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UniProtKB/Swiss-Prot entry Q2IGX0

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

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Entry information
Entry name DAPB_ANADE
Primary accession number Q2IGX0
Secondary accession numbers None
Integrated into Swiss-Prot on January 15, 2008
Sequence was last modified on March 7, 2006 (Sequence version 1)
Annotations were last modified on    July 22, 2008 (Entry version 20)
Name and origin of the protein
Protein name Dihydrodipicolinate reductase
Synonyms DHPR
EC 1.3.1.26
Gene name
Name: dapB
OrderedLocusNames: Adeh_4068
From
Anaeromyxobacter dehalogenans (strain 2CP-C) [TaxID: 290397] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales; Cystobacterineae; Myxococcaceae; Anaeromyxobacter.
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 T., Hammon N., Israni S., Pitluck S., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Kiss H., Schmutz J., Larimer F., Land M., Kyrpides N., Anderson I., Sanford R.A., Ritalahti K.M., Thomas H.S., Kirby J.R., Zhulin I.B., Loeffler F.E., Richardson P.;
"Complete sequence of Anaeromyxobacter dehalogenans 2CP-C.";
Submitted (JAN-2006) 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
CP000251; ABC83832.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq YP_467269.1; -.
3D structure databases
ModBase Q2IGX0.
Enzyme and pathway databases
BioCyc ADEH290397:ADEH_4068-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.
IPR016040; NAD(P)-bd.
Graphical view of domain structure.
Gene3D G3DSA:3.40.50.720; NAD(P)-bd; 2.
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.
BLOCKS Q2IGX0.
Genome annotation databases
GeneID 3888259; -.
GenomeReviews CP000251_GR; Adeh_4068.
KEGG ade:Adeh_4068; -.
Phylogenomic databases
HOGENOM Q2IGX0; -.
Genome annotation databases
CMR Q2IGX0; Adeh_4068.
Other
ProtoNet Q2IGX0.
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   270  270     Dihydrodipicolinate reductase. PRO_1000008532
Sequence information
Length: 270 AA [This is the length of the unprocessed precursor] Molecular weight: 27724 Da [This is the MW of the unprocessed precursor] CRC64: AB021B5366761657 [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MTKVVVTGAA GRMGTQIVRL VRATPGLSVS GAVERAGSPA IGKDAGTLAG GEPLGVAVVD 

        70         80         90        100        110        120 
DLAKALPGAD VVIDFTSHEA SVRHAQACAA AGVALVIGST GFTPDAKAKV AEAARKVPVV 

       130        140        150        160        170        180 
LSPNMSVGVN VVFELVRQAA RVLGDAYDVE VVEIHHKHKR DAPSGTAVRL GEVAAEALGR 

       190        200        210        220        230        240 
APADALAYSR HGILGERPPW QIGIQTLRGG DVVGEHTVFF CGEGERVEIT HRATSREQFA 

       250        260        270 
RGAARAAAWL PGKAPGVYDM ADVLGLRGGK
Q2IGX0 in FASTA format

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