NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Tokyo 1998;
DOI=10.1038/35024074; PubMed=10993077 [NCBI, ExPASy, EBI, Israel, Japan]
Shigenobu S., Watanabe H., Hattori M., Sakaki Y., Ishikawa H.;
"Genome sequence of the endocellular bacterial symbiont of aphids Buchnera sp. APS.";
Nature 407:81-86(2000).

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 .
SUBUNIT: Homotetramer (By similarity).
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

BA000003; BAB12864.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_239978.1; -.

3D structure databases

HSSP

P04036; 1DRU. [HSSP ENTRY / PDB]

ModBase

P57246.

Enzyme and pathway databases

BioCyc

BSP107806:BU146-MON; -.

Ontologies

GO:0005737;	Cellular component: cytoplasm (inferred from electronic annotation from HAMAP).
GO:0005488;	Molecular function: binding (inferred from electronic annotation from InterPro).
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).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
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

1109590; -.

GenomeReviews

BA000003_GR; BU146.

KEGG

buc:BU146; -.

Phylogenomic databases

HOGENOM

P57246; -.

Genome annotation databases

CMR

P57246; BU146.

Other

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_0000141419`

Sequence information

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

Molecular weight: 30146 Da [This is the MW of the unprocessed precursor]

CRC64: 5FA5F0811A302823 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MNKKTRIAIT GPIGRMGRML IKEIQNNKHS HLTVAVVQKK HQLIGQDIGR IIGIGEIGVL 

        70         80         90        100        110        120 
ISDELNIKKN DFDVLIDFTR PAGTLEYLKY CNKFKKNIVI GTTGFSKEEI DIIKSYSQKI 

       130        140        150        160        170        180 
AIIIASNFSI GINLLFQLIK KTTQIIGKDS DINILEYHHR NKIDAPSGTA LEIGEVISKV 

       190        200        210        220        230        240 
MNWNLNQDSI YYQKGITGIR DAKKIGFSIV RAGNIVGKHT VMFSSYDEEI KITHTASNRM 

       250        260 
SFARGAIQSA LWIHKKNTGL FDMTDVLSL

P57246 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