[1]	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.; "Genome sequence of Campylobacter curvus 525.92 isolated from human feces."; 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

CP000767; EAU01118.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

YP_001407514.1; -.

3D structure databases

ModBase

A7GWC2.

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

5407347; -.

GenomeReviews

CP000767_GR; Ccur92_02100.

KEGG

ccv:CCV52592_0841; -.

CMR

A7GWC2; Ccur92_02100.

Other

ProtoNet

A7GWC2.

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`	`1 254`	`254`		`Dihydrodipicolinate reductase.`	`PRO_1000008550`

Sequence information

Length: 254 AA [This is the length of the unprocessed precursor]

Molecular weight: 26952 Da [This is the MW of the unprocessed precursor]

CRC64: 6B2FFB9B3A70EBF8 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MINIGIHGAS GKMGQMIINC LKDSKDAKLT ALYTIEPLGS VPEGVIVTDD LNELFANCDV 

        70         80         90        100        110        120 
VIDFTIKEGA LNLINYARTN PKPLVIGTTG LGDDGTNLLN LAANAMPILY ATNMSLGVAV 

       130        140        150        160        170        180 
LNRLASLAAK TLAEFDIEIV EQHHRHKKDA PSGTALTLAQ HAANARGLNL KDVIVTGRDG 

       190        200        210        220        230        240 
LVGARSKDEI AVLAVRGGDV VGRHTIGFYN EGEFIEINHT ATSRATFAKG AIKAAVWLSS 

       250 
QKNGLYSIYD CLGL

A7GWC2 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