NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=VF5;
DOI=10.1038/32831; PubMed=9537320 [NCBI, ExPASy, EBI, Israel, Japan]
Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L., Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R., Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.;
"The complete genome of the hyperthermophilic bacterium Aquifex aeolicus.";
Nature 392:353-358(1998).

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

AE000657; AAC07008.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

B70379; B70379.

RefSeq

NP_213623.1; -.

3D structure databases

HSSP

P04036; 1DRW. [HSSP ENTRY / PDB]

ModBase

O67061.

Enzyme and pathway databases

BioCyc

AAEO224324:AQ_916-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).
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

1193603; -.

AE000657_GR; aq_916.

aae:aq_916; -.

fig|224324.1.peg.638; -.

Phylogenomic databases

HOGENOM

O67061; -.

Genome annotation databases

CMR

O67061; aq_916.

Other

ProtoNet

O67061.

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`	`1 265`	`265`		`Dihydrodipicolinate reductase.`	`PRO_0000141407`

Sequence information

Length: 265 AA [This is the length of the unprocessed precursor]

Molecular weight: 28961 Da [This is the MW of the unprocessed precursor]

CRC64: EC3240CBCE8BE27A [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSVRVVVCGA LGRMGRRIIE LALQDKDVEV VGGVEHPDCV PSIDLGEALG KEELKGKPLT 

        70         80         90        100        110        120 
SRLEELLPYT DVVIEFSGNP TAAVGHAELT TLEKKAIVIG TTGFTKQEIE QIKEFSKNAP 

       130        140        150        160        170        180 
VLLSPNMSLG VNLLFKLAEI AAKVLKDKNF DAEIMEIHHR FKKDAPSGTA MKLAEILSET 

       190        200        210        220        230        240 
LEKKNLVFGR KGEAPRKEDE IGVMALRGGD VVGDHTVYFL GFGERIELTH RATSRDTFAK 

       250        260 
GAVEAAKWIK GKEPGFYTMF DVLGL

O67061 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