Q5SJA1 (LDH_THET8) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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

Gene names

Name:	ldh
Ordered Locus Names:	TTHA1113

Organism

Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)

Taxonomic identifier

300852 [NCBI]

Taxonomic lineage

Bacteria › Deinococcus-Thermus › Deinococci › Thermales › Thermaceae › Thermus

Protein attributes

Sequence length	310 AA.
Sequence status	Complete.
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 By similarity. HAMAP MF_00488
Subcellular location	Cytoplasm By similarity 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 Complete proteome Reference proteome
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

Chain

1 – 310

310

L-lactate dehydrogenase HAMAP MF_00488

PRO_0000237569

Regions

Nucleotide binding

9 – 37

29

NAD By similarity

Sites

Active site

172

1

Proton acceptor

Binding site

85

1

Substrate By similarity

Binding site

117

1

NAD or substrate By similarity

Binding site

148

1

Substrate By similarity

Binding site

227

1

Substrate By similarity

Amino acid modifications

Modified residue

218

1

Phosphotyrosine By similarity

Secondary structure

1

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310

Helix Strand Turn

Details...

Beta strand

2 – 6

5

Helix

10 – 22

13

Beta strand

26 – 31

6

Helix

35 – 46

12

Helix

49 – 51

3

Beta strand

56 – 59

4

Helix

62 – 65

4

Beta strand

69 – 73

5

Helix

85 – 106

22

Beta strand

111 – 114

4

Beta strand

116 – 118

3

Helix

119 – 130

12

Helix

134 – 136

3

Beta strand

137 – 139

3

Helix

143 – 157

15

Turn

161 – 163

3

Beta strand

168 – 173

6

Helix

190 – 194

5

Helix

203 – 214

12

Helix

216 – 224

9

Helix

229 – 243

15

Beta strand

248 – 259

12

Beta strand

262 – 274

13

Beta strand

277 – 281

5

Helix

288 – 308

21

Sequences

	Sequence		Length	Mass (Da)
	Q5SJA1 [UniParc]. Last modified December 21, 2004. Version 1. Checksum: 71D12243E8C00DE4	FASTA	310	32,795
	10 20 30 40 50 60 MKVGIVGSGM VGSATAYALA LLGVAREVVL VDLDRKLAQA HAEDILHATP FAHPVWVRAG 70 80 90 100 110 120 SYGDLEGARA VVLAAGVAQR PGETRLQLLD RNAQVFAQVV PRVLEAAPEA VLLVATNPVD 130 140 150 160 170 180 VMTQVAYRLS GLPPGRVVGS GTILDTARFR ALLAEYLRVA PQSVHAYVLG EHGDSEVLVW 190 200 210 220 230 240 SSAQVGGVPL LEFAEARGRA LSPEDRARID EGVRRAAYRI IEGKGATYYG IGAGLARLVR 250 260 270 280 290 300 AILTDEKGVY TVSAFTPEVE GVLEVSLSLP RILGAGGVEG TVYPSLSPEE REALRRSAEI 310 LKEAAFALGF

References

[1]	"Complete genome sequence of Thermus thermophilus HB8." Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T., Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S. Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: HB8 / ATCC 27634 / DSM 579.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AP008226 Genomic DNA. Translation: BAD70936.1.

RefSeq

YP_144379.1. NC_006461.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2V6M	X-ray	2.20	A/B/C/D	1-310	[»]
2V7P	X-ray	2.10	A/B/C/D	1-310	[»]
2XXB	X-ray	2.15	A/B	1-310	[»]
2XXE	X-ray	3.00	A/B/C/D	1-310	[»]
2XXJ	X-ray	1.96	A/B/C/D	1-310	[»]

ProteinModelPortal

Q5SJA1.

SMR

Q5SJA1. Positions 1-310.

ModBase

Search...

Protein-protein interaction databases

STRING

Q5SJA1.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

GeneID

3169622.

GenomeReviews

Gene locus TTHA1113 in contig AP008226_GR.

KEGG

ttj:TTHA1113.

NMPDR

fig|300852.3.peg.1282.

PATRIC

23957185. VBITheThe93045_1092.

Phylogenomic databases

eggNOG

COG0039.

HOGENOM

HBG566126.

OMA

DSEISLW.

PhylomeDB

Q5SJA1.

ProtClustDB

CLSK244627.

Enzyme and pathway databases

BioCyc

TTHE300852:TTHA1113-MONOMER.

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.
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.

PANTHER

PTHR11540:SF3. PTHR11540:SF3. 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

LDH_THET8

Accession

Primary (citable) accession number: Q5SJA1

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2006
Last sequence update:	December 21, 2004
Last modified:	January 25, 2012
This is version 58 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program