Reviewed, UniProtKB/Swiss-Prot P00343 (LDH_LACCA)

Names and origin

Protein names

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

Gene names

Name:

ldh

Organism

Lactobacillus casei

Taxonomic identifier

1582 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Lactobacillales › Lactobacillaceae › Lactobacillus

Protein attributes

Sequence length	326 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. HAMAP MF_00488
Pathway	Fermentation; pyruvate fermentation to lactate; (S)-lactate from pyruvate: step 1/1. HAMAP MF_00488
Subunit structure	Homotetramer. HAMAP MF_00488
Subcellular location	Cytoplasm HAMAP MF_00488.
Sequence similarities	Belongs to the LDH/MDH superfamily. LDH family.

Ontologies

Keywords
Biological process	Glycolysis
Cellular component	Cytoplasm
Ligand	NAD
Molecular function	Oxidoreductase
PTM	Phosphoprotein
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	anaerobic glycolysis Inferred from electronic annotation. Source: HAMAP 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: HAMAP 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.3

Chain

2 – 326

325

L-lactate dehydrogenase HAMAP MF_00488

PRO_0000168347

Regions

Nucleotide binding

18 – 46

29

NAD By similarity

Sites

Active site

181

1

Proton acceptor By similarity

Binding site

94

1

Substrate By similarity

Binding site

126

1

NAD or substrate By similarity

Binding site

157

1

Substrate By similarity

Binding site

235

1

Substrate By similarity

Amino acid modifications

Modified residue

226

1

Phosphotyrosine By similarity

Experimental info

Sequence conflict

26

1

Y → F AA sequence Ref.3

Sequence conflict

52

1

I → T AA sequence Ref.3

Sequence conflict

88 – 89

2

QK → KQ AA sequence Ref.3

Sequence conflict

119

1

G → L AA sequence Ref.3

Sequence conflict

270

1

L → I AA sequence Ref.3

Sequence conflict

273

1

I → L AA sequence Ref.3

Secondary structure

1

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326

Helix Strand Turn

Details...

Beta strand

12 – 14

3

Turn

17 – 18

2

Helix

19 – 31

13

Turn

32

1

Beta strand

37 – 39

3

Helix

45 – 54

10

Turn

55 – 56

2

Turn

59 – 60

2

Turn

70 – 74

5

Beta strand

79 – 81

3

Turn

84

1

Turn

96

1

Helix

97 – 100

4

Turn

101 – 102

2

Turn

104 – 109

6

Helix

110 – 114

5

Turn

115 – 116

2

Beta strand

120 – 122

3

Helix

128 – 139

12

Turn

143 – 145

3

Turn

150 – 151

2

Helix

152 – 165

14

Turn

170 – 171

2

Beta strand

174 – 179

6

Beta strand

186 – 193

8

Turn

195 – 196

2

Turn

216 – 221

6

Helix

222 – 224

3

Turn

225 – 228

4

Turn

235 – 236

2

Helix

237 – 252

16

Turn

253

1

Beta strand

278 – 282

5

Turn

283 – 284

2

Beta strand

285 – 289

5

Turn

295 – 296

2

Helix

297 – 303

7

Turn

304 – 316

13

Sequences

	Sequence		Length	Mass (Da)
	P00343-1 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 934905641592AF8A	FASTA	326	35,531
	10 20 30 40 50 60 MASITDKDHQ KVILVGDGAV GSSYAYAMVL QGIAQEIGIV DIFKDKTKGD AIDLSNALPF 70 80 90 100 110 120 TSPKKIYSAE YSDAKDADLV VITAGAPQKP GETRLDLVNK NLKILKSIVD PIVDSGFNGI 130 140 150 160 170 180 FLVAANPVDI LTYATWKLSG FPKNRVVGSG TSLDTARFRQ SIAEMVNVDA RSVHAYIMGE 190 200 210 220 230 240 HGDTEFPVWS HANIGGVTIA EWVKAHPEIK EDKLVKMFED VRDAAYEIIK LKGATFYGIA 250 260 270 280 290 300 TALARISKAI LNDENAVLPL SVYMDGQYGL NDIYIGTPAV INRNGIQNIL EIPLTDHEEE 310 320 SMQKSASQLK KVLTDAFAKN DIETRQ

References

[1]	"Cloning and nucleotide sequence of the Lactobacillus casei lactate dehydrogenase gene." Kim S.F., Baek S.J., Pack M.Y. Appl. Environ. Microbiol. 57:2413-2417(1991) [PubMed: 1768113] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 393 / DSM 20011 / IFO 15883 / JCM 1134 / NCDO 161.
[2]	Taguchi H., Ohta T. Submitted (NOV-1991) to the PIR data bank Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 393 / DSM 20011 / IFO 15883 / JCM 1134 / NCDO 161.
[3]	"The complete primary structure of the allosteric L-lactate dehydrogenase from Lactobacillus casei." Hensel R., Mayr U., Yang C. Eur. J. Biochem. 134:503-511(1983) [PubMed: 6411465] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-326.
[4]	"Structure determination of the allosteric L-lactate dehydrogenase from Lactobacillus-casei at 3A resolution." Buehner M., Hecht H.J. Acta Crystallogr. A 40:32-34(1984) Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

D12591 Genomic DNA. Translation: BAA02133.1.
M76708 Genomic DNA. Translation: AAA25245.2.

PIR

DELBLA. A43944.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1LLC	X-ray	3.00	A	2-326	[»]
2ZQY	X-ray	2.60	A/B/C/D	1-326	[»]
2ZQZ	X-ray	2.50	A/B/C/D/E/F	1-326	[»]

ModBase

Search...

Enzyme and pathway databases

BioCyc

MetaCyc:MONOMER-8681.

BRENDA

1.1.1.27. 610.

Family and domain databases

HAMAP

MF_00488. Lactate_dehydrog.
[Tree]

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.
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.

TIGRFAMs

TIGR01771. L-LDH-NAD. 1 hit.

PROSITE

PS00064. L_LDH. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

LDH_LACCA

Accession

Primary (citable) accession number: P00343

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	January 23, 2007
Last modified:	February 9, 2010
This is version 95 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)