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UniProtKB/Swiss-Prot entry Q8K9Z5

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

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Entry information
Entry name DAPB_BUCAP
Primary accession number Q8K9Z5
Secondary accession numbers None
Integrated into Swiss-Prot on November 8, 2002
Sequence was last modified on October 1, 2002 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 47)
Name and origin of the protein
Protein name Dihydrodipicolinate reductase
Synonyms DHPR
EC 1.3.1.26
Gene name
Name: dapB
OrderedLocusNames: BUsg_139
From
Buchnera aphidicola subsp. Schizaphis graminum [TaxID: 98794] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; Enterobacteriaceae; Buchnera.
Protein existence 3: Inferred from homology;
References
[1]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1126/science.1071278; PubMed=12089438 [NCBI, ExPASy, EBI, Israel, Japan]
Tamas I., Klasson L., Canbaeck B., Naeslund A.K., Eriksson A.-S., Wernegreen J.J., Sandstroem J.P., Moran N.A., Andersson S.G.E.;
"50 million years of genomic stasis in endosymbiotic bacteria.";
Science 296:2376-2379(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
AE013218; AAM67707.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_660496.1; -.
3D structure databases
HSSP P04036; 1DRW. [HSSP ENTRY / PDB]
ModBase Q8K9Z5.
Enzyme and pathway databases
BioCyc BAPH198804:BUSG139-MON; -.
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:0008839; Molecular function: dihydrodipicolinate reductase activity (inferred from electronic annotation from HAMAP).
GO:0019877; Biological process: diaminopimelate biosynthetic process (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_00102; -; 1.
PBIL [Tree]
InterPro IPR000846; DapB.
IPR011770; DapB_bac/pln.
IPR016040; NAD(P)-bd.
Graphical view of domain structure.
Gene3D G3DSA:3.40.50.720; NAD(P)-bd; 1.
PANTHER PTHR20836; DapB_bac/pln; 1.
Pfam PF05173; DapB_C; 1.
PF01113; DapB_N; 1.
Pfam graphical view of domain structure.
ProDom PD004105; DapB; 1.
[Domain structure / List of seq. sharing at least 1 domain]
TIGRFAMs TIGR00036; dapB; 1.
PROSITE PS01298; DAPB; 1.
ProtoNet Q8K9Z5.
Genome annotation databases
GeneID 1005956; -.
GenomeReviews AE013218_GR; BUsg_139.
KEGG bas:BUsg139; -.
Phylogenomic databases
HOGENOM Q8K9Z5; -.
Genome annotation databases
CMR Q8K9Z5; BUsg_139.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Amino-acid biosynthesis; Complete proteome; Cytoplasm; Diaminopimelate biosynthesis; Lysine biosynthesis; NADP; Oxidoreductase.
Features
SEVIEWER logo Feature table viewer
KeyFrom To Length Description FTId
CHAIN   1   273  273     Dihydrodipicolinate reductase. PRO_0000141420
Sequence information
Length: 273 AA [This is the length of the unprocessed precursor] Molecular weight: 30674 Da [This is the MW of the unprocessed precursor] CRC64: E49AD0EADB67042F [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MKKKITRIAI TGAMGRMGQV LIKEIQKNKN TVLTAALVKN NHPLIGQNIG EKIGIGKTSV 

        70         80         90        100        110        120 
SISSDINIEK NDFDVLIDFT KPSGTFYFLE QCYEFKKNMI IGTTGFSEKE IKTINSYAKK 

       130        140        150        160        170        180 
IALIKASNFS IGINLLYQLI QKTTKILGNT SDIDIIEYHH RNKIDIPSGT ALSIGENISK 

       190        200        210        220        230        240 
VMNWELNKHS LYYTKGITKK IRETKKIGFS SIRSGNIIGK HTVLFSSSDE EIKITHSAFN 

       250        260        270 
RESFAKGAIE AAVWIHEKKH GLFNMNDILK DKF
Q8K9Z5 in FASTA format

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