NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Fouts D.E., Mongodin E.F., Puiu D., Sebastian Y., Miller W.G., Mandrell R.E., Lastovica A.J., Nelson K.E.;
"Complete genome sequence of Campylobacter jejuni subsp doylei 269.97 isolated from human blood.";
Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.

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

CP000768; ABS44158.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

YP_001397444.1; -.

3D structure databases

ModBase

A7H1R4.

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

GeneID

5389928; -.

GenomeReviews

CP000768_GR; JJD26997_0207.

KEGG

cjd:JJD26997_0207; -.

CMR

A7H1R4; JJD26997_0207.

Other

ProtoNet

A7H1R4.

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`	`1 248`	`248`		`Dihydrodipicolinate reductase.`	`PRO_1000008553`

Sequence information

Length: 248 AA [This is the length of the unprocessed precursor]

Molecular weight: 27560 Da [This is the MW of the unprocessed precursor]

CRC64: 040E16B10D696DCC [This is a checksum on the sequence]

        10         20         30         40         50         60 
MIKIGIYGAK GRMGKQIEEC LKSETQAEIS ILYNKGGNLE ELFEKSDVII DFSSPSGTHE 

        70         80         90        100        110        120 
LLNYARTMPK PLTIGTTGLD EKILHLMQSA SKVMPIFYAT NMSLGVAVLN YLASKASQML 

       130        140        150        160        170        180 
RNFDIEILEM HHRHKKDAPS GTAMTLAQSV AKARNLELEK VRVSGRDGII GERSKDEIAV 

       190        200        210        220        230        240 
MSLRGGDIVG RHTVGFYEDG EFLELNHTAT SRATFAKGAI KIAIWLSKQE AKMYSINDFF 


RNLKCVQL

A7H1R4 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
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	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