pyruvate metabolism.
DR Reactome; R-GGA-70268; Pyruvate metabolism.
DR SABIO-RK; P00337; -.
DR UniPathway; UPA00554; UER00611.
DR PRO; PR:P00337; -.
DR Proteomes; UP000000539; Chromosome 1.
DR Bgee; ENSGALG00000035836; Expressed in testis and 12 other tissues.
DR ExpressionAtlas; P00337; baseline and differential.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0045121; C:membrane raft; IEA:Ensembl.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:Ensembl.
DR GO; GO:1990204; C:oxidoreductase complex; IEA:Ensembl.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0004459; F:L-lactate dehydrogenase activity; IBA:GO_Central.
DR GO; GO:0006089; P:lactate metabolic process; IEA:Ensembl.
DR GO; GO:0006090; P:pyruvate metabolic process; IEA:Ensembl.
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 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Direct protein sequencing; NAD; Oxidoreductase;
KW Reference proteome.
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_0000168466"
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"
FT CONFLICT 132
FT /note="T -> V (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 213..215
FT /note="ELN -> QLD (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT HELIX 4..8
FT /evidence="ECO:0007829|PDB:5K0Z"
FT STRAND 9..11
FT /evidence="ECO:0007829|PDB:5K0Z"
FT STRAND 23..26
FT /evidence="ECO:0007829|PDB:5K0Z"
FT HELIX 32..41
FT /evidence="ECO:0007829|PDB:5K0Z"
FT STRAND 46..51
FT /evidence="ECO:0007829|PDB:5K0Z"
FT HELIX 56..66
FT /evidence="ECO:0007829|PDB:5K0Z"
FT HELIX 67..71
FT /evidence="ECO:0007829|PDB:5K0Z"
FT STRAND 76..79
FT /evidence="ECO:0007829|PDB:5K0Z"
FT TURN 83..88
FT /evidence="ECO:0007829|PDB:5K0Z"
FT STRAND 90..94
FT /evidence="ECO:0007829|PDB:5K0Z"
FT HELIX 110..127
FT /evidence="ECO:0007829|PDB:5K0Z"
FT STRAND 132..135
FT /evidence="ECO:0007829|PDB:5K0Z"
FT STRAND 137..139
FT /evidence="ECO:0007829|PDB:5K0Z"
FT HELIX 140..149
FT /evidence="ECO:0007829|PDB:5K0Z"
FT HELIX 155..157
FT /evidence="ECO:0007829|PDB:5K0Z"
FT STRAND 158..160
FT /evidence="ECO:0007829|PDB:5K0Z"
FT HELIX 164..176
FT /evidence="ECO:0007829|PDB:5K0Z"
FT TURN 177..179
FT /evidence="ECO:0007829|PDB:5K0Z"
FT TURN 182..184
FT /evidence="ECO:0007829|PDB:5K0Z"
FT STRAND 185..191
FT /evidence="ECO:0007829|PDB:5K0Z"
FT STRAND 197..206
FT /evidence="ECO:0007829|PDB:5K0Z"
FT HELIX 211..214
FT /evidence="ECO:0007829|PDB:5K0Z"
FT TURN 216..219
FT /evidence="ECO:0007829|PDB:5K0Z"
FT HELIX 228..245
FT /evidence="ECO:0007829|PDB:5K0Z"
FT HELIX 250..264
FT /evidence="ECO:0007829|PDB:5K0Z"
FT STRAND 269..276
FT /evidence="ECO:0007829|PDB:5K0Z"
FT STRAND 280..282
FT /evidence="ECO:0007829|PDB:5K0Z"
FT STRAND 288..295
FT /evidence="ECO:0007829|PDB:5K0Z"
FT STRAND 297..304
FT /evidence="ECO:0007829|PDB:5K0Z"
FT HELIX 310..327
FT /evidence="ECO:0007829|PDB:5K0Z"
SQ SEQUENCE 333 AA; 36318 MW; 184FB610B7EDA81B CRC64;
MATLKEKLIT PVAAGSTVPS NKITVVGVGQ VGMACAISIL GKGLCDELAL VDVLEDKLKG
EMMDLQHGSL FLQTHKIVAD KDYAVTANSK IVVVTAGVRQ QEGESRLNLV QRNVNVFKFI
IPQIVKYSPN CTILVVSNPV DILTYVTWKL SGLPKHRVIG SGCNLDTARF RYLMAERLGI
HPTSCHGWIL GEHGDSSVAV WSGVNVAGVS LQELNPAMGT DKDSENWKEV HKQVVESAYE
VIRLKGYTNW AIGLSVAELC ETMLKNLYRV HSVSTLVKGT YGIENDVFLS LPCVLSASGL
TSVINQKLKD DEVAQLKKSA DTLWSIQKDL KDL
