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UniProtKB/Swiss-Prot entry P52643


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

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Entry information
Entry name LDHD_ECOLI
Primary accession number P52643
Secondary accession number P78152
Integrated into Swiss-Prot on October 1, 1996
Sequence was last modified on October 1, 1996 (Sequence version 1)
Annotations were last modified on    July 22, 2008 (Entry version 65)
Name and origin of the protein
Protein name D-lactate dehydrogenase
Synonyms D-LDH
EC 1.1.1.28
Fermentative lactate dehydrogenase
Gene name
Name: ldhA
Synonyms: hslI, htpH
OrderedLocusNames: b1380, JW1375
From
Escherichia coli (strain K12) [TaxID: 83333] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; Enterobacteriaceae; Escherichia.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=K12;
PubMed=9025293 [NCBI, ExPASy, EBI, Israel, Japan]
Bunch P.K., Mat-Jan F., Lee N., Clark D.P.;
"The ldhA gene encoding the fermentative lactate dehydrogenase of Escherichia coli.";
Microbiology 143:187-195(1997).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
DOI=10.1093/dnares/3.6.363; PubMed=9097039 [NCBI, ExPASy, EBI, Israel, Japan]
Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T., Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T., Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S., Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Takeuchi Y., Wada C., Yamamoto Y., Horiuchi T.;
"A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 28.0-40.1 min region on the linkage map.";
DNA Res. 3:363-377(1996).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
DOI=10.1126/science.277.5331.1453; PubMed=9278503 [NCBI, ExPASy, EBI, Israel, Japan]
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.;
"The complete genome sequence of Escherichia coli K-12.";
Science 277:1453-1474(1997).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
DOI=10.1038/msb4100049; PubMed=16738553 [NCBI, ExPASy, EBI, Israel, Japan]
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110.";
Mol. Syst. Biol. 2:E1-E5(2006).
[5]
CHARACTERIZATION AS AN HEAT-SHOCK GENE.
PubMed=8349564 [NCBI, ExPASy, EBI, Israel, Japan]
Chuang S.E., Blattner F.R.;
"Characterization of twenty-six new heat shock genes of Escherichia coli.";
J. Bacteriol. 175:5242-5252(1993).
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
U36928; AAB51772.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U00096; AAC74462.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AP009048; BAA14990.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR G64888; G64888.
RefSeq AP_002007.1; -.
NP_415898.1; -.
3D structure databases
HSSP P30901; 2DLD. [HSSP ENTRY / PDB]
ModBase P52643.
Protein-protein interaction databases
IntAct P52643; -.
Enzyme and pathway databases
BioCyc EcoCyc:DLACTDEHYDROGNAD-MON; -.
2D gel databases
ECO2DBASE D033.4; 6TH EDITION.
Organism-specific databases
EchoBASE EB2978; -.
EcoGene EG13186; ldhA.
Ontologies
GO
GO:0005737; Cellular component: cytoplasm (inferred from direct assay from UniProtKB).
QuickGo view.
Family and domain databases
InterPro IPR006139; D-isomer_2_OHA_DHase.
IPR006140; D-isomer_2_OHA_DHase_NAD-bd.
IPR016040; NAD(P)-bd.
Graphical view of domain structure.
Gene3D G3DSA:3.40.50.720; NAD(P)-bd; 1.
Pfam PF00389; 2-Hacid_dh; 1.
PF02826; 2-Hacid_dh_C; 1.
Pfam graphical view of domain structure.
PROSITE PS00065; D_2_HYDROXYACID_DH_1; 1.
PS00670; D_2_HYDROXYACID_DH_2; 1.
PS00671; D_2_HYDROXYACID_DH_3; 1.
BLOCKS P52643.
Genome annotation databases
GeneID 946315; -.
GenomeReviews U00096_GR; b1380.
AP009048_GR; JW1375.
KEGG ecj:JW1375; -.
eco:b1380; -.
Phylogenomic databases
HOGENOM P52643; -.
Genome annotation databases
CMR P52643; b1380.
Other
ProtoNet P52643.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Complete proteome; NAD; Oxidoreductase; Stress response.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   329  329     D-lactate dehydrogenase. PRO_0000075952
ACT_SITE   234   234        By similarity. 
ACT_SITE   263   263        By similarity. 
ACT_SITE   295   295        Proton donor (By similarity). 
Sequence information
Length: 329 AA [This is the length of the unprocessed precursor] Molecular weight: 36535 Da [This is the MW of the unprocessed precursor] CRC64: EF85419988438D6D [This is a checksum on the sequence]
        10         20         30         40         50         60 
MKLAVYSTKQ YDKKYLQQVN ESFGFELEFF DFLLTEKTAK TANGCEAVCI FVNDDGSRPV 

        70         80         90        100        110        120 
LEELKKHGVK YIALRCAGFN NVDLDAAKEL GLKVVRVPAY DPEAVAEHAI GMMMTLNRRI 

       130        140        150        160        170        180 
HRAYQRTRDA NFSLEGLTGF TMYGKTAGVI GTGKIGVAML RILKGFGMRL LAFDPYPSAA 

       190        200        210        220        230        240 
ALELGVEYVD LPTLFSESDV ISLHCPLTPE NYHLLNEAAF EQMKNGVMIV NTSRGALIDS 

       250        260        270        280        290        300 
QAAIEALKNQ KIGSLGMDVY ENERDLFFED KSNDVIQDDV FRRLSACHNV LFTGHQAFLT 

       310        320 
AEALTSISQT TLQNLSNLEK GETCPNELV 

P52643 in FASTA format

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