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UniProtKB/Swiss-Prot entry Q81FP4


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

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Entry information
Entry name DAPB_BACCR
Primary accession number Q81FP4
Secondary accession numbers None
Integrated into Swiss-Prot on December 15, 2003
Sequence was last modified on June 1, 2003 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 39)
Name and origin of the protein
Protein name Dihydrodipicolinate reductase
Synonyms DHPR
EC 1.3.1.26
Gene name
Name: dapB
OrderedLocusNames: BC_1532
From
Bacillus cereus (strain ATCC 14579 / DSM 31) [TaxID: 226900] [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=10.1038/nature01582; PubMed=12721630 [NCBI, ExPASy, EBI, Israel, Japan]
Ivanova N., Sorokin A., Anderson I., Galleron N., Candelon B., Kapatral V., Bhattacharyya A., Reznik G., Mikhailova N., Lapidus A., Chu L., Mazur M., Goltsman E., Larsen N., D'Souza M., Walunas T., Grechkin Y., Pusch G., Haselkorn R., Fonstein M., Ehrlich S.D., Overbeek R., Kyrpides N.C.;
"Genome sequence of Bacillus cereus and comparative analysis with Bacillus anthracis.";
Nature 423:87-91(2003).
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
AE016877; AAP08512.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_831311.1; -.
3D structure databases
HSSP P04036; 1DRW. [HSSP ENTRY / PDB]
ModBase Q81FP4.
Enzyme and pathway databases
BioCyc BCER226900:BC_1532-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.
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 Q81FP4.
Genome annotation databases
GeneID 1203881; -.
GenomeReviews AE016877_GR; BC_1532.
KEGG bce:BC1532; -.
Phylogenomic databases
HOGENOM Q81FP4; -.
Genome annotation databases
CMR Q81FP4; BC_1532.
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_0000141409
Sequence information
Length: 266 AA [This is the length of the unprocessed precursor] Molecular weight: 29197 Da [This is the MW of the unprocessed precursor] CRC64: C945C50657245F8F [This is a checksum on the sequence]
        10         20         30         40         50         60 
MKEIKVIIAG PRGRMGHEAV LLMERTEHFN LVAAVDYKHG GEKISDLPGM PALHAPIYAD 

        70         80         90        100        110        120 
LHTCLDEVEA DVLLDLTTPE VGKQHVTLAV ERGLRSVIGT TGFTEEELTR LTENAKEKAV 

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

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

       250        260 
MSGVKLSIET VMNLDHLVYG LENIID 

Q81FP4 in FASTA format

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BLAST logo BLAST submission on ExPASy/SIB
or at NCBI (USA)
Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
PROSITE logo ScanProsite, MotifScan SWISS-MODEL Submit a homology modeling request to SWISS-MODEL
NPSA logo NPSA Sequence analysis tools

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