P00336 (LDHB_PIG) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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

Alternative name(s):
LDH heart subunit
Short name=LDH-H

Gene names

Name:

LDHB

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	334 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.
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
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	glycolysis Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
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 – 334

333

L-lactate dehydrogenase B chain

PRO_0000168462

Regions

Nucleotide binding

30 – 58

29

NAD By similarity

Sites

Active site

194

1

Proton acceptor By similarity

Binding site

100

1

NAD By similarity

Binding site

107

1

Substrate By similarity

Binding site

139

1

NAD or substrate By similarity

Binding site

170

1

Substrate By similarity

Binding site

249

1

Substrate By similarity

Amino acid modifications

Modified residue

2

1

N-acetylalanine Ref.2

Modified residue

7

1

N6-acetyllysine By similarity

Modified residue

58

1

N6-acetyllysine By similarity

Modified residue

119

1

N6-acetyllysine By similarity

Modified residue

240

1

Phosphotyrosine By similarity

Modified residue

248

1

Phosphotyrosine By similarity

Modified residue

249

1

Phosphothreonine By similarity

Modified residue

329

1

N6-acetyllysine By similarity

Experimental info

Sequence conflict

14 – 15

2

EE → QQ AA sequence Ref.2

Sequence conflict

81

1

D → N AA sequence Ref.2

Sequence conflict

131

1

D → N AA sequence Ref.2

Sequence conflict

214

1

E → Q AA sequence Ref.2

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

334

Helix Strand Turn

Details...

Beta strand

24 – 26

3

Helix

31 – 43

13

Beta strand

49 – 51

3

Helix

57 – 69

13

Helix

70 – 72

3

Helix

86 – 88

3

Beta strand

92 – 95

4

Turn

98 – 99

2

Turn

107 – 108

2

Helix

112 – 119

8

Turn

120 – 121

2

Helix

122 – 128

7

Beta strand

133 – 136

4

Helix

141 – 152

12

Helix

155 – 158

4

Turn

163 – 164

2

Helix

165 – 179

15

Turn

215 – 218

4

Helix

228 – 240

13

Helix

247 – 266

20

Turn

267

1

Beta strand

294 – 297

4

Turn

298 – 299

2

Beta strand

300 – 304

5

Helix

313 – 331

19

Sequences

	Sequence		Length	Mass (Da)
	P00336 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: A0A2389BAB8FFD73	FASTA	334	36,612
	10 20 30 40 50 60 MATLKEKLIA PVAEEETTIP NNKITVVGVG QVGMACAISI LGKSLTDELA LVDVLEDKLK 70 80 90 100 110 120 GEMMDLQHGS LFLQTPKIVA DKDYSVTANS KIVVVTAGVR QQEGESRLNL VQRNVNVFKF 130 140 150 160 170 180 IIPQIVKYSP DCIIIVVSNP VDILTYVTWK LSGLPKHRVI GSGCNLDSAR FRYLMAEKLG 190 200 210 220 230 240 VHPSSCHGWI LGEHGDSSVA VWSGVNVAGV SLQELNPEMG TDNDSENWKE VHKMVVESAY 250 260 270 280 290 300 EVIKLKGYTN WAIGLSVADL IESMLKNLSR IHPVSTMVQG MYGIENEVFL SLPCVLNARG 310 320 330 LTSVINQKLK DDEVAQLKNS ADTLWGIQKD LKDL

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 2-334.
[3]	Kiltz H.-H. Submitted (OCT-1977) to the PIR data bank Cited for: SEQUENCE REVISION TO 22; 148; 216 AND 218.
[4]	"Structure of the active ternary complex of pig heart lactate dehydrogenase with S-lac-NAD at 2.7-A resolution." Grau U.M., Trommer W.E., Rossmann M.G. J. Mol. Biol. 151:289-307(1981) [PubMed: 7338899] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS).
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U07180 mRNA. Translation: AAA50438.1.

PIR

DEPGLH. A91671.

RefSeq

NP_001106758.1. NM_001113287.1.

UniGene

Ssc.71163.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
5LDH	X-ray	2.70	A/B	2-334	[»]

ProteinModelPortal

P00336.

SMR

P00336. Positions 2-333.

ModBase

Search...

Protein-protein interaction databases

STRING

P00336.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

GeneID

100621540.

KEGG

ssc:407246.

Organism-specific databases

CTD

3945.

Phylogenomic databases

GeneTree

ENSGT00550000074541.

HOVERGEN

HBG000462.

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

LDHB_PIG

Accession

Primary (citable) accession number: P00336

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	January 23, 2007
Last modified:	January 25, 2012
This is version 101 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program