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UniProtKB/Swiss-Prot entry P26297


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

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Entry information
Entry name LDHD_LACDA
Primary accession number P26297
Secondary accession number Q1G7V7
Integrated into Swiss-Prot on May 1, 1992
Sequence was last modified on January 23, 2007 (Sequence version 3)
Annotations were last modified on    September 2, 2008 (Entry version 74)
Name and origin of the protein
Protein name D-lactate dehydrogenase
Synonyms D-LDH
EC 1.1.1.28
D-specific D-2-hydroxyacid dehydrogenase
Gene name
Name: ldhA
OrderedLocusNames: Ldb0101
From
Lactobacillus delbrueckii subsp. bulgaricus (strain ATCC 11842 / DSM 20081) [TaxID: 390333] [HAMAP proteome]
Taxonomy Bacteria; Firmicutes; Lactobacillales; Lactobacillaceae; Lactobacillus.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
DOI=10.1016/0014-5793(91)81226-X; PubMed=1915894 [NCBI, ExPASy, EBI, Israel, Japan]
Bernard N., Ferain T., Garmyn D., Hols P., Delcour J.;
"Cloning of the D-lactate dehydrogenase gene from Lactobacillus delbrueckii subsp. bulgaricus by complementation in Escherichia coli.";
FEBS Lett. 290:61-64(1991).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
PubMed=1569100 [NCBI, ExPASy, EBI, Israel, Japan]
Kochhar S., Hunziker P., Leong-Morgenthaler P.M., Hottinger H.;
"Primary structure, physicochemical properties, and chemical modification of NAD(+)-dependent D-lactate dehydrogenase. Evidence for the presence of Arg-235, His-303, Tyr-101, and Trp-19 at or near the active site.";
J. Biol. Chem. 267:8499-8513(1992).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
DOI=10.1016/0006-291X(92)91683-H; PubMed=1610363 [NCBI, ExPASy, EBI, Israel, Japan]
Kochhar S., Chuard N., Hottinger H.;
"Cloning and overexpression of the Lactobacillus bulgaricus NAD(+)-dependent D-lactate dehydrogenase gene in Escherichia coli: purification and characterization of the recombinant enzyme.";
Biochem. Biophys. Res. Commun. 185:705-712(1992).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1073/pnas.0603024103; PubMed=16754859 [NCBI, ExPASy, EBI, Israel, Japan]
van de Guchte M., Penaud S., Grimaldi C., Barbe V., Bryson K., Nicolas P., Robert C., Oztas S., Mangenot S., Couloux A., Loux V., Dervyn R., Bossy R., Bolotin A., Batto J.-M., Walunas T., Gibrat J.-F., Bessieres P., Weissenbach J., Ehrlich S.D., Maguin E.;
"The complete genome sequence of Lactobacillus bulgaricus reveals extensive and ongoing reductive evolution.";
Proc. Natl. Acad. Sci. U.S.A. 103:9274-9279(2006).
[5]
SIMILARITY TO OTHER ENZYMES OF THIS FAMILY.
DOI=10.1016/0006-291X(92)91157-L; PubMed=1567457 [NCBI, ExPASy, EBI, Israel, Japan]
Kochhar S., Hunziker P., Leong-Morgenthaler P.M., Hottinger H.;
"Evolutionary relationship of NAD(+)-dependent D-lactate dehydrogenase: comparison of primary structure of 2-hydroxy acid dehydrogenases.";
Biochem. Biophys. Res. Commun. 184:60-66(1992).
[6]
MUTAGENESIS OF HIS-206; ARG-236; ASP-260; GLU-265 AND HIS-297.
PubMed=9063466 [NCBI, ExPASy, EBI, Israel, Japan]
Bernard N., Johnsen K., Gelpi J.L., Alvarez J.A., Ferain T., Garmyn D., Hols P., Cortes A., Clarke A.R., Holbrook J.J., Delcour J.;
"D-2-hydroxy-4-methylvalerate dehydrogenase from Lactobacillus delbrueckii subsp. bulgaricus. II. Mutagenic analysis of catalytically important residues.";
Eur. J. Biochem. 244:213-219(1997).
[7]
3D-STRUCTURE MODELING.
DOI=10.1006/bbrc.1993.1398; PubMed=8476420 [NCBI, ExPASy, EBI, Israel, Japan]
Vinals C., Depiereux E., Feytmans E.;
"Prediction of structurally conserved regions of D-specific hydroxy acid dehydrogenases by multiple alignment with formate dehydrogenase.";
Biochem. Biophys. Res. Commun. 192:182-188(1993).
[8]
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH NADH, AND SUBUNIT.
DOI=10.1016/S0022-2836(02)00086-4; PubMed=12054772 [NCBI, ExPASy, EBI, Israel, Japan]
Razeto A., Kochhar S., Hottinger H., Dauter M., Wilson K.S., Lamzin V.S.;
"Domain closure, substrate specificity and catalysis of D-lactate dehydrogenase from Lactobacillus bulgaricus.";
