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UniProtKB/Swiss-Prot entry A5FXD9

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

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Entry information
Entry name DAPB_ACICJ
Primary accession number A5FXD9
Secondary accession numbers None
Integrated into Swiss-Prot on January 15, 2008
Sequence was last modified on June 12, 2007 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 14)
Name and origin of the protein
Protein name Dihydrodipicolinate reductase
Synonyms DHPR
EC 1.3.1.26
Gene name
Name: dapB
OrderedLocusNames: Acry_1055
From
Acidiphilium cryptum (strain JF-5) [TaxID: 349163] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales; Acetobacteraceae; Acidiphilium.
Protein existence 3: Inferred from homology;
References
[1]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Sims D., Brettin T., Bruce D., Han C., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Magnuson T., Richardson P.;
"Complete sequence of chromosome of Acidiphilium cryptum JF-5.";
Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases.
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
CP000697; ABQ30271.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq YP_001234190.1; -.
3D structure databases
ModBase A5FXD9.
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.
Genome annotation databases
GeneID 5162498; -.
GenomeReviews CP000697_GR; Acry_1055.
KEGG acr:Acry_1055; -.
CMR A5FXD9; Acry_1055.
Other
ProtoNet A5FXD9.
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   247  247     Dihydrodipicolinate reductase. PRO_1000008529
Sequence information
Length: 247 AA [This is the length of the unprocessed precursor] Molecular weight: 25070 Da [This is the MW of the unprocessed precursor] CRC64: CB148C8846410468 [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MNGADLRIGI AGITGRMGKL LAEAVPLAGA TLAGGIGRDG DLAALARESD VVIDFTVAAT 

        70         80         90        100        110        120 
VSRHAGILAA AGTPWVLGTT GFDPAAEADI ADAAARIPVF QAANFAPGVN LVIALAERLG 

       130        140        150        160        170        180 
ATLAAETHDA EILEMHHRQK IDAPSGTALA IGAAVARGRG VDLAAVKDSG RDGHTGKRET 

       190        200        210        220        230        240 
GAIGFAALRG GQIVGSHSAI FTSAVEQITL THHALDRRIF AEGAVRAALW LAGRAPGRYG 


MRDLLGL
A5FXD9 in FASTA format

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