NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Saunders E.H., Schmutz J., Larimer F., Land M., Kyrpides N., Mavrommatis K., Richardson P.;
"Complete sequence of Anabaena variabilis ATCC 29413.";
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.

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

CP000117; ABA20098.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

YP_320993.1; -.

3D structure databases

ModBase

Q3MFY8.

Enzyme and pathway databases

BioCyc

AVAR240292:AVA_0474-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

GeneID

3682440; -.

GenomeReviews

CP000117_GR; Ava_0474.

KEGG

ava:Ava_0474; -.

NMPDR

fig|240292.3.peg.1613; -.

Phylogenomic databases

HOGENOM

Q3MFY8; -.

Genome annotation databases

CMR

Q3MFY8; Ava_0474.

Other

ProtoNet

Q3MFY8.

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`	`1 278`	`278`		`Dihydrodipicolinate reductase.`	`PRO_1000057677`

Sequence information

Length: 278 AA [This is the length of the unprocessed precursor]

Molecular weight: 29464 Da [This is the MW of the unprocessed precursor]

CRC64: F02D1FF0D93EBD6B [This is a checksum on the sequence]

        10         20         30         40         50         60 
MTNQAPIPVI VNGAAGKMGR EVVKAIAQAP DLNLLGAIDS SPEHQGKDAG ELAGLSEPLE 

        70         80         90        100        110        120 
VPITNQLEPM LGYVAGERQG PPGVIVDFTH PDSVYDNVRS AIAYGIRPVV GTTGLSPAQI 

       130        140        150        160        170        180 
QNLADFAEKA STGCLIIPNF SIGMVLLQQA AVTASQYFDH VEIIELHHNQ KADAPSGTAI 

       190        200        210        220        230        240 
QTAELLAELG KTFNSAIVEE TEKIPGARGS LAGEGIRIHS VRLPGLIAHQ EVIFGAPGQI 

       250        260        270 
YTLRHDTSDR ACYMPGVLLA IRKVLQLKSL VYGLEKIL

Q3MFY8 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
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	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