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

 LDHA_MACFA              Reviewed;         332 AA.
Q9BE24; Q4R5M9; Q60HF1;
16-NOV-2001, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 4.
25-OCT-2017, entry version 102.
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; ORFNames=QccE-13024, QccE-13248, QflA-14835;
Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Cercopithecidae; Cercopithecinae; Macaca.
NCBI_TaxID=9541;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Frontal cortex;
Osada N., Hida M., Kusuda J., Tanuma R., Iseki K., Hirai M., Terao K.,
Suzuki Y., Sugano S., Hashimoto K.;
"Isolation of full-length cDNA clones from macaque brain cDNA
libraries.";
Submitted (APR-2001) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain cortex;
Kusuda J., Osada N., Tanuma R., Hirata M., Sugano S., Hashimoto K.;
"Isolation and characterization of cDNA for macaque neurological
disease genes.";
Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain cortex;
International consortium for macaque cDNA sequencing and analysis;
"DNA sequences of macaque genes expressed in brain or testis and its
evolutionary implications.";
Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
-!- CATALYTIC ACTIVITY: (S)-lactate + NAD(+) = pyruvate + NADH.
-!- PATHWAY: Fermentation; pyruvate fermentation to lactate; (S)-
lactate from pyruvate: step 1/1.
-!- SUBUNIT: Homotetramer. {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
-!- PTM: ISGylated. {ECO:0000250}.
-!- SIMILARITY: Belongs to the LDH/MDH superfamily. LDH family.
{ECO:0000305}.
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EMBL; AB060222; BAB41156.1; -; mRNA.
EMBL; AB125176; BAD51964.1; -; mRNA.
EMBL; AB169514; BAE01596.1; -; mRNA.
UniGene; Mfa.123; -.
ProteinModelPortal; Q9BE24; -.
SMR; Q9BE24; -.
PRIDE; Q9BE24; -.
HOVERGEN; HBG000462; -.
UniPathway; UPA00554; UER00611.
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.
2: Evidence at transcript level;
Acetylation; Cytoplasm; Isopeptide bond; NAD; Oxidoreductase;
Phosphoprotein; Ubl conjugation.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:P00338}.
CHAIN 2 332 L-lactate dehydrogenase A chain.
/FTId=PRO_0000168412.
NP_BIND 29 57 NAD. {ECO:0000250}.
ACT_SITE 193 193 Proton acceptor. {ECO:0000250}.
BINDING 99 99 NAD. {ECO:0000250}.
BINDING 106 106 Substrate. {ECO:0000250}.
BINDING 138 138 NAD or substrate. {ECO:0000250}.
BINDING 169 169 Substrate. {ECO:0000250}.
BINDING 248 248 Substrate. {ECO:0000250}.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000250|UniProtKB:P00338}.
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 18 18 Phosphothreonine.
{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 70 70 L -> F (in Ref. 1; BAB41156).
{ECO:0000305}.
SEQUENCE 332 AA; 36632 MW; 70FB912E7A6A7DA5 CRC64;
MATLKDQLIH NLLKEEQTPQ NKITVVGVGA VGMACAISIL MKDLADELAL VDVIEDKLKG
EMMDLQHGSL FLRTPKIVSG KDYSVTANSK LVIITAGARQ QEGESRLNLV QRNVNIFKFI
VPNVVKYSPN CKLLIVSNPV DILTYVAWKI SGFPKNRVIG SGCNLDSARF RYLMGERLGV
HPLSCHGWVL GEHGDSSVPV WSGMNVAGVS LKTLHPDLGT DKDKEQWKEV HKQVVESAYE
VIKLKGYTSW AIGLSVADLA ESIMKNLRRV HPVSTMIKGL YGIKDDVFLS VPCILGQNGI
SDLVKVTLTP EEEARLKKSA DTLWGIQKEL QF


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