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UniProtKB/Swiss-Prot entry Q73AW1

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

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Entry information
Entry name DAPB_BACC1
Primary accession number Q73AW1
Secondary accession numbers None
Integrated into Swiss-Prot on March 21, 2006
Sequence was last modified on July 5, 2004 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 35)
Name and origin of the protein
Protein name Dihydrodipicolinate reductase
Synonyms DHPR
EC 1.3.1.26
Gene name
Name: dapB
OrderedLocusNames: BCE_1661
From
Bacillus cereus (strain ATCC 10987) [TaxID: 222523] [HAMAP proteome]
Taxonomy Bacteria; Firmicutes; Bacillales; Bacillaceae; Bacillus; Bacillus cereus group.
Protein existence 3: Inferred from homology;
References
[1]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1093/nar/gkh258; PubMed=14960714 [NCBI, ExPASy, EBI, Israel, Japan]
Rasko D.A., Ravel J., Oekstad O.A., Helgason E., Cer R.Z., Jiang L., Shores K.A., Fouts D.E., Tourasse N.J., Angiuoli S.V., Kolonay J.F., Nelson W.C., Kolstoe A.-B., Fraser C.M., Read T.D.;
"The genome sequence of Bacillus cereus ATCC 10987 reveals metabolic adaptations and a large plasmid related to Bacillus anthracis pXO1.";
Nucleic Acids Res. 32:977-988(2004).
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
AE017194; AAS40590.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_977982.1; -.
3D structure databases
ModBase Q73AW1.
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.
Graphical view of domain structure.
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 Q73AW1.
Genome annotation databases
GeneID 2747880; -.
GenomeReviews AE017194_GR; BCE_1661.
KEGG bca:BCE_1661; -.
NMPDR fig|222523.1.peg.1654; -.
TIGR BCE_1661; -.
Phylogenomic databases
HOGENOM Q73AW1; -.
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   266  266     Dihydrodipicolinate reductase. PRO_0000228321
Sequence information
Length: 266 AA [This is the length of the unprocessed precursor] Molecular weight: 29263 Da [This is the MW of the unprocessed precursor] CRC64: 4ACFF04A1302DE94 [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MKEIKVIIAG PRGRMGHEAV LLMERTEHFN LVAAVDYKHG GEKISDLPGM PALDTPIYAD 

        70         80         90        100        110        120 
LHTCLEEVEA DVLLDLTTPE VGKQHVTLAV ERGLRSVIGT TGFTEEELKQ LTETAKEKAV 

       130        140        150        160        170        180 
GTIIAPNFAI GAVLMMKFSQ MAAKYFQDVE VIELHHDQKL DAPSGTAVKT VELIRQNRES 

       190        200        210        220        230        240 
KQQGHPNEVE QLKGARGANV DGIHIHSVRL PGLIAHQEVM FGGDGQMLTV RHDSFNRASF 

       250        260 
MSGVKLSIET VMNLDHLVYG LENIID
Q73AW1 in FASTA format

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