Reviewed, UniProtKB/Swiss-Prot P00341 (LDHA_SQUAC)

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-M

Gene names

Name:

ldha

Organism

Squalus acanthias (Spiny dogfish)

Taxonomic identifier

7797 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Chondrichthyes › Elasmobranchii › Squalea › Hypnosqualea › Squaliformes › Squaloidei › Squalidae › Squalus

Protein attributes

Sequence length	333 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
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	anaerobic glycolysis Inferred from electronic annotation. Source: InterPro oxidation reduction 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 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 – 333

332

L-lactate dehydrogenase A chain

PRO_0000168455

Regions

Nucleotide binding

30 – 58

29

NAD

Sites

Active site

194

1

Proton acceptor

Binding site

100

1

NAD

Binding site

107

1

Substrate By similarity

Binding site

139

1

NAD or substrate By similarity

Binding site

170

1

Substrate

Binding site

249

1

Substrate By similarity

Amino acid modifications

Modified residue

2

1

N-acetylalanine

Experimental info

Sequence conflict

124

1

D → N AA sequence Ref.2

Sequence conflict

184

1

S → C AA sequence Ref.2

Sequence conflict

198 – 200

3

SVP → VPS AA sequence Ref.2

Sequence conflict

206 – 211

6

NVAGVS → WNA AA sequence Ref.2

Sequence conflict

222

1

D → N AA sequence Ref.2

Sequence conflict

226 – 227

2

EN → QD AA sequence Ref.2

Sequence conflict

286 – 287

2

ND → DN AA sequence Ref.2

Sequence conflict

297 – 298

2

DN → ND AA sequence Ref.2

Secondary structure

1

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333

Helix Strand Turn

Details...

Helix

4 – 8

5

Beta strand

21 – 27

7

Helix

31 – 42

12

Beta strand

47 – 52

6

Helix

56 – 67

12

Helix

68 – 72

5

Beta strand

77 – 80

4

Helix

84 – 87

4

Beta strand

91 – 95

5

Helix

107 – 110

4

Helix

111 – 128

18

Beta strand

133 – 136

4

Beta strand

138 – 140

3

Helix

141 – 152

12

Helix

156 – 158

3

Beta strand

159 – 161

3

Helix

165 – 179

15

Helix

183 – 185

3

Helix

202 – 204

3

Beta strand

210 – 215

6

Helix

216 – 219

4

Turn

222 – 229

8

Helix

230 – 246

17

Helix

251 – 265

15

Beta strand

270 – 277

8

Beta strand

289 – 297

9

Beta strand

300 – 304

5

Helix

311 – 329

19

Sequences

	Sequence		Length	Mass (Da)
	P00341-1 [UniParc]. Last modified January 23, 2007. Version 4. Checksum: 20C3B5F84B6C0117	FASTA	333	36,695
	10 20 30 40 50 60 MATLKDKLIG HLATSQEPRS YNKITVVGVG AVGMACAISI LMKDLADEVA LVDVMEDKLK 70 80 90 100 110 120 GEMMDLQHGS LFLHTAKIVS GKDYSVSAGS KLVVITAGAR QQEGESRLNL VQRNVNIFKF 130 140 150 160 170 180 IIPDIVKHSP DCIILVVSNP VDVLTYVAWK LSGLPMHRII GSGCNLDSAR FRYLMGERLG 190 200 210 220 230 240 VHSSSCHGWV IGEHGDSSVP VWSGMNVAGV SLKELHPELG TDKDKENWKK LHKDVVDSAY 250 260 270 280 290 300 EVIKLKGYTS WAIGLSVADL AETIMKNLCR VHPVSTMVKD FYGIKNDVFL SLPCVLDNHG 310 320 330 ISNIVKMKLK PDEEQQLQKS ATTLWDIQKD LKF

References

[1]	"The cDNA sequence of the lactate dehydrogenase-A of the spiny dogfish (Squalus acanthias): corrections to the amino acid sequence and an analysis of the phylogeny of vertebrate lactate dehydrogenases." Stock D.W., Powers D.A. Mol. Mar. Biol. Biotechnol. 4:284-294(1995) [PubMed: 8541980] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Skeletal muscle.
[2]	"Amino acid sequence of dogfish muscle lactate dehydrogenase." Taylor S.S. J. Biol. Chem. 252:1799-1806(1977) [PubMed: 838743] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-333.
[3]	"Atomic co-ordinates for dogfish M4 apo-lactate dehydrogenase." Adams M.J., Ford G.C., Liljas A., Rossmann M.G. Biochem. Biophys. Res. Commun. 53:46-51(1973) [PubMed: 4795361] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY.
[4]	"Structural adaptations of lactate dehydrogenase isozymes." Eventoff W., Rossmann M.G., Taylor S.S., Torff H.-J., Meyer H., Keil W., Kiltz H.-H. Proc. Natl. Acad. Sci. U.S.A. 74:2677-2681(1977) [PubMed: 197516] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
[5]	"Refined crystal structure of dogfish M4 apo-lactate dehydrogenase." Abad-Zapatero C., Griffith J.P., Sussman J.L., Rossmann M.G. J. Mol. Biol. 198:445-467(1987) [PubMed: 3430615] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH NAD AND SUBSTRATE ANALOG.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

U38893 mRNA. Translation: AAA91038.1.

PIR

DEDFLM. A00350.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1LDM	X-ray	2.10	A	2-333	[»]
3LDH	X-ray	3.00	A	4-332	[»]
6LDH	X-ray	2.00	A	2-333	[»]
8LDH	X-ray	2.80	A	2-333	[»]

ModBase

Search...

Phylogenomic databases

HOVERGEN

P00341.

Enzyme and pathway databases

BRENDA

1.1.1.27. 981.

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.
[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_SQUAC

Accession

Primary (citable) accession number: P00341
Secondary accession number(s): Q92114

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	January 23, 2007
Last modified:	June 16, 2009
This is version 83 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)