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UniProtKB/Swiss-Prot entry Q92F65


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

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Entry information
Entry name LDH1_LISIN
Primary accession number Q92F65
Secondary accession number Q8VTS6
Integrated into Swiss-Prot on January 23, 2002
Sequence was last modified on December 1, 2001 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 53)
Name and origin of the protein
Protein name L-lactate dehydrogenase 1
Synonyms L-LDH 1
EC 1.1.1.27
Gene name
Name: ldh1
Synonyms: ldh
OrderedLocusNames: lin0242
From
Listeria innocua [TaxID: 1642] [HAMAP proteome]
Taxonomy Bacteria; Firmicutes; Bacillales; Listeriaceae; Listeria.
Protein existence 3: Inferred from homology;
References
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=CLIP 11262 / Serovar 6a;
DOI=10.1126/science.1063447; PubMed=11679669 [NCBI, ExPASy, EBI, Israel, Japan]
Glaser P., Frangeul L., Buchrieser C., Rusniok C., Amend A., Baquero F., Berche P., Bloecker H., Brandt P., Chakraborty T., Charbit A., Chetouani F., Couve E., de Daruvar A., Dehoux P., Domann E., Dominguez-Bernal G., Duchaud E., Durant L., Dussurget O., Entian K.-D., Fsihi H., Garcia-del Portillo F., Garrido P., Gautier L., Goebel W., Gomez-Lopez N., Hain T., Hauf J., Jackson D., Jones L.-M., Kaerst U., Kreft J., Kuhn M., Kunst F., Kurapkat G., Madueno E., Maitournam A., Mata Vicente J., Ng E., Nedjari H., Nordsiek G., Novella S., de Pablos B., Perez-Diaz J.-C., Purcell R., Remmel B., Rose M., Schlueter T., Simoes N., Tierrez A., Vazquez-Boland J.-A., Voss H., Wehland J., Cossart P.;
"Comparative genomics of Listeria species.";
Science 294:849-852(2001).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 223-313.
STRAIN=dd644;
DOI=10.1007/s002840010300; PubMed=11683362 [NCBI, ExPASy, EBI, Israel, Japan]
Cai S., Wiedmann M.;
"Characterization of the prfA virulence gene cluster insertion site in non-hemolytic Listeria spp.: probing the evolution of the Listeria virulence gene island.";
Curr. Microbiol. 43:271-277(2001).
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
AL596164; CAC95475.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF322004; AAL36598.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR AC1463; AC1463.
RefSeq NP_469587.1; -.
3D structure databases
HSSP P00344; 2LDB. [HSSP ENTRY / PDB]
ModBase Q92F65.
Enzyme and pathway databases
BioCyc LINN272626:LIN0242-MON; -.
Organism-specific databases
ListiList LIN00242; -.
Ontologies
GO
GO:0005737; Cellular component: cytoplasm (inferred from electronic annotation from HAMAP).
GO:0005488; Molecular function: binding (inferred from electronic annotation from InterPro).
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).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
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.
PRINTS PR00086; LLDHDRGNASE.
TIGRFAMs TIGR01771; L-LDH-NAD; 1.
PROSITE PS00064; L_LDH; 1.
ProtoNet Q92F65.
Genome annotation databases
GeneID 1128650; -.
GenomeReviews AL592022_GR; lin0242.
KEGG lin:lin0242; -.
NMPDR fig|272626.1.peg.240; -.
Phylogenomic databases
HOGENOM Q92F65; -.
Genome annotation databases
CMR Q92F65; lin0242.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Complete proteome; Cytoplasm; Glycolysis; NAD; Oxidoreductase; Phosphoprotein.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   313  313     L-lactate dehydrogenase 1. PRO_0000168361
NP_BIND   13    41  29     NAD (By similarity). 
ACT_SITE   176   176        Proton acceptor (By similarity). 
BINDING   89    89        Substrate (By similarity). 
BINDING   121   121        NAD or substrate (By similarity). 
BINDING   152   152        Substrate (By similarity). 
BINDING   227   227        Substrate (By similarity). 
MOD_RES   218   218        Phosphotyrosine (By similarity). 
CONFLICT   223   223        K -> L (in Ref. 2; AAL36598). 
Sequence information
Length: 313 AA [This is the length of the unprocessed precursor] Molecular weight: 34218 Da [This is the MW of the unprocessed precursor] CRC64: E95D336CB317E4C1 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MKDHQKIILV GDGAVGSSYA FACVNLSIGQ EFGIIDIDKD RTIGDAMDLS HAVPFSTPKK 

        70         80         90        100        110        120 
IYSANYSDCH DADLVVVTAG TAQKPGETRL DLVNRNIKIM KGIVDEVMAS GFDGIFLIAS 

       130        140        150        160        170        180 
NPVDILTYAT WKFSGLPKER VIGSGTSLDT ARFRMSIADY LKVDARNVHG YILGEHGDTQ 

       190        200        210        220        230        240 
FPAWSHTTVG GLPITEWINE DEQGAMDTIF VSVRDAAYEI INKKGATFYG VAAALARITK 

       250        260        270        280        290        300 
AILNNENAIL PLSVYLDGHY GMNDIYIGAP AVVNRQGVRH IVEMNLNDKE KEQMKNSADT 

       310 
LKKVLDDAMK QID 

Q92F65 in FASTA format

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