NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=GR4;
DOI=10.1007/s002030000169; PubMed=10896225 [NCBI, ExPASy, EBI, Israel, Japan]
Garcia-Rodriguez F.M., Zekri S., Toro N.;
"Characterization of the Sinorhizobium meliloti genes encoding a functional dihydrodipicolinate synthase (dapA) and dihydrodipicolinate reductase (dapB).";
Arch. Microbiol. 173:438-444(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 .
SUBCELLULAR LOCATION: Cytoplasm (By similarity).
SIMILARITY: Belongs to the dihydrodipicolinate reductase family.
SEQUENCE CAUTION:
- Sequence=CAA10958.1; Type=Frameshift; Positions=Several;

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

AJ222715; CAA10958.1; ALT_FRAME; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

HSSP

P04036; 1DRW. [HSSP ENTRY / PDB]

ModBase

O69783.

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; 1.

Other

ProtoNet

O69783.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Amino-acid biosynthesis; Cytoplasm; Diaminopimelate biosynthesis; Lysine biosynthesis; NADP; Oxidoreductase; Plasmid.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 >242`	`>242`	`Dihydrodipicolinate reductase.`	`PRO_0000141477`
`NON_TER`	`242 242`

Sequence information

Length: 242 AA [This is the length of the partial sequence of the unprocessed precursor]

Molecular weight: 24880 Da [This is the MW of the partial sequence of the unprocessed precursor]

CRC64: 31C962599F153CC5 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSQMRLVVVG AAGRMGRTLI KAIAENPGCM LSGAVERPGS AAVGQDAGFV AGMASCGVLV 

        70         80         90        100        110        120 
TDEPGSAFAE ADGVLDFTTP DATAEYSSLA AQVGIVHVVG TTGMEPVHFS KLVRAARTIP 

       130        140        150        160        170        180 
VVQSGNMSLG VNILAALVQK VAAILDKEWD IEVLEMHHRM KVDAPSGAAL LLGEAAASGR 

       190        200        210        220        230        240 
QTILSDHYVA GRDGYTGCRT VGTIGFAPCA GXVVGDHKVV FAGAGXRIEL SHIAEDRSLF 


AQ

O69783 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