Acetylornithine/succinyldiaminopimelate aminotransferase

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Reviewed, UniProtKB/Swiss-Prot P59317 (ARGD_ECOL6)

Last modified February 9, 2010. Version 65. 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:
    Acetylornithine/succinyldiaminopimelate aminotransferase
      Short name=ACOAT
      Short name=Succinyldiaminopimelate transferase
      Short name=DapATase
    EC=2.6.1.11
    EC=2.6.1.17

Gene names

Name:	argD
Synonyms:	dapC
Ordered Locus Names:	c4134

Organism

Escherichia coli O6 [Complete proteome] [HAMAP]

Taxonomic identifier

217992 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

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Protein attributes

Sequence length	406 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Inferred from homology.

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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.

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Ontologies

Keywords
Biological process	Amino-acid biosynthesis Arginine biosynthesis Lysine biosynthesis
Cellular component	Cytoplasm
Ligand	Pyridoxal phosphate
Molecular function	Aminotransferase Transferase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	arginine biosynthetic process Inferred from electronic annotation. Source: HAMAP lysine biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	N2-acetyl-L-ornithine:2-oxoglutarate 5-aminotransferase activity Inferred from electronic annotation. Source: HAMAP pyridoxal phosphate binding Inferred from electronic annotation. Source: InterPro succinyldiaminopimelate transaminase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed By similarity

Chain

2 – 406

405

Acetylornithine/succinyldiaminopimelate aminotransferase HAMAