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UniProtKB/Swiss-Prot entry P19869

[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name LDH2_BIFLO
Primary accession number P19869
Secondary accession numbers Q9L505 Q9L506
Integrated into Swiss-Prot on February 1, 1991
Sequence was last modified on January 23, 2007 (Sequence version 3)
Annotations were last modified on    July 22, 2008 (Entry version 80)
Name and origin of the protein
Protein name L-lactate dehydrogenase 2
Synonyms L-LDH 2
EC 1.1.1.27
Gene name
Name: ldh2
Synonyms: ldh
OrderedLocusNames: BL1308
From
Bifidobacterium longum [TaxID: 216816] [HAMAP proteome]
Taxonomy Bacteria; Actinobacteria; Actinobacteridae; Bifidobacteriales; Bifidobacteriaceae; Bifidobacterium.
Protein existence 1: Evidence at protein level;
References
[1]
 NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-40 AND 315-320.
DOI=10.1016/0378-1119(89)90476-9; PubMed=2695396 [NCBI, ExPASy, EBI, Israel, Japan]
Minowa T., Iwata S., Sakai H., Masaki H., Ohta T.;
"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.";
Gene 85:161-168(1989).
[2]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=NCC 2705;
DOI=10.1073/pnas.212527599; PubMed=12381787 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"The genome sequence of Bifidobacterium longum reflects its adaptation to the human gastrointestinal tract.";
Proc. Natl. Acad. Sci. U.S.A. 99:14422-14427(2002).
[3]
 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;
Roy D., Sirois S.;
Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases.
[4]
 X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH NAD.
STRAIN=AM 101-2;
DOI=10.1006/jmbi.1993.1122; PubMed=8450537 [NCBI, ExPASy, EBI, Israel, Japan]
Iwata S., Ohta T.;
"Molecular basis of allosteric activation of bacterial L-lactate dehydrogenase.";
J. Mol. Biol. 230:21-27(1993).
[5]
 X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH NAD.
STRAIN=AM 101-2;
DOI=10.1038/nsb0394-176; PubMed=7656036 [NCBI, ExPASy, EBI, Israel, Japan]
Iwata S., Kamata K., Yoshida S., Ohta T.;
"T and R states in the crystals of bacterial L-lactate dehydrogenase reveal the mechanism for allosteric control.";
Nat. Struct. Biol. 1:176-185(1994).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
M33585; AAA22900.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AE014295; AAN25108.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF261669; AAF70510.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF261670; AAF70511.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR JQ0183; JQ0183.
RefSeq NP_696472.1; -.
3D structure databases
PDB
1LLD; X-ray; 2.00 A; A/B=1-320.[ExPASy / RCSB / EBI]
1LTH; X-ray; 2.50 A; R/T=1-320.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1LLD; -.
1LTH; -.
ModBase P19869.
Enzyme and pathway databases
BioCyc BLON206672:BL1308-MON; -.
MetaCyc:MON-13065; -.
Ontologies
GO
GO:0005737; Cellular component: cytoplasm (inferred from electronic annotation from HAMAP).
GO:0004459; Molecular function: L-lactate dehydrogenase activity (inferred from electronic annotation from HAMAP).
GO:0019642; Biological process: anaerobic glycolysis (inferred from electronic annotation from HAMAP).
QuickGo view.
Family and domain databases
HAMAP MF_00488; -; 1.
PBIL [Tree]
InterPro IPR001557; L-lactate/malate_DHase.
IPR011304; L-lactate_DHase.
IPR001236; Lactate/malate_DHase.
IPR015955; Lactate_DHase/Glyco_Ohase_4_C.
IPR016040; NAD(P)-bd.
Graphical view of domain structure.
Gene3D G3DSA:3.90.110.10; lact_mal_DH; 1.
G3DSA:3.40.50.720; NAD(P)-bd; 1.
Pfam PF02866; Ldh_1_C; 1.
PF00056; Ldh_1_N; 1.
Pfam graphical view of domain structure.
PIRSF PIRSF000102; Lac_mal_DH; 1.
TIGRFAMs TIGR01771; L-LDH-NAD; 1.
PROSITE PS00064; L_LDH; 1.
BLOCKS P19869.
Genome annotation databases
GeneID 1022790; -.
GenomeReviews AE014295_GR; BL1308.
KEGG blo:BL1308; -.
Phylogenomic databases
HOGENOM P19869; -.
Other
LinkHub P19869; -.
Genome annotation databases
CMR P19869; BL1308.
Other
ProtoNet P19869.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Complete proteome; Cytoplasm; Direct protein sequencing; Glycolysis; NAD; Oxidoreductase; Phosphoprotein.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
INIT_MET   1     1        Removed. 
CHAIN   2   320  319     L-lactate dehydrogenase 2. PRO_0000168331
NP_BIND   17    45  29     NAD. 
NP_BIND   159   176  18     NAD. 
ACT_SITE   181   181        Proton acceptor. 
BINDING   87    87        NAD (By similarity). 
BINDING   94    94        Substrate (By similarity). 
BINDING   126   126        NAD or substrate (By similarity). 
BINDING   157   157        Substrate (By similarity). 
BINDING   237   237        Substrate (By similarity). 
MOD_RES   228   228        Phosphotyrosine (By similarity). 
STRAND   10    14  5      
HELIX   18    29  12      
STRAND   34    39  6      
HELIX   43    55  13      
HELIX   56    59  4      
STRAND   64    69  6      
HELIX   71    74  4      
STRAND   78    82  5      
HELIX   94   115  22      
STRAND   119   123  5      
HELIX   128   139  12      
STRAND   145   148  4      
HELIX   152   166  15      
HELIX   170   172  3      
STRAND   177   182  6      
HELIX   199   201  3      
HELIX   213   231  19      
HELIX   239   253  15      
STRAND   258   265  8      
STRAND   267   269  3      
STRAND   274   284  11      
STRAND   287   289  3      
HELIX   298   316  19      
TURN   317   319  3      
Sequence information
Length: 320 AA [This is the length of the unprocessed precursor] Molecular weight: 34240 Da [This is the MW of the unprocessed precursor] CRC64: D3E092AA9C353C4E [This is a checksum on the sequence] 
        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
P19869 in FASTA format

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