Reviewed, UniProtKB/Swiss-Prot P00344 (LDH_BACST)

Names and origin

Protein names

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

Gene names

Name:	ldh
Synonyms:	lct

Organism

Bacillus stearothermophilus (Geobacillus stearothermophilus)

Taxonomic identifier

1422 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Geobacillus

Protein attributes

Sequence length	317 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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

Chain

1 – 317

317

L-lactate dehydrogenase HAMAP MF_00488

PRO_0000168328

Regions

Nucleotide binding

15 – 43

29

NAD By similarity

Sites

Active site

179

1

Proton acceptor HAMAP MF_00488

Binding site

92

1

Substrate HAMAP MF_00488

Binding site

124

1

NAD or substrate HAMAP MF_00488

Binding site

155

1

Substrate HAMAP MF_00488

Binding site

233

1

Substrate HAMAP MF_00488

Amino acid modifications

Modified residue

224

1

Phosphotyrosine By similarity

Experimental info

Sequence conflict

113

1

S → H Ref.3

Secondary structure

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317

Helix Strand Turn

Details...

Beta strand

6 – 12

7

Helix

16 – 26

11

Turn

27 – 29

3

Beta strand

32 – 37

6

Helix

41 – 54

14

Helix

55 – 57

3

Beta strand

62 – 64

3

Helix

69 – 71

3

Beta strand

76 – 80

5

Helix

96 – 112

17

Beta strand

117 – 121

5

Helix

126 – 137

12

Beta strand

143 – 146

4

Helix

148 – 150

3

Helix

152 – 163

12

Helix

168 – 170

3

Beta strand

175 – 177

3

Turn

179 – 182

4

Helix

212 – 220

9

Helix

223 – 230

8

Helix

235 – 249

15

Beta strand

254 – 261

8

Beta strand

263 – 267

5

Beta strand

272 – 280

9

Beta strand

283 – 287

5

Turn

296 – 299

4

Helix

300 – 308

9

Helix

310 – 313

4

Sequences

	Sequence		Length	Mass (Da)
	P00344-1 [UniParc]. Last modified January 1, 1988. Version 1. Checksum: 4B146CF681C91046	FASTA	317	34,863
	10 20 30 40 50 60 MKNNGGARVV VIGAGFVGAS YVFALMNQGI ADEIVLIDAN ESKAIGDAMD FNHGKVFAPK 70 80 90 100 110 120 PVDIWHGDYD DCRDADLVVI CAGANQKPGE TRLDLVDKNI AIFRSIVESV MASGFQGLFL 130 140 150 160 170 180 VATNPVDILT YATWKFSGLP HERVIGSGTI LDTARFRFLL GEYFSVAPQN VHAYIIGEHG 190 200 210 220 230 240 DTELPVWSQA YIGVMPIRKL VESKGEEAQK DLERIFVNVR DAAYQIIEKK GATYYGIAMG 250 260 270 280 290 300 LARVTRAILH NENAILTVSA YLDGLYGERD VYIGVPAVIN RNGIREVIEI ELNDDEKNRF 310 HHSAATLKSV LARAFTR

References

[1]	"Structure and function of L-lactate dehydrogenases from thermophilic and mesophilic bacteria. III) The primary structure of thermophilic lactate dehydrogenase from Bacillus stearothermophilus. Hydroxylamine-, o-iodosobenzoic acid- and tryptic-fragments. The complete amino-acid sequence." Wirz B., Suter F., Zuber H. Hoppe-Seyler's Z. Physiol. Chem. 364:893-909(1983) [PubMed: 6352452] [Abstract] Cited for: PROTEIN SEQUENCE. Strain: ATCC 29609 / DSM 2027 / NCA 1503 / NCIB 8924.
[2]	"Cloning, expression and complete nucleotide sequence of the Bacillus stearothermophilus L-lactate dehydrogenase gene." Barstow D.A., Clarke A.R., Chia W.N., Wigley D., Sharman A.F., Holbrook J.J., Atkinson T., Minton N.P. Gene 46:47-55(1986) [PubMed: 3026926] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"Structure and function of L-lactate dehydrogenases from thermophilic and mesophilic bacteria, VI. Nucleotide sequences of lactate dehydrogenase genes from the thermophilic bacteria Bacillus stearothermophilus, B. caldolyticus and B. caldotenax." Zuelli F., Weber H., Zuber H. Biol. Chem. Hoppe-Seyler 368:1167-1177(1987) [PubMed: 3675869] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]	"Structure and function of L-lactate dehydrogenases from thermophilic and mesophilic bacteria. II) The primary structure of thermophilic lactate dehydrogenase from Bacillus stearothermophilus. Cyanogen bromide fragments and partial sequence." Tratschin J.D., Wirz B., Frank G., Zuber H. Hoppe-Seyler's Z. Physiol. Chem. 364:879-892(1983) [PubMed: 6618448] [Abstract] Cited for: PARTIAL PROTEIN SEQUENCE. Strain: ATCC 29609 / DSM 2027 / NCA 1503 / NCIB 8924.
[5]	"Structure of a ternary complex of an allosteric lactate dehydrogenase from Bacillus stearothermophilus at 2.5-A resolution." Wigley D.B., Gamblin S.J., Turkenburg J.P., Dodson E.J., Piontek K., Muirhead H., Holbrook J.J. J. Mol. Biol. 223:317-335(1992) [PubMed: 1731077] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH NAD AND SUBSTRATE ANALOG.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

M14788 Genomic DNA. Translation: AAA22568.1.
M19396 Genomic DNA. Translation: AAA22567.1.

PIR

DEBSLF. A26053.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1LDB	X-ray	2.80	A/B/C/D	1-317	[»]
1LDN	X-ray	2.50	A/B/C/D/E/F/G/H	1-316	[»]
2LDB	X-ray	3.00	A/B/C/D	1-317	[»]

ModBase

Search...

Enzyme and pathway databases

BRENDA

1.1.1.27. 266715.

Family and domain databases

HAMAP

MF_00488.
[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_BACST

Accession

Primary (citable) accession number: P00344

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	January 1, 1988
Last modified:	June 16, 2009
This is version 92 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

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