Reviewed, UniProtKB/Swiss-Prot P19869 (LDH2_BIFLO)

Names and origin

Protein names

Recommended name:
    L-lactate dehydrogenase 2
      Short name=L-LDH 2
    EC=1.1.1.27

Gene names

Name:	ldh2
Synonyms:	ldh
Ordered Locus Names:	BL1308

Organism

Bifidobacterium longum [Complete proteome] [HAMAP]

Taxonomic identifier

216816 [NCBI]

Taxonomic lineage

Bacteria › Actinobacteria › Actinobacteridae › Bifidobacteriales › Bifidobacteriaceae › Bifidobacterium

Protein attributes

Sequence length	320 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 Complete proteome 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.1

Chain

2 – 320

319

L-lactate dehydrogenase 2 HAMAP MF_00488

PRO_0000168331

Regions

Nucleotide binding

17 – 45

29

NAD HAMAP MF_00488

Nucleotide binding

159 – 176

18

NAD HAMAP MF_00488

Sites

Active site

181

1

Proton acceptor HAMAP MF_00488

Binding site

87

1

NAD 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

237

1

Substrate By similarity

Amino acid modifications

Modified residue

228

1

Phosphotyrosine By similarity

Secondary structure

1

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320

Helix Strand Turn

Details...

Beta strand

10 – 14

5

Helix

18 – 29

12

Beta strand

34 – 39

6

Helix

43 – 55

13

Helix

56 – 59

4

Beta strand

64 – 69

6

Helix

71 – 74

4

Beta strand

78 – 82

5

Helix

94 – 115

22

Beta strand

119 – 123

5

Helix

128 – 139

12

Beta strand

145 – 148

4

Helix

152 – 166

15

Helix

170 – 172

3

Beta strand

177 – 182

6

Helix

199 – 201

3

Helix

213 – 231

19

Helix

239 – 253

15

Beta strand

258 – 265

8

Beta strand

267 – 269

3

Beta strand

274 – 284

11

Beta strand

287 – 289

3

Helix

298 – 316

19

Turn

317 – 319

3

Sequences

	Sequence		Length	Mass (Da)
	P19869-1 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: D3E092AA9C353C4E	FASTA	320	34,240
	10 20 30 40 50 60 MAETTVKPTK LAVIGAGAVG STLAFAAAQR GIAREIVLED IAKERVEAEV LDMQHGSSFY 70 80 90 100 110 120 PTVSIDGSDD PEICRDADMV VITAGPRQKP GQSRLELVGA TVNILKAIMP NLVKVAPNAI 130 140 150 160 170 180 YMLITNPVDI ATHVAQKLTG LPENQIFGSG TNLDSARLRF LIAQQTGVNV KNVHAYIAGE 190 200 210 220 230 240 HGDSEVPLWE SATIGGVPMC DWTPLPGHDP LDADKREEIH QEVKNAAYKI INGKGATNYA 250 260 270 280 290 300 IGMSGVDIIE AVLHDTNRIL PVSSMLKDFH GISDICMSVP TLLNRQGVNN TINTPVSDKE 310 320 LAALKRSAET LKETAAQFGF

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Sequence and characteristics of the Bifidobacterium longum gene encoding L-lactate dehydrogenase and the primary structure of the enzyme: a new feature of the allosteric site." Minowa T., Iwata S., Sakai H., Masaki H., Ohta T. Gene 85:161-168(1989) [PubMed: 2695396] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-40 AND 315-320.
[2]	"The genome sequence of Bifidobacterium longum reflects its adaptation to the human gastrointestinal tract." Schell M.A., Karmirantzou M., Snel B., Vilanova D., Berger B., Pessi G., Zwahlen M.-C., Desiere F., Bork P., Delley M., Pridmore R.D., Arigoni F. Proc. Natl. Acad. Sci. U.S.A. 99:14422-14427(2002) [PubMed: 12381787] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: NCC 2705.
[3]	Roy D., Sirois S. Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 130-233. Strain: ATCC 15707 / DSM 20219 / JCM 1217 / NCTC 11818 / E194b and ATCC 15708 / JCM 7054 / LMG 10498 / S3.
[4]	"Molecular basis of allosteric activation of bacterial L-lactate dehydrogenase." Iwata S., Ohta T. J. Mol. Biol. 230:21-27(1993) [PubMed: 8450537] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH NAD. Strain: AM 101-2.
[5]	"T and R states in the crystals of bacterial L-lactate dehydrogenase reveal the mechanism for allosteric control." Iwata S., Kamata K., Yoshida S., Ohta T. Nat. Struct. Biol. 1:176-185(1994) [PubMed: 7656036] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH NAD. Strain: AM 101-2.

Cross-references

Sequence databases

EMBLGenBankDDBJ

M33585 Genomic DNA. Translation: AAA22900.1.
AE014295 Genomic DNA. Translation: AAN25108.1.
AF261669 Genomic DNA. Translation: AAF70510.1.
AF261670 Genomic DNA. Translation: AAF70511.1.

PIR

JQ0183.

RefSeq

NP_696472.1.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1LLD	X-ray	2.00	A/B	2-320	[»]
1LTH	X-ray	2.50	R/T	2-320	[»]

ModBase

Search...

Genome annotation databases

GeneID

1022790.

GenomeReviews

Gene locus BL1308 in contig AE014295_GR.

KEGG

blo:BL1308.

Organism-specific databases

CMR

Search...

Phylogenomic databases

HOGENOM

P19869.

OMA

P19869. VHAYVLG.

Enzyme and pathway databases

BioCyc

BLON206672:BL1308-MON.
MetaCyc:MON-13065.

BRENDA

1.1.1.27. 39917.

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

LDH2_BIFLO

Accession

Primary (citable) accession number: P19869
Secondary accession number(s): Q9L505, Q9L506

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1991
Last sequence update:	January 23, 2007
Last modified:	June 16, 2009
This is version 88 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)