J. Mol. Biol. 318:109-119(2002).
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
X60220; CAA42781.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M85224; AAA25246.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
CR954253; CAI96942.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A38094; A38094.
RefSeq YP_618304.1; -.
3D structure databases
PDB
1DLD; Model; -; A=1-333.[ExPASy / RCSB / EBI]
1J49; X-ray; 2.20 A; A/B=1-333.[ExPASy / RCSB / EBI]
1J4A; X-ray; 1.90 A; A/B/C/D=1-333.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1DLD; -.
1J49; -.
1J4A; -.
ModBase P26297.
Enzyme and pathway databases
BioCyc LDEL390333:LDB0101-MON; -.
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 P26297.
Genome annotation databases
GeneID 4085369; -.
GenomeReviews CR954253_GR; Ldb0101.
KEGG ldb:Ldb0101; -.
Phylogenomic databases
HOGENOM P26297; -.
Other
LinkHub P26297; -.
Genome annotation databases
CMR P26297; Ldb0101.
Other
ProtoNet P26297.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Complete proteome; Direct protein sequencing; NAD; Oxidoreductase.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
INIT_MET   1     1        Removed. 
CHAIN   2   333  332     D-lactate dehydrogenase. PRO_0000075953
NP_BIND   153   179  27     NADH. 
ACT_SITE   236   236         
ACT_SITE   265   265         
ACT_SITE   297   297        Proton donor. 
MUTAGEN   206   206        H->Q: Increase of activity. 
MUTAGEN   236   236        R->K: Decrease of activity. 
MUTAGEN   260   260        D->N: Decrease of activity. 
MUTAGEN   265   265        E->Q: Decrease of activity. 
MUTAGEN   297   297        H->Q: 90% loss of activity. 
CONFLICT   41    41        V -> A (in Ref. 2; AAA25246). 
CONFLICT   117   117        R -> A (in Ref. 1; CAA42781). 
CONFLICT   122   122        D -> A (in Ref. 2; AAA25246). 
CONFLICT   152   152        I -> V (in Ref. 2; AAA25246). 
CONFLICT   174   174        A -> T (in Ref. 1; CAA42781). 
CONFLICT   220   220        E -> K (in Ref. 2; AAA25246). 
CONFLICT   254   254        I -> V (in Ref. 2; AAA25246). 
CONFLICT   268   268        I -> V (in Ref. 2; AAA25246). 
CONFLICT   273   273        W -> R (in Ref. 2; AAA25246). 
STRAND   3     6  4      
HELIX   11    13  3      
HELIX   14    22  9      
STRAND   27    31  5      
TURN   38    40  3      
HELIX   41    44  4      
STRAND   48    52  5      
HELIX   60    67  8      
TURN   68    70  3      
STRAND   73    79  7      
HELIX   86    92  7      
STRAND   95    97  3      
HELIX   104   119  16      
HELIX   122   130  9      
HELIX   144   146  3      
STRAND   147   152  6      
HELIX   156   167  12      
STRAND   171   175  5      
HELIX   181   186  6      
HELIX   193   199  7      
STRAND   201   205  5      
TURN   211   215  5      
HELIX   219   224  6      
STRAND   229   233  5      
HELIX   237   239  3      
HELIX   242   250  9      
STRAND   254   260  7      
TURN   266   270  5      
HELIX   281   288  8      
STRAND   292   294  3      
HELIX   303   321  19      
STRAND   327   329  3      
Sequence information
Length: 333 AA [This is the length of the unprocessed precursor] Molecular weight: 37049 Da [This is the MW of the unprocessed precursor] CRC64: 16E8B68D54B9D9D4 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MTKIFAYAIR EDEKPFLKEW EDAHKDVEVE YTDKLLTPET VALAKGADGV VVYQQLDYTA 

        70         80         90        100        110        120 
ETLQALADNG ITKMSLRNVG VDNIDMAKAK ELGFQITNVP VYSPNAIAEH AAIQAARILR 

       130        140        150        160        170        180 
QDKAMDEKVA RHDLRWAPTI GREVRDQVVG VIGTGHIGQV FMQIMEGFGA KVIAYDIFRN 

       190        200        210        220        230        240 
PELEKKGYYV DSLDDLYKQA DVISLHVPDV PANVHMINDE SIAKMKQDVV IVNVSRGPLV 

       250        260        270        280        290        300 
DTDAVIRGLD SGKIFGYAMD VYEGEVGIFN EDWEGKEFPD ARLADLIARP NVLVTPHTAF 

       310        320        330 
YTTHAVRNMV VKAFDNNLEL VEGKEAETPV KVG 

P26297 in FASTA format

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