P19858 (LDHA_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
L-lactate dehydrogenase A chain
Short name=LDH-A
EC=1.1.1.27

Alternative name(s):
LDH muscle subunit
Short name=LDH-M

Gene names

Name:

LDHA

Organism

Bos taurus (Bovine)

Taxonomic identifier

9913 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos

Protein attributes

Sequence length	332 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript level

General annotation (Comments)

Catalytic activity	(S)-lactate + NAD+ = pyruvate + NADH.
Pathway	Fermentation; pyruvate fermentation to lactate; (S)-lactate from pyruvate: step 1/1.
Subunit structure	Homotetramer.
Subcellular location	Cytoplasm.
Post-translational modification	ISGylated By similarity.
Sequence similarities	Belongs to the LDH/MDH superfamily. LDH family.

Ontologies

Keywords
Biological process	Glycolysis
Cellular component	Cytoplasm
Ligand	NAD
Molecular function	Oxidoreductase
PTM	Acetylation Phosphoprotein Ubl conjugation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	glycolysis Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	L-lactate dehydrogenase activity Inferred from electronic annotation. Source: EC nucleotide binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed
	Chain	2 – 332	331	L-lactate dehydrogenase A chain		PRO_0000168410
Regions
	Nucleotide binding	29 – 57	29	NAD By similarity
Sites
	Active site	193	1	Proton acceptor By similarity
	Binding site	106	1	Substrate By similarity
	Binding site	138	1	NAD or substrate By similarity
	Binding site	169	1	Substrate By similarity
	Binding site	248	1	Substrate By similarity
Amino acid modifications
	Modified residue	2	1	N-acetylalanine By similarity
	Modified residue	5	1	N6-acetyllysine By similarity
	Modified residue	14	1	N6-acetyllysine By similarity
	Modified residue	57	1	N6-acetyllysine By similarity
	Modified residue	81	1	N6-acetyllysine By similarity
	Modified residue	118	1	N6-acetyllysine By similarity
	Modified residue	126	1	N6-acetyllysine By similarity
	Modified residue	239	1	Phosphotyrosine By similarity
	Modified residue	278	1	N6-acetyllysine By similarity
	Modified residue	318	1	N6-acetyllysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	P19858 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: DAC59F02BBA7D16C	FASTA	332	36,598
	10 20 30 40 50 60 MATLKDQLIQ NLLKEEHVPQ NKITIVGVGA VGMACAISIL MKDLADEVAL VDVMEDKLKG 70 80 90 100 110 120 EMMDLQHGSL FLRTPKIVSG KDYNVTANSR LVIITAGARQ QEGESRLNLV QRNVNIFKFI 130 140 150 160 170 180 IPNIVKYSPN CKLLVVSNPV DILTYVAWKI SGFPKNRVIG SGCNLDSARF RYLMGERLGV 190 200 210 220 230 240 HPLSCHGWIL GEHGDSSVPV WSGVNVAGVS LKNLHPELGT DADKEQWKAV HKQVVDSAYE 250 260 270 280 290 300 VIKLKGYTSW AIGLSVADLA ESIMKNLRRV HPISTMIKGL YGIKEDVFLS VPCILGQNGI 310 320 330 SDVVKVTLTH EEEACLKKSA DTLWGIQKEL QF

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Primary structure of bovine lactate dehydrogenase-A isozyme and its synthesis in Escherichia coli." Ishiguro N., Osame S., Kagiya R., Ichijo S., Shinagawa M. Gene 91:281-285(1990) [PubMed: 2210387] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	NIH - Mammalian Gene Collection (MGC) project Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Hereford. Tissue: Fetal skin.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	D90141 mRNA. Translation: BAA14169.1. D90142 mRNA. Translation: BAA14170.1. D90143 mRNA. Translation: BAA14171.1. BC146210 mRNA. Translation: AAI46211.1.
IPI	IPI00906445.
PIR	JQ2222.
RefSeq	NP_776524.1. NM_174099.2.
UniGene	Bt.3809.
3D structure databases
ProteinModelPortal	P19858.
SMR	P19858. Positions 2-332.
ModBase	Search...
Protein-protein interaction databases
STRING	P19858.
Proteomic databases
PRIDE	P19858.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSBTAT00000011447; ENSBTAP00000011447; ENSBTAG00000008683. ENSBTAT00000056276; ENSBTAP00000047729; ENSBTAG00000008683.
GeneID	281274.
KEGG	bta:281274.
Organism-specific databases
CTD	3939.
Phylogenomic databases
eggNOG	maNOG08436.
GeneTree	ENSGT00550000074541.
HOVERGEN	HBG000462.
InParanoid	P19858.
OrthoDB	EOG4RR6HR.
PhylomeDB	P19858.
Family and domain databases
InterPro	IPR001557. L-lactate/malate_DH. IPR011304. L-lactate_DH. IPR018177. L-lactate_DH_AS. IPR022383. Lactate/malate_DH_C. IPR001236. Lactate/malate_DH_N. IPR015955. Lactate_DH/Glyco_Ohase_4_C. IPR016040. NAD(P)-bd_dom. [Graphical view]
Gene3D	G3DSA:3.90.110.10. lact_mal_DH. 1 hit. G3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
KO	K00016.
Pfam	PF02866. Ldh_1_C. 1 hit. PF00056. Ldh_1_N. 1 hit. [Graphical view]
PIRSF	PIRSF000102. Lac_mal_DH. 1 hit.
PRINTS	PR00086. LLDHDRGNASE.
SUPFAM	SSF56327. Lactate_DH/Glyco_hydro_4_C. 1 hit.
TIGRFAMs	TIGR01771. L-LDH-NAD. 1 hit.
PROSITE	PS00064. L_LDH. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

LDHA_BOVIN

Accession

Primary (citable) accession number: P19858
Secondary accession number(s): A6H7E0

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1991
Last sequence update:	January 23, 2007
Last modified:	December 14, 2011
This is version 102 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program