Dihydrodipicolinate reductase - Escherichia coli (strain K12)

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Reviewed, UniProtKB/Swiss-Prot P04036 (DAPB_ECOLI)

Last modified June 16, 2009. Version 93. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
    Dihydrodipicolinate reductase
      Short name=DHPR
    EC=1.3.1.26

Gene names

Name:	dapB
Ordered Locus Names:	b0031, JW0029

Organism

Escherichia coli (strain K12) [Complete proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

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Protein attributes

Sequence length	273 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

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General annotation (Comments)

Catalytic activity	2,3,4,5-tetrahydrodipicolinate + NAD(P)⁺ = 2,3-dihydrodipicolinate + NAD(P)H. HAMAP MF_00102
Enzyme regulation	The activity is repressed by lysine. HAMAP MF_00102
Pathway	Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; tetrahydrodipicolinate from L-aspartate: step 4/4. HAMAP MF_00102
Subunit structure	Homotetramer. HAMAP MF_00102
Subcellular location	Cytoplasm. HAMAP MF_00102
Sequence similarities	Belongs to the dihydrodipicolinate reductase family.

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Ontologies

Keywords
Biological process	Amino-acid biosynthesis Diaminopimelate biosynthesis Lysine biosynthesis
Cellular component	Cytoplasm
Ligand	NADP
Molecular function	Oxidoreductase
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	diaminopimelate biosynthetic process Inferred from electronic annotation. Source: HAMAP oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytosol Inferred from direct assay. Source: UniProtKB
Molecular function	binding Inferred from electronic annotation. Source: InterPro dihydrodipicolinate reductase activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 273

273

Dihydrodipicolinate reductase HAMAP MF_00102

PRO_0000141437

Secondary structure

273

Helix Strand Turn

Details...

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Sequences

Sequence

Length

Mass (Da)

Tools

P04036-1 [UniParc].

Last modified November 1, 1986. Version 1.
Checksum: 0ADE6837A6CF932C
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FASTA

273

28,757

        10         20         30         40         50         60 
MHDANIRVAI AGAGGRMGRQ LIQAALALEG VQLGAALERE GSSLLGSDAG ELAGAGKTGV 

        70         80         90        100        110        120 
TVQSSLDAVK DDFDVFIDFT RPEGTLNHLA FCRQHGKGMV IGTTGFDEAG KQAIRDAAAD 

       130        140        150        160        170        180 
IAIVFAANFS VGVNVMLKLL EKAAKVMGDY TDIEIIEAHH RHKVDAPSGT ALAMGEAIAH 

       190        200        210        220        230        240 
ALDKDLKDCA VYSREGHTGE RVPGTIGFAT VRAGDIVGEH TAMFADIGER LEITHKASSR 

       250        260        270 
MTFANGAVRS ALWLSGKESG LFDMRDVLDL NNL

« Hide

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Nucleotide sequence and expression of the Escherichia coli dapB gene." Bouvier J., Richaud C., Richaud F., Patte J.-C., Stragier P. J. Biol. Chem. 259:14829-14834(1984) [PubMed: 6094578] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Systematic sequencing of the Escherichia coli genome: analysis of the 0-2.4 min region." Yura T., Mori H., Nagai H., Nagata T., Ishihama A., Fujita N., Isono K., Mizobuchi K., Nakata A. Nucleic Acids Res. 20:3305-3308(1992) [PubMed: 1630901] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12.
[3]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed: 9278503] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[4]	"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed: 16738553] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]	"Multiple regulatory signals in the control region of the Escherichia coli carAB operon." Bouvier J., Patte J.-C., Stragier P. Proc. Natl. Acad. Sci. U.S.A. 81:4139-4143(1984) [PubMed: 6377309] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 269-273.
[6]	"Three-dimensional structure of Escherichia coli dihydrodipicolinate reductase." Scapin G., Blanchard J.S., Sacchettini J.C. Biochemistry 34:3502-3512(1995) [PubMed: 7893645] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
[7]	"Three-dimensional structure of Escherichia coli dihydrodipicolinate reductase in complex with NADH and the inhibitor 2,6-pyridinedicarboxylate." Scapin G., Reddy S.G., Zheng R., Blanchard J.S. Biochemistry 36:15081-15088(1997) [PubMed: 9398235] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).
+	Additional computationally mapped references.

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Cross-references

Sequence databases

M10611 Genomic DNA. Translation: AAA23666.1.
U00096 Genomic DNA. Translation: AAC73142.1.
AP009048 Genomic DNA. Translation: BAB96600.1.
J01597 Genomic DNA. No translation available.

PIR

RDECPD. A00375.

RefSeq

AP_000695.1.
NP_414572.1.

3D structure databases

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1ARZ	X-ray	2.60	A/B/C/D	1-273	[»]
1DIH	X-ray	2.20	A	1-273	[»]
1DRU	X-ray	2.20	A	1-273	[»]
1DRV	X-ray	2.20	A	1-273	[»]
1DRW	X-ray	2.20	A	1-273	[»]

ModBase

Search...

2-D gel databases

SWISS-2DPAGE

P04036.

Genome annotation databases

GeneID

944762.

GenomeReviews

Gene locus JW0029 in contig AP009048_GR.
Gene locus b0031 in contig U00096_GR.

KEGG

ecj:JW0029.
eco:b0031.

Organism-specific databases

EchoBASE

EB0202.

EcoGene

EG10206. dapB.

CMR

Search...

Phylogenomic databases

HOGENOM

P04036.

OMA

P04036. TIGFSTI.

Enzyme and pathway databases

BioCyc

EcoCyc:DIHYDROPICRED-MON.
MetaCyc:DIHYDROPICRED-MON.

Family and domain databases

HAMAP

MF_00102.
[Tree]

InterPro

IPR000846. DapB.
IPR011770. DapB_bac/pln.
IPR016040. NAD(P)-bd_dom.
[Graphical view]

Gene3D

G3DSA:3.40.50.720. NAD(P)-bd. 2 hits.

PANTHER

PTHR20836. DapB_bac/pln. 1 hit.

Pfam

PF05173. DapB_C. 1 hit.
PF01113. DapB_N. 1 hit.
[Graphical view]

ProDom

PD004105. DapB. 1 hit.
[Graphical view] [Entries sharing at least one domain]

TIGRFAMs

TIGR00036. dapB. 1 hit.

PROSITE

PS01298. DAPB. 1 hit.
[Graphical view]

ProtoNet

Search...

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Entry information

Entry name

DAPB_ECOLI

Accession

Primary (citable) accession number: P04036

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1986
Last sequence update:	November 1, 1986
Last modified:	June 16, 2009
This is version 93 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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