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L-lactate dehydrogenase A chain (LDH-A) (EC 1.1.1.27) (LDH muscle subunit) (LDH-M)

 LDHA_PIG                Reviewed;         332 AA.
P00339;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
25-OCT-2017, entry version 146.
RecName: Full=L-lactate dehydrogenase A chain;
Short=LDH-A;
EC=1.1.1.27;
AltName: Full=LDH muscle subunit;
Short=LDH-M;
Name=LDHA;
Sus scrofa (Pig).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Suina; Suidae;
Sus.
NCBI_TaxID=9823;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Muscle;
PubMed=7937776; DOI=10.1073/pnas.91.20.9392;
Tsuji S., Qureshi M.A., Hou E.W., Fitch W.M., Li S.S.-L.;
"Evolutionary relationships of lactate dehydrogenases (LDHs) from
mammals, birds, an amphibian, fish, barley, and bacteria: LDH cDNA
sequences from Xenopus, pig, and rat.";
Proc. Natl. Acad. Sci. U.S.A. 91:9392-9396(1994).
[2]
PROTEIN SEQUENCE OF 2-332, AND ACETYLATION AT ALA-2.
PubMed=838465; DOI=10.1515/bchm2.1977.358.1.123;
Kiltz H.-H., Keil W., Griesbach M., Petry K., Meyer H.;
"The primary structure of porcine lactate dehydrogenase: isoenzymes M4
and H4.";
Hoppe-Seyler's Z. Physiol. Chem. 358:123-127(1977).
[3]
X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEX WITH NAD AND
SUBSTRATE ANALOG.
PubMed=1678537; DOI=10.1098/rstb.1991.0047;
Dunn C.R., Wilks H.M., Halsall D.J., Atkinson T., Clarke A.R.,
Muirhead H., Holbrook J.J.;
"Design and synthesis of new enzymes based on the lactate
dehydrogenase framework.";
Philos. Trans. R. Soc. Lond., B, Biol. Sci. 332:177-184(1991).
-!- CATALYTIC ACTIVITY: (S)-lactate + NAD(+) = pyruvate + NADH.
-!- PATHWAY: Fermentation; pyruvate fermentation to lactate; (S)-
lactate from pyruvate: step 1/1.
-!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:1678537}.
-!- SUBCELLULAR LOCATION: Cytoplasm.
-!- PTM: ISGylated. {ECO:0000250}.
-!- SIMILARITY: Belongs to the LDH/MDH superfamily. LDH family.
{ECO:0000305}.
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EMBL; U07178; AAA50436.1; -; mRNA.
PIR; A00348; DEPGLM.
UniGene; Ssc.50275; -.
PDB; 9LDB; X-ray; 2.20 A; A/B=2-332.
PDB; 9LDT; X-ray; 2.00 A; A/B=2-332.
PDBsum; 9LDB; -.
PDBsum; 9LDT; -.
ProteinModelPortal; P00339; -.
SMR; P00339; -.
STRING; 9823.ENSSSCP00000014202; -.
iPTMnet; P00339; -.
PaxDb; P00339; -.
PeptideAtlas; P00339; -.
PRIDE; P00339; -.
Ensembl; ENSSSCT00000014597; ENSSSCP00000014202; ENSSSCG00000013366.
eggNOG; KOG1495; Eukaryota.
eggNOG; COG0039; LUCA.
GeneTree; ENSGT00550000074541; -.
HOGENOM; HOG000213793; -.
HOVERGEN; HBG000462; -.
InParanoid; P00339; -.
OMA; MDLMQTA; -.
OrthoDB; EOG091G0HME; -.
TreeFam; TF314963; -.
Reactome; R-SSC-70268; Pyruvate metabolism.
UniPathway; UPA00554; UER00611.
EvolutionaryTrace; P00339; -.
Proteomes; UP000008227; Chromosome 2.
Bgee; ENSSSCG00000013366; -.
Genevisible; P00339; SS.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0004459; F:L-lactate dehydrogenase activity; IEA:UniProtKB-EC.
GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
GO; GO:0019752; P:carboxylic acid metabolic process; IEA:InterPro.
Gene3D; 3.90.110.10; -; 1.
HAMAP; MF_00488; Lactate_dehydrog; 1.
InterPro; IPR001557; L-lactate/malate_DH.
InterPro; IPR011304; L-lactate_DH.
InterPro; IPR018177; L-lactate_DH_AS.
InterPro; IPR022383; Lactate/malate_DH_C.
InterPro; IPR001236; Lactate/malate_DH_N.
InterPro; IPR015955; Lactate_DH/Glyco_Ohase_4_C.
InterPro; IPR036291; NAD(P)-bd_dom_sf.
Pfam; PF02866; Ldh_1_C; 1.
Pfam; PF00056; Ldh_1_N; 1.
PIRSF; PIRSF000102; Lac_mal_DH; 1.
PRINTS; PR00086; LLDHDRGNASE.
SUPFAM; SSF51735; SSF51735; 1.
SUPFAM; SSF56327; SSF56327; 1.
TIGRFAMs; TIGR01771; L-LDH-NAD; 1.
PROSITE; PS00064; L_LDH; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Complete proteome; Cytoplasm;
Direct protein sequencing; Isopeptide bond; NAD; Oxidoreductase;
Phosphoprotein; Reference proteome; Ubl conjugation.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:838465}.
