LDHA_CHICK
ID LDHA_CHICK Reviewed; 332 AA.
AC P00340;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=L-lactate dehydrogenase A chain;
DE Short=LDH-A;
DE EC=1.1.1.27 {ECO:0000250|UniProtKB:P00338};
GN Name=LDHA;
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].
RX PubMed=2243792; DOI=10.1093/nar/18.21.6432;
RA Hirota Y., Katsumata A., Takeya T.;
RT "Nucleotide and deduced amino acid sequences of chicken lactate
RT dehydrogenase-A.";
RL Nucleic Acids Res. 18:6432-6432(1990).
RN [2]
RP PROTEIN SEQUENCE OF 2-332.
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:P00338}.
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:P00338};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23445;
CC Evidence={ECO:0000250|UniProtKB:P00338};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:23446;
CC Evidence={ECO:0000250|UniProtKB:P00338};
CC -!- PATHWAY: Fermentation; pyruvate fermentation to lactate; (S)-lactate
CC from pyruvate: step 1/1. {ECO:0000250|UniProtKB:P00338}.
CC -!- SUBUNIT: Homotetramer.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the LDH/MDH superfamily. LDH family.
CC {ECO:0000305}.
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DR EMBL; X53828; CAA37824.1; -; mRNA.
DR PIR; A00349; DECHLM.
DR PIR; S12151; S12151.
DR RefSeq; NP_990615.1; NM_205284.1.
DR AlphaFoldDB; P00340; -.
DR SMR; P00340; -.
DR BioGRID; 676481; 2.
DR IntAct; P00340; 1.
DR STRING; 9031.ENSGALP00000038626; -.
DR iPTMnet; P00340; -.
DR PaxDb; P00340; -.
DR GeneID; 396221; -.
DR KEGG; gga:396221; -.
DR CTD; 3939; -.
DR VEuPathDB; HostDB:geneid_396221; -.
DR eggNOG; KOG1495; Eukaryota.
DR InParanoid; P00340; -.
DR OrthoDB; 1204514at2759; -.
DR PhylomeDB; P00340; -.
DR Reactome; R-GGA-373920; Pyruvate metabolism.
DR SABIO-RK; P00340; -.
DR UniPathway; UPA00554; UER00611.
DR PRO; PR:P00340; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
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 1: Evidence at protein level;
KW Cytoplasm; Direct protein sequencing; NAD; Oxidoreductase;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.2"
FT CHAIN 2..332
FT /note="L-lactate dehydrogenase A chain"
FT /id="PRO_0000168420"
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 63
FT /note="L -> M (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 78
FT /note="I -> T (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 192
FT /note="E -> Q (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 332 AA; 36514 MW; 5ED8279CFAD7B62B CRC64;
MSLKDHLIHN VHKEEHAHAH NKISVVGVGA VGMACAISIL MKDLADELTL VDVVEDKLKG
EMLDLQHGSL FLKTPKIISG KDYSVTAHSK LVIVTAGARQ QEGESRLNLV QRNVNIFKFI
IPNVVKYSPD CKLLIVSNPV DILTYVAWKI SGFPKHRVIG SGCNLDSARF RHLMGERLGI
HPLSCHGWIV GEHGDSSVPV WSGVNVAGVS LKALHPDMGT DADKEHWKEV HKQVVDSAYE
VIKLKGYTSW AIGLSVADLA ETIMKNLRRV HPISTAVKGM HGIKDDVFLS VPCVLGSSGI
TDVVKMILKP DEEEKIKKSA DTLWGIQKEL QF
