NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1038/ng.2007.38; PubMed=18037886 [NCBI, ExPASy, EBI, Israel, Japan]
Saenz H.L., Engel P., Stoeckli M.C., Lanz C., Raddatz G., Vayssier-Taussat M., Birtles R., Schuster S.C., Dehio C.;
"Genomic analysis of Bartonella identifies type IV secretion systems as host adaptability factors.";
Nat. Genet. 39:1469-1476(2007).

Comments

CATALYTIC ACTIVITY: 2,3,4,5-tetrahydrodipicolinate + NAD(P)⁺ = 2,3-dihydrodipicolinate + NAD(P)H.
PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; tetrahydrodipicolinate from L-aspartate: step 4/4 .
SUBCELLULAR LOCATION: Cytoplasm (By similarity).
SIMILARITY: Belongs to the dihydrodipicolinate reductase family.

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

AM260525; CAK02160.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

YP_001610155.1; -.

3D structure databases

ModBase

A9IXE5.

Ontologies

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; 1.

PANTHER

PTHR20836; DapB_bac/pln; 1.

ProDom

PD004105; DapB; 1.
[Domain structure / List of seq. sharing at least 1 domain]

TIGR00036; dapB; 1.

PS01298; DAPB; 1.

Genome annotation databases

GeneID

5829171; -.

GenomeReviews

AM260525_GR; BT1893.

CMR

A9IXE5; BT1893.

Other

ProtoNet

A9IXE5.

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

Feature table viewer

`Key`	`From To`	`Length`		`Description`	`FTId`
`CHAIN`	`1 270`	`270`		`Dihydrodipicolinate reductase.`	`PRO_1000075671`

Sequence information

Length: 270 AA [This is the length of the unprocessed precursor]

Molecular weight: 29152 Da [This is the MW of the unprocessed precursor]

CRC64: 1EC834FEFA66BABA [This is a checksum on the sequence]

        10         20         30         40         50         60 
MRLTVVGANG RMGRELITAI RQRKDVELCA VLVRKNSPFV GKDASVLIGS DSLGIRITDD 

        70         80         90        100        110        120 
PENAFSSTEG IVDFSHPQAS LLYADYAAQK KLVHIIGTTG FSKTEEEKIA EFAKYTTIVK 

       130        140        150        160        170        180 
SGNMSLGINL LANLVKKAAK ALEADDFDIE IYEMHHANKV DAPSGTALLL GQAAAEGRNV 

       190        200        210        220        230        240 
MLQDVRINER NGYTGKREKG SIGFSCSRGG TVIGEHSVIF AGSHERIVLS HTAQERSIFA 

       250        260        270 
NGALKAASWA KNHANGLYSM LDVLGLNDQF

A9IXE5 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

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