Reviewed, UniProtKB/Swiss-Prot Q9FJ82 (DAPB3_ARATH)

Names and origin

Protein names

Recommended name:
    Putative dihydrodipicolinate reductase 3, chloroplastic
      Short name=DHPR 3
    EC=1.3.1.26

Gene names

Name:	DAPB3
Ordered Locus Names:	At5g52100
ORF Names:	MSG15.20

Organism

Arabidopsis thaliana (Mouse-ear cress) [Complete proteome]

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Arabidopsis

Protein attributes

Sequence length	298 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript level.

General annotation (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; (S)-tetrahydrodipicolinate from L-aspartate: step 4/4.
Subcellular location	Plastid › chloroplast Potential.
Miscellaneous	Unlike DAPB1 and DAPB2, DAPB3 is unable to complement an E.coli dapB strain.
Sequence similarities	Belongs to the dihydrodipicolinate reductase family.

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Diaminopimelate biosynthesis Lysine biosynthesis
Cellular component	Chloroplast Plastid
Domain	Transit peptide
Ligand	NADP
Molecular function	Oxidoreductase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	diaminopimelate biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW photosynthesis, light reaction Inferred from mutant phenotype. Source: TAIR
Cellular component	chloroplast stroma Inferred from direct assay. Source: TAIR
Molecular function	binding Inferred from electronic annotation. Source: InterPro dihydrodipicolinate reductase activity Ref.4 Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 25	25	Chloroplast Potential
	Chain	26 – 298	273	Putative dihydrodipicolinate reductase 3, chloroplastic		PRO_0000307184
Experimental info
	Sequence conflict	106	1	Missing in AAM60980. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Q9FJ82-1 [UniParc]. Last modified March 1, 2001. Version 1. Checksum: DC15436BDE54D2D3	FASTA	298	32,038
	10 20 30 40 50 60 MAAVNCHFFQ LSRHLKPSRP SFSCSASQPS QNNIKVIING AAKEIGRAAV VAVTKARGME 70 80 90 100 110 120 LAGAVDNHFV GEDIGLLCDM EEPLEIPVVS DLTMVLGSIS QGKEVGVVID FTDPSTVYEN 130 140 150 160 170 180 VKQATAFGMK SVVYVPRIKP ETVSALSALC DKATMGCLVA PTLSIGSILL QQAVIMASFH 190 200 210 220 230 240 YNNVELVESR PNAADLPSPE AIQIANNISN LGQIYNREDS STDVQARGQV IGEDGVRVHS 250 260 270 280 290 MVLPGLPSST QVYFSSPGDV YTVKHDIIDV RSLMPGLLLA IRKVVRLKNL VYGLEKFL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Structural analysis of Arabidopsis thaliana chromosome 5. VII. Sequence features of the regions of 1,013,767 bp covered by sixteen physically assigned P1 and TAC clones." Nakamura Y., Sato S., Asamizu E., Kaneko T., Kotani H., Miyajima N., Tabata S. DNA Res. 5:297-308(1998) [PubMed: 9872454] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[2]	"Full-length cDNA from Arabidopsis thaliana." Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., Feldmann K.A. Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[3]	"Arabidopsis ORF clones." Kim C.J., Bautista V.R., Chen H., De Los Reyes C., Wu S.Y., Ecker J.R. Submitted (JAN-2007) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia.
[4]	"Biosynthesis of lysine in plants: evidence for a variant of the known bacterial pathways." Hudson A.O., Bless C., Macedo P., Chatterjee S.P., Singh B.K., Gilvarg C., Leustek T. Biochim. Biophys. Acta 1721:27-36(2005) [PubMed: 15652176] [Abstract] Cited for: FUNCTION.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AB015478 Genomic DNA. Translation: BAB11058.1. AY084406 mRNA. Translation: AAM60980.1. BT030092 mRNA. Translation: ABN04830.1.
IPI	IPI00522022.
RefSeq	NP_200023.1.
UniGene	At.29638
3D structure databases
HSSP	HSSP built from PDB template 1P9L based on UniProtKB P72024.
SMR	Q9FJ82. Positions 34-298.
ModBase	Search...
Protein-protein interaction databases
STRING	Q9FJ82.
Proteomic databases
PRIDE	Q9FJ82.
Genome annotation databases
GeneID	835286.
GenomeReviews	Gene locus AT5G52100 in contig BA000015_GR.
KEGG	ath:AT5G52100.
NMPDR	fig|3702.1.peg.27089.
Organism-specific databases
TAIR	At5g52100.
Phylogenomic databases
eggNOG	COG0289.
HOGENOM	HBG594002.
InParanoid	Q9FJ82.
OMA	QLGVEVI.
Enzyme and pathway databases
BRENDA	1.3.1.26. 302.
Gene expression databases
Genevestigator	Q9FJ82.
Family and domain databases
InterPro	IPR000846. DapB. IPR011770. Dihydrodipicolinate_Rdtase. IPR016040. NAD(P)-bd_dom. [Graphical view]
Gene3D	G3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
PANTHER	PTHR20836. DapB_bac/pln. 1 hit.
Pfam	PF05173. DapB_C. 1 hit. PF01113. DapB_N. 1 hit. [Graphical view]
TIGRFAMs	TIGR00036. dapB. 1 hit.
ProtoNet	Search...

Entry information

Entry name

DAPB3_ARATH

Accession

Primary (citable) accession number: Q9FJ82
Secondary accession number(s): Q8LG90

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 23, 2007
Last sequence update:	March 1, 2001
Last modified:	February 9, 2010
This is version 49 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)