P00339 (LDHA_PIG) 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

Sus scrofa (Pig) [Complete proteome]

Taxonomic identifier

9823 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Suina › Suidae › Sus

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 protein 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	3D-structure Complete proteome Direct protein sequencing
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 Ref.2

Chain

2 – 332

331

L-lactate dehydrogenase A chain

PRO_0000168416

Regions

Nucleotide binding

29 – 57

29

NAD

Sites

Active site

193

1

Proton acceptor

Binding site

99

1

NAD

Binding site

106

1

Substrate

Binding site

138

1

NAD or substrate

Binding site

169

1

Substrate

Binding site

248

1

Substrate

Amino acid modifications

Modified residue

2

1

N-acetylalanine Ref.2

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

Experimental info

Sequence conflict

233

1

Q → E AA sequence Ref.2

Sequence conflict

286

1

D → N AA sequence Ref.2

Secondary structure

1

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332

Helix Strand Turn

Details...

Helix

3 – 7

5

Beta strand

8 – 10

3

Beta strand

19 – 25

7

Helix

29 – 40

12

Beta strand

45 – 50

6

Helix

54 – 66

13

Helix

67 – 70

4

Beta strand

75 – 81

7

Helix

82 – 85

4

Beta strand

89 – 93

5

Helix

105 – 108

4

Helix

109 – 126

18

Beta strand

131 – 134

4

Beta strand

136 – 138

3

Helix

139 – 150

12

Beta strand

156 – 159

4

Helix

163 – 177

15

Helix

181 – 183

3

Beta strand

184 – 190

7

Beta strand

192 – 205

14

Helix

210 – 213

4

Beta strand

218 – 221

4

Helix

227 – 244

18

Helix

249 – 263

15

Beta strand

268 – 275

8

Beta strand

279 – 281

3

Beta strand

287 – 295

9

Beta strand

298 – 303

6

Helix

311 – 329

19

Sequences

	Sequence		Length	Mass (Da)
	P00339 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: FD3B4673557C9B72	FASTA	332	36,619
	10 20 30 40 50 60 MATLKDQLIH NLLKEEHVPH NKITVVGVGA VGMACAISIL MKELADEIAL VDVMEDKLKG 70 80 90 100 110 120 EMMDLQHGSL FLRTPKIVSG KDYNVTANSR LVVITAGARQ QEGESRLNLV QRNVNIFKFI 130 140 150 160 170 180 IPNIVKYSPN CKLLVVSNPV DILTYVAWKI SGFPKNRVIG SGCNLDSARF RYLMGERLGV 190 200 210 220 230 240 HPLSCHGWIL GEHGDSSVPV WSGVNVAGVS LKNLHPELGT DADKEHWKAV HKQVVDSAYE 250 260 270 280 290 300 VIKLKGYTSW AIGLSVADLA ESIMKNLRRV HPISTMIKGL YGIKEDVFLS VPCILGQNGI 310 320 330 SDVVKVTLTP EEEAHLKKSA DTLWGIQKEL QF

References

[1]	"Evolutionary relationships of lactate dehydrogenases (LDHs) from mammals, birds, an amphibian, fish, barley, and bacteria: LDH cDNA sequences from Xenopus, pig, and rat." Tsuji S., Qureshi M.A., Hou E.W., Fitch W.M., Li S.S.-L. Proc. Natl. Acad. Sci. U.S.A. 91:9392-9396(1994) [PubMed: 7937776] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Muscle.
[2]	"The primary structure of porcine lactate dehydrogenase: isoenzymes M4 and H4." Kiltz H.-H., Keil W., Griesbach M., Petry K., Meyer H. Hoppe-Seyler's Z. Physiol. Chem. 358:123-127(1977) [PubMed: 838465] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-332.
[3]	"Design and synthesis of new enzymes based on the lactate dehydrogenase framework." Dunn C.R., Wilks H.M., Halsall D.J., Atkinson T., Clarke A.R., Muirhead H., Holbrook J.J. Philos. Trans. R. Soc. Lond., B, Biol. Sci. 332:177-184(1991) [PubMed: 1678537] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS)IN COMPLEX WITH NAD AND SUBSTRATE ANALOG.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U07178 mRNA. Translation: AAA50436.1.

PIR

DEPGLM. A00348.

UniGene

Ssc.50275.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
9LDB	X-ray	2.20	A/B	2-332	[»]
9LDT	X-ray	2.00	A/B	2-332	[»]

ProteinModelPortal

P00339.

SMR

P00339. Positions 2-332.

ModBase

Search...

Protein-protein interaction databases

STRING

P00339.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSSSCT00000014598; ENSSSCP00000014203; ENSSSCG00000013366.

Phylogenomic databases

HOVERGEN

HBG000462.

OrthoDB

EOG4RR6HR.

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.

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_PIG

Accession

Primary (citable) accession number: P00339

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	January 23, 2007
Last modified:	December 14, 2011
This is version 97 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program