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UniProtKB/Swiss-Prot entry Q057Y0

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

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Entry information
Entry name DAPB_BUCCC
Primary accession number Q057Y0
Secondary accession numbers None
Integrated into Swiss-Prot on February 5, 2008
Sequence was last modified on November 14, 2006 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 18)
Name and origin of the protein
Protein name Dihydrodipicolinate reductase
Synonyms DHPR
EC 1.3.1.26
Gene name
Name: dapB
OrderedLocusNames: BCc_092
From
Buchnera aphidicola subsp. Cinara cedri [TaxID: 372461] [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.1130441; PubMed=17038625 [NCBI, ExPASy, EBI, Israel, Japan]
Perez-Brocal V., Gil R., Ramos S., Lamelas A., Postigo M., Michelena J.M., Silva F.J., Moya A., Latorre A.;
"A small microbial genome: the end of a long symbiotic relationship?";
Science 314:312-313(2006).
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
CP000263; ABJ90569.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq YP_802662.1; -.
3D structure databases
ModBase Q057Y0.
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 Q057Y0.
Genome annotation databases
GeneID 4440637; -.
GenomeReviews CP000263_GR; BCc_092.
KEGG bcc:BCc_092; -.
CMR Q057Y0; BCc_092.
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_1000057680
Sequence information
Length: 273 AA [This is the length of the unprocessed precursor] Molecular weight: 31312 Da [This is the MW of the unprocessed precursor] CRC64: 755D18EC24F37736 [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MKNKTKIIIS GALGRMGKIL IKETKKNKLI KLVYALINNN IDIKNHNQFY KVKEKKKFIT 

        70         80         90        100        110        120 
LNNLKKKKKI LKFDTIIDFS SPKYSIKIIK YCLKNNKKIV LGTTGFNTEQ IKIINNASKK 

       130        140        150        160        170        180 
IPIIYSPNFS IGINIIYKIL KNISKILGKN SDIEIIESHH RNKIDAPSGT ALQLGKIISK 

       190        200        210        220        230        240 
SMKWNFKKSA IFSRYGNIGI RKKKRIGFST IREGNTIGEH TVLFSNKYEK ISIFHKAIHR 

       250        260        270 
SVFAKGALKA AIWISRKKNG LYNMSDMLKK IKI
Q057Y0 in FASTA format

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