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UniProtKB/Swiss-Prot entry Q822G7

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

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Entry information
Entry name DAPB_CHLCV
Primary accession number Q822G7
Secondary accession numbers None
Integrated into Swiss-Prot on August 22, 2003
Sequence was last modified on June 1, 2003 (Sequence version 1)
Annotations were last modified on    July 22, 2008 (Entry version 33)
Name and origin of the protein
Protein name Dihydrodipicolinate reductase
Synonyms DHPR
EC 1.3.1.26
Gene name
Name: dapB
OrderedLocusNames: CCA_00715
From
Chlamydophila caviae [TaxID: 83557] [HAMAP proteome]
Taxonomy Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae; Chlamydophila.
Protein existence 3: Inferred from homology;
References
[1]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=GPIC;
DOI=10.1093/nar/gkg321; PubMed=12682364 [NCBI, ExPASy, EBI, Israel, Japan]
Read T.D., Myers G.S.A., Brunham R.C., Nelson W.C., Paulsen I.T., Heidelberg J.F., Holtzapple E.K., Khouri H.M., Federova N.B., Carty H.A., Umayam L.A., Haft D.H., Peterson J.D., Beanan M.J., White O., Salzberg S.L., Hsia R.-C., McClarty G., Rank R.G., Bavoil P.M., Fraser C.M.;
"Genome sequence of Chlamydophila caviae (Chlamydia psittaci GPIC): examining the role of niche-specific genes in the evolution of the Chlamydiaceae.";
Nucleic Acids Res. 31:2134-2147(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
AE015925; AAP05457.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_829579.1; -.
3D structure databases
HSSP P04036; 1DRW. [HSSP ENTRY / PDB]
ModBase Q822G7.
Enzyme and pathway databases
BioCyc CCAV227941:CCA_00715-MON; -.
Ontologies
GO
GO:0005737; Cellular component: cytoplasm (inferred from electronic annotation from HAMAP).
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).
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]
PROSITE PS01298; DAPB; 1.
BLOCKS Q822G7.
Genome annotation databases
GeneID 1218400; -.
GenomeReviews AE015925_GR; CCA_00715.
KEGG cca:CCA00715; -.
TIGR CCA_00715; -.
Phylogenomic databases
HOGENOM Q822G7; -.
Other
ProtoNet Q822G7.
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   246  246     Dihydrodipicolinate reductase. PRO_0000141426
Sequence information
Length: 246 AA [This is the length of the unprocessed precursor] Molecular weight: 26756 Da [This is the MW of the unprocessed precursor] CRC64: 8D70D9050278287B [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MRVGIIGCSG RMGTLLSNLL RATARFTLGP GFSRTSTHSL ASVIDNNDVL VDFSSSSLSE 

        70         80         90        100        110        120 
ELFRALLSNP KPLIFATTKP APSSSIDEKI EDLAAYVPVV VCPNTSLGAY VQKRLAALLA 

       130        140        150        160        170        180 
AVFDDAYDIR ITEVHHRGKK DAISGTANEL VSILCDAKKK EWQQEYRVGA DSDSVKNIEL 

       190        200        210        220        230        240 
HASRVGNISG EHEIAFISDK EQITLRHTVF SREVFAEGVL RILDWLLNES PPPGCYGPEV 


GLKVSV
Q822G7 in FASTA format

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