NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=Tohama I / ATCC BAA-589 / NCTC 13251;
Pradel E.;
Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases.

[2]

NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Tohama I / ATCC BAA-589 / NCTC 13251;
DOI=10.1038/ng1227; PubMed=12910271 [NCBI, ExPASy, EBI, Israel, Japan]
Parkhill J., Sebaihia M., Preston A., Murphy L.D., Thomson N.R., Harris D.E., Holden M.T.G., Churcher C.M., Bentley S.D., Mungall K.L., Cerdeno-Tarraga A.-M., Temple L., James K.D., Harris B., Quail M.A., Achtman M., Atkin R., Baker S., Basham D., Bason N., Cherevach I., Chillingworth T., Collins M., Cronin A., Davis P., Doggett J., Feltwell T., Goble A., Hamlin N., Hauser H., Holroyd S., Jagels K., Leather S., Moule S., Norberczak H., O'Neil S., Ormond D., Price C., Rabbinowitsch E., Rutter S., Sanders M., Saunders D., Seeger K., Sharp S., Simmonds M., Skelton J., Squares R., Squares S., Stevens K., Unwin L., Whitehead S., Barrell B.G., Maskell D.J.;
"Comparative analysis of the genome sequences of Bordetella pertussis, Bordetella parapertussis and Bordetella bronchiseptica.";
Nat. Genet. 35:32-40(2003).

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

AJ238308; CAB41012.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BX640418; CAE42781.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_881136.1; -.

3D structure databases

HSSP

P04036; 1DRW. [HSSP ENTRY / PDB]

ModBase

Q9X6Y9.

Enzyme and pathway databases

BioCyc

BPER257313:BP2509-MON; -.

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.

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]

TIGR00036; dapB; 1.

PS01298; DAPB; 1.

Genome annotation databases

2665670; -.

BX470248_GR; BP2509.

bpe:BP2509; -.

fig|257313.1.peg.2210; -.

Phylogenomic databases

HOGENOM

Q9X6Y9; -.

Genome annotation databases

CMR

Q9X6Y9; BP2509.

Other

ProtoNet

Q9X6Y9.

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`	`1 269`	`269`		`Dihydrodipicolinate reductase.`	`PRO_0000141415`

Sequence information

Length: 269 AA [This is the length of the unprocessed precursor]

Molecular weight: 28328 Da [This is the MW of the unprocessed precursor]

CRC64: 68DF3E7158BDAA31 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MTQATPQRIA IAGASGRMGQ MLIEAVLDTE GVELAVALDR AGSPSIGQDA GAALGRPCGV 

        70         80         90        100        110        120 
TITDQLDALA QADCLIDFTR PEGTLQHLQA CLRHDVKMVI GTTGFDSSGR AEIKVAAQKI 

       130        140        150        160        170        180 
AIVFAPNMSV GVNATLKLLD MAARILNSGY DVEIFEAHHR NKVDAPSGTA LIMGETVASA 

       190        200        210        220        230        240 
WDVALPDVAT WTRHGDTGVR KPGTIGFSVV RGGDIVGDHT VFFCGTGERI EISHRSSSRA 

       250        260 
TYAQGAVRAA RFLARQDNGL YDMQAVLGL

Q9X6Y9 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