CHAIN 2 332 L-lactate dehydrogenase A chain.
/FTId=PRO_0000168416.
NP_BIND 29 57 NAD. {ECO:0000269|PubMed:1678537}.
ACT_SITE 193 193 Proton acceptor.
BINDING 99 99 NAD. {ECO:0000269|PubMed:1678537}.
BINDING 106 106 Substrate.
BINDING 138 138 NAD or substrate.
{ECO:0000269|PubMed:1678537}.
BINDING 169 169 Substrate.
BINDING 248 248 Substrate.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000269|PubMed:838465}.
MOD_RES 5 5 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P00338}.
MOD_RES 5 5 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:P06151}.
MOD_RES 14 14 N6-acetyllysine.
{ECO:0000250|UniProtKB:P00338}.
MOD_RES 57 57 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P00338}.
MOD_RES 81 81 N6-acetyllysine.
{ECO:0000250|UniProtKB:P00338}.
MOD_RES 118 118 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P00338}.
MOD_RES 118 118 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:P06151}.
MOD_RES 126 126 N6-acetyllysine.
{ECO:0000250|UniProtKB:P00338}.
MOD_RES 224 224 N6-acetyllysine.
{ECO:0000250|UniProtKB:P06151}.
MOD_RES 232 232 N6-acetyllysine.
{ECO:0000250|UniProtKB:P06151}.
MOD_RES 239 239 Phosphotyrosine.
{ECO:0000250|UniProtKB:P06151}.
MOD_RES 243 243 N6-acetyllysine.
{ECO:0000250|UniProtKB:P06151}.
MOD_RES 309 309 Phosphothreonine.
{ECO:0000250|UniProtKB:P04642}.
MOD_RES 318 318 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P00338}.
MOD_RES 318 318 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:P06151}.
MOD_RES 322 322 Phosphothreonine.
{ECO:0000250|UniProtKB:P04642}.
CROSSLNK 57 57 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate.
{ECO:0000250|UniProtKB:P00338}.
CONFLICT 233 233 Q -> E (in Ref. 2; AA sequence).
{ECO:0000305}.
CONFLICT 286 286 D -> N (in Ref. 2; AA sequence).
{ECO:0000305}.
HELIX 4 8 {ECO:0000244|PDB:9LDT}.
STRAND 20 26 {ECO:0000244|PDB:9LDT}.
HELIX 30 41 {ECO:0000244|PDB:9LDT}.
STRAND 46 51 {ECO:0000244|PDB:9LDT}.
HELIX 55 67 {ECO:0000244|PDB:9LDT}.
HELIX 68 71 {ECO:0000244|PDB:9LDT}.
STRAND 76 82 {ECO:0000244|PDB:9LDT}.
HELIX 83 86 {ECO:0000244|PDB:9LDT}.
STRAND 90 94 {ECO:0000244|PDB:9LDT}.
HELIX 106 109 {ECO:0000244|PDB:9LDT}.
HELIX 110 127 {ECO:0000244|PDB:9LDT}.
STRAND 132 135 {ECO:0000244|PDB:9LDT}.
STRAND 137 139 {ECO:0000244|PDB:9LDT}.
HELIX 140 151 {ECO:0000244|PDB:9LDT}.
STRAND 157 160 {ECO:0000244|PDB:9LDT}.
HELIX 164 178 {ECO:0000244|PDB:9LDT}.
HELIX 182 184 {ECO:0000244|PDB:9LDT}.
STRAND 189 191 {ECO:0000244|PDB:9LDT}.
HELIX 201 203 {ECO:0000244|PDB:9LDT}.
HELIX 211 214 {ECO:0000244|PDB:9LDT}.
STRAND 219 222 {ECO:0000244|PDB:9LDT}.
HELIX 228 245 {ECO:0000244|PDB:9LDT}.
HELIX 250 264 {ECO:0000244|PDB:9LDT}.
STRAND 269 276 {ECO:0000244|PDB:9LDT}.
TURN 278 280 {ECO:0000244|PDB:9LDT}.
STRAND 288 296 {ECO:0000244|PDB:9LDT}.
STRAND 299 303 {ECO:0000244|PDB:9LDT}.
HELIX 310 330 {ECO:0000244|PDB:9LDT}.
SEQUENCE 332 AA; 36619 MW; FD3B4673557C9B72 CRC64;
MATLKDQLIH NLLKEEHVPH NKITVVGVGA VGMACAISIL MKELADEIAL VDVMEDKLKG
EMMDLQHGSL FLRTPKIVSG KDYNVTANSR LVVITAGARQ QEGESRLNLV QRNVNIFKFI
IPNIVKYSPN CKLLVVSNPV DILTYVAWKI SGFPKNRVIG SGCNLDSARF RYLMGERLGV
HPLSCHGWIL GEHGDSSVPV WSGVNVAGVS LKNLHPELGT DADKEHWKAV HKQVVDSAYE
VIKLKGYTSW AIGLSVADLA ESIMKNLRRV HPISTMIKGL YGIKEDVFLS VPCILGQNGI
SDVVKVTLTP EEEAHLKKSA DTLWGIQKEL QF


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