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P0A9D8 (DAPD_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 64. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-succinyltransferase

EC=2.3.1.117
Alternative name(s):
Tetrahydrodipicolinate N-succinyltransferase
Short name=THDP succinyltransferase
Short name=THP succinyltransferase
Short name=Tetrahydropicolinate succinylase
Gene names
Name:dapD
Ordered Locus Names:b0166, JW0161
OrganismEscherichia coli (strain K12)
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length274 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

Succinyl-CoA + (S)-2,3,4,5-tetrahydropyridine-2,6-dicarboxylate + H2O = CoA + N-succinyl-L-2-amino-6-oxoheptanedioate. HAMAP MF_00811

Pathway

Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; LL-2,6-diaminopimelate from (S)-tetrahydrodipicolinate (succinylase route): step 1/3. HAMAP MF_00811

Subunit structure

Homotrimer By similarity. HAMAP MF_00811

Subcellular location

Cytoplasm HAMAP MF_00811.

Sequence similarities

Belongs to the transferase hexapeptide repeat family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 2742742,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-succinyltransferase HAMAP MF_00811
PRO_0000196933

Sites

Binding site1041Substrate By similarity
Binding site1411Substrate By similarity

Experimental info

Sequence conflict311V → D in AAA23667. Ref.1
Sequence conflict1631G → R in AAA23667. Ref.1
Sequence conflict1771I → M in AAA23667. Ref.1
Sequence conflict1901V → L in AAA23667. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P0A9D8 [UniParc].

Last modified July 19, 2005. Version 1.
Checksum: 42D7A38610DD3AF6

FASTA27429,892
        10         20         30         40         50         60 
MQQLQNIIET AFERRAEITP ANADTVTREA VNQVIALLDS GALRVAEKID GQWVTHQWLK 

        70         80         90        100        110        120 
KAVLLSFRIN DNQVIEGAES RYFDKVPMKF ADYDEARFQK EGFRVVPPAA VRQGAFIARN 

       130        140        150        160        170        180 
TVLMPSYVNI GAYVDEGTMV DTWATVGSCA QIGKNVHLSG GVGIGGVLEP LQANPTIIED 

       190        200        210        220        230        240 
NCFIGARSEV VEGVIVEEGS VISMGVYIGQ STRIYDRETG EIHYGRVPAG SVVVSGNLPS 

       250        260        270 
KDGKYSLYCA VIVKKVDAKT RGKVGINELL RTID 

« Hide

References

« Hide 'large scale' references
[1]"Regulation of expression and nucleotide sequence of the Escherichia coli dapD gene."
Richaud C., Richaud F., Martin C., Haziza C., Patte J.-C.
J. Biol. Chem. 259:14824-14828(1984) [PubMed: 6094577] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Systematic sequencing of the Escherichia coli genome: analysis of the 2.4-4.1 min (110,917-193,643 bp) region."
Fujita N., Mori H., Yura T., Ishihama A.
Nucleic Acids Res. 22:1637-1639(1994) [PubMed: 8202364] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[3]"Sequence of minutes 4-25 of Escherichia coli."
Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M., Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D., Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.
Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[4]"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.
[5]"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.
[6]"The genes of the glutamine synthetase adenylylation cascade are not regulated by nitrogen in Escherichia coli."
van Heeswijk W.C., Rabenberg M., Westerhoff H.V., Kahn D.D.
Mol. Microbiol. 9:443-458(1993) [PubMed: 8412694] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-15.
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[7]Pasquali C., Sanchez J.-C., Ravier F., Golaz O., Hughes G.J., Frutiger S., Paquet N., Wilkins M., Appel R.D., Bairoch A., Hochstrasser D.F.
Submitted (SEP-1994) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 1-11.
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[8]"Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12."
Link A.J., Robison K., Church G.M.
Electrophoresis 18:1259-1313(1997) [PubMed: 9298646] [Abstract]
Cited for: PROTEIN SEQUENCE OF 1-12.
Strain: K12 / EMG2.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
K02970 Genomic DNA. Translation: AAA23667.1.
U70214 Genomic DNA. Translation: AAB08595.1.
U00096 Genomic DNA. Translation: AAC73277.1.
AP009048 Genomic DNA. Translation: BAB96742.1.
Z21842 Genomic DNA. Translation: CAA79888.1.
PIRXNECSD. F64740.
RefSeqNP_414708.1. NC_000913.2.

3D structure databases

ProteinModelPortalP0A9D8.
SMRP0A9D8. Positions 2-274.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-31866N.
IntActP0A9D8. 4 interactions.

2D gel databases

SWISS-2DPAGEP0A9D8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBESCT00000004043; EBESCP00000004043; EBESCG00000003300.
EBESCT00000014470; EBESCP00000013761; EBESCG00000013531.
GeneID944862.
GenomeReviewsGene locus JW0161 in contig AP009048_GR.
Gene locus b0166 in contig U00096_GR.
KEGGecj:JW0161.
eco:b0166.
PATRIC32115439. VBIEscCol129921_0171.

Organism-specific databases

EchoBASEEB0203.
EcoGeneEG10207. dapD.

Phylogenomic databases

eggNOGCOG2171.
GeneTreeEBGT00050000010899.
HOGENOMHBG704071.
OMAKAILLYF.
PhylomeDBP0A9D8.
ProtClustDBPRK11830.

Enzyme and pathway databases

BioCycEcoCyc:MONOMER0-2001.
MetaCyc:MONOMER0-2001.

Gene expression databases

GenevestigatorP0A9D8.

Family and domain databases

HAMAPMF_00811. DapD.
[Tree]
InterProIPR005664. DapD.
IPR001451. Hexapep_transf.
IPR018357. Hexapep_transf_CS.
IPR023180. THP_succinylTrfase_dom1.
IPR011004. Trimer_LpxA-like.
[Graphical view]
Gene3DG3DSA:1.10.166.10. THP_succinylTrfase_dom1. 1 hit.
KOK00674.
PANTHERPTHR19136:SF52. PTHR19136:SF52. 1 hit.
PfamPF00132. Hexapep. 2 hits.
[Graphical view]
SUPFAMSSF51161. Trimer_LpxA_like. 1 hit.
TIGRFAMsTIGR00965. DapD. 1 hit.
PROSITEPS00101. HEXAPEP_TRANSFERASES. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameDAPD_ECOLI
AccessionPrimary (citable) accession number: P0A9D8
Secondary accession number(s): P03948
Entry history
Integrated into UniProtKB/Swiss-Prot: October 23, 1986
Last sequence update: July 19, 2005
Last modified: January 25, 2012
This is version 64 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families