NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 15356 / HD100 / DSM 50701 / NCIB 9529;
DOI=10.1126/science.1093027; PubMed=14752164 [NCBI, ExPASy, EBI, Israel, Japan]
Rendulic S., Jagtap P., Rosinus A., Eppinger M., Baar C., Lanz C., Keller H., Lambert C., Evans K.J., Goesmann A., Meyer F., Sockett R.E., Schuster S.C.;
"A predator unmasked: life cycle of Bdellovibrio bacteriovorus from a genomic perspective.";
Science 303:689-692(2004).

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

BX842646; CAE77729.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_967075.1; -.

3D structure databases

HSSP

P04036; 1ARZ. [HSSP ENTRY / PDB]

ModBase

Q6MRM8.

Enzyme and pathway databases

BioCyc

BBAC264462:BD0047-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]

TIGRFAMs

TIGR00036; dapB; 1.

PROSITE

PS01298; DAPB; FALSE_NEG.

ProtoNet

Q6MRM8.

Genome annotation databases

2733554; -.

BX842601_GR; Bd0047.

bba:Bd0047; -.

fig|264462.1.peg.45; -.

Phylogenomic databases

HOGENOM

Q6MRM8; -.

Genome annotation databases

CMR

Q6MRM8; Bd0047.

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`	`1 229`	`229`		`Dihydrodipicolinate reductase.`	`PRO_0000228328`

Sequence information

Length: 229 AA [This is the length of the unprocessed precursor]

Molecular weight: 25371 Da [This is the MW of the unprocessed precursor]

CRC64: A70F6574A1FF1A91 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MKKIKIGLMG SAGRMGQEIA GVIEANPRCE LVYAPLRGEK WDSKKAQAVD VWIDFTSPEA 

        70         80         90        100        110        120 
LKDILKKASE TKTPVVCGTT GFSKKEKELL KTYSKKIPVL WSSNMSLGVA VLNEALKAFS 

       130        140        150        160        170        180 
AISHFDFQIE EIHHNRKKDR PSGTAITLQE NLEKAVDKKL PEALAIRGGG VFGVHKIFAM 

       190        200        210        220 
SDEEVLTFEH TALNRTVFAK GSVQAAEWLV KQKPGLYQIR DVLFGKSKK

Q6MRM8 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