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P59317 (ARGD_ECOL6) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 79. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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:
Acetylornithine/succinyldiaminopimelate aminotransferase

Short name=ACOAT
Short name=DapATase
Short name=Succinyldiaminopimelate transferase
EC=2.6.1.11
EC=2.6.1.17
Gene names
Name:argD
Synonyms:dapC
Ordered Locus Names:c4134
OrganismEscherichia coli O6 [Complete proteome] [HAMAP]
Taxonomic identifier217992 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length406 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology

General annotation (Comments)

Function

Involved in both the arginine and lysine biosynthetic pathways By similarity. HAMAP MF_01107

Catalytic activity

N(2)-acetyl-L-ornithine + 2-oxoglutarate = N-acetyl-L-glutamate 5-semialdehyde + L-glutamate. HAMAP MF_01107

N-succinyl-L-2,6-diaminoheptanedioate + 2-oxoglutarate = N-succinyl-2-L-amino-6-oxoheptanedioate + L-glutamate. HAMAP MF_01107

Cofactor

Binds 1 pyridoxal phosphate per subunit By similarity. HAMAP MF_01107

Pathway

Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 4/4. HAMAP MF_01107

Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; LL-2,6-diaminopimelate from (S)-tetrahydrodipicolinate (succinylase route): step 2/3. HAMAP MF_01107

Subunit structure

Homodimer By similarity. HAMAP MF_01107

Subcellular location

Cytoplasm Probable HAMAP MF_01107.

Miscellaneous

The reaction catalyzed by ACOAT is highly reversible. This enzyme may also transaminate ornithine By similarity. HAMAP MF_01107

Sequence similarities

Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. ArgD subfamily.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 406405Acetylornithine/succinyldiaminopimelate aminotransferase HAMAP MF_01107
PRO_0000112744

Regions

Region108 – 1092Pyridoxal phosphate binding By similarity
Region226 – 2294Pyridoxal phosphate binding By similarity

Sites

Binding site1411Pyridoxal phosphate; via carbonyl oxygen By similarity
Binding site1441N2-acetyl-L-ornithine By similarity
Binding site2831N2-acetyl-L-ornithine By similarity
Binding site2841Pyridoxal phosphate By similarity

Amino acid modifications

Modified residue2551N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
P59317 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: D968726560815570

FASTA40643,801
        10         20         30         40         50         60 
MAIEQTAITR ATFDEVILPI YAPAEFIPVK GQGSRIWDQQ GKEYVDFAGG IAVTALGHCH 

        70         80         90        100        110        120 
PALVNALKTQ GETLWHISNV FTNEPALRLG RKLIEATFAE RVVFMNSGTE ANETAFKLAR 

       130        140        150        160        170        180 
HYACVRHSPF KTKIIAFHNA FHGRSLFTVS VGGQPKYSDG FGPKPADIIH VPFNDLHAVK 

       190        200        210        220        230        240 
AVMDDHTCAV VVEPIQGEGG VTAATPEFLQ GLRELCDQHQ ALLVFDEVQC GMGRTGDLFA 

       250        260        270        280        290        300 
YMHYGVTPDI LTSAKALGGG FPVSAMLTTA EIASAFHPGS HGSTYGGNPL ACAVAGAAFD 

       310        320        330        340        350        360 
IINTPEVLEG IQAKRQHFVD HLQKIDQQYD VFSDIRGMGL LIGAELKPQY KGRARDFLYA 

       370        380        390        400 
GAEEGVMVLN AGPDVMRFAP SLVVEDADID EGMHRFAHAV AKVVGA 

« Hide

References

[1]"Extensive mosaic structure revealed by the complete genome sequence of uropathogenic Escherichia coli."
Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D., Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F., Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T., Donnenberg M.S., Blattner F.R.
Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002) [PubMed: 12471157] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: O6:H1 / CFT073 / ATCC 700928 / UPEC.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE014075 Genomic DNA. Translation: AAN82572.1.
RefSeqNP_755998.1. NC_004431.1.

3D structure databases

ProteinModelPortalP59317.
SMRP59317. Positions 18-404.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBESCT00000042031; EBESCP00000040380; EBESCG00000041081.
GeneID1038036.
GenomeReviewsGene locus c4134 in contig AE014075_GR.
KEGGecc:c4134.
NMPDRfig|199310.1.peg.4041.
PATRIC18286018. VBIEscCol75197_3885.

Organism-specific databases

CMRSearch...

Phylogenomic databases

GeneTreeEBGT00050000010246.
HOGENOMHBG725944.
OMAYADGFGP.
ProtClustDBPRK05093.

Family and domain databases

HAMAPMF_01107. ArgD_aminotrans_3.
[Tree]
InterProIPR017652. Ac/SuccinylOrn_transaminase.
IPR004636. AcOrn/SuccinylOrn_aminoTrfase.
IPR005814. Aminotrans_3.
IPR015424. PyrdxlP-dep_Trfase_major_dom.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view]
Gene3DG3DSA:3.40.640.10. PyrdxlP-dep_Trfase_major_sub1. 1 hit.
G3DSA:3.90.1150.10. PyrdxlP-dep_Trfase_major_sub2. 2 hits.
KOK00821.
PANTHERPTHR11986. Aminotrans_3. 1 hit.
PTHR11986:SF19. ArgD_aminotrans. 1 hit.
PfamPF00202. Aminotran_3. 1 hit.
[Graphical view]
SUPFAMSSF53383. PyrdxlP-dep_Trfase_major. 1 hit.
TIGRFAMsTIGR03246. Arg_catab_astC. 1 hit.
TIGR00707. ArgD. 1 hit.
PROSITEPS00600. AA_TRANSFER_CLASS_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameARGD_ECOL6
AccessionPrimary (citable) accession number: P59317
Entry history
Integrated into UniProtKB/Swiss-Prot: February 12, 2003
Last sequence update: January 23, 2007
Last modified: January 25, 2012
This is version 79 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families