NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1101/gr.3771305; PubMed=16077009 [NCBI, ExPASy, EBI, Israel, Japan]
Degnan P.H., Lazarus A.B., Wernegreen J.J.;
"Genome sequence of Blochmannia pennsylvanicus indicates parallel evolutionary trends among bacterial mutualists of insects.";
Genome Res. 15:1023-1033(2005).

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

CP000016; AAZ40765.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

YP_277638.1; -.

3D structure databases

ModBase

Q493S0.

Enzyme and pathway databases

BioCyc

CBLO291272:BPEN_125-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).
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]

TIGRFAMs

TIGR00036; dapB; 1.

PROSITE

PS01298; DAPB; FALSE_NEG.

Genome annotation databases

GeneID

3563160; -.

GenomeReviews

CP000016_GR; BPEN_125.

KEGG

bpn:BPEN_125; -.

Phylogenomic databases

HOGENOM

Q493S0; -.

Genome annotation databases

CMR

Q493S0; BPEN_125.

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`	`1 282`	`282`		`Dihydrodipicolinate reductase.`	`PRO_0000228329`

Sequence information

Length: 282 AA [This is the length of the unprocessed precursor]

Molecular weight: 30864 Da [This is the MW of the unprocessed precursor]

CRC64: 5309FAC65A17FA81 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSDTPLRIAV TGVTGRMGKE IVTCIVKEEK QFSQEIVLGA AITRLNTNIC GMDAGILINT 

        70         80         90        100        110        120 
DALGIEITDN LESIKDNFDV LVDFTAPDIS IEYLKFCVNN NKNIVIGTTG FNQIHKNIIL 

       130        140        150        160        170        180 
NASHKIGIVF SSNFSIGVAL ISKLLHKITQ VIGNTSDISI IETHHNRKRD IPSGTSLTMQ 

       190        200        210        220        230        240 
NIIVNALRSI HSNRIIDSNL DSTTYSPASS YKDILIHSIR AGDVVGEHTV LFAGPGERLE 

       250        260        270        280 
ITHKASDRLI FAHGALRAAF WVGRDKIGLF DISDILEMDT LL

Q493S0 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