Reviewed, UniProtKB/Swiss-Prot P19858 (LDHA_BOVIN)

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.
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
Gene Ontology (GO)
Biological process	anaerobic glycolysis Inferred from electronic annotation. Source: InterPro oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	L-lactate dehydrogenase activity Inferred from electronic annotation. Source: EC protein binding Inferred from sequence or structural similarity. Source: AgBase
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)
	P19858-1 [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.

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	IPI00716974.
PIR	JQ2222.
RefSeq	NP_776524.1.
UniGene	Bt.3809
3D structure databases
SMR	P19858. Positions 2-332.
ModBase	Search...
Protein-protein interaction databases
STRING	P19858.
Genome annotation databases
Ensembl	ENSBTAT00000011447; ENSBTAP00000011447; ENSBTAG00000008683; Bos taurus. [Genome view] ENSBTAT00000047709; ENSBTAP00000044888; ENSBTAG00000008683; Bos taurus. [Genome view] ENSBTAT00000056276; ENSBTAP00000047729; ENSBTAG00000008683; Bos taurus. [Genome view]
GeneID	281274.
KEGG	bta:281274.
Organism-specific databases
CTD	281274.
Phylogenomic databases
eggNOG	maNOG08436.
HOVERGEN	P19858.
InParanoid	P19858.
OrthoDB	EOG91K1XC.
PhylomeDB	P19858.
Enzyme and pathway databases
BRENDA	1.1.1.27. 251.
Family and domain databases
InterPro	IPR001557. L-lactate/malate_DH. IPR011304. L-lactate_DH. IPR018177. L-lactate_DH_AS. IPR001236. Lactate/malate_DH. 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.
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.
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:	February 9, 2010
This is version 85 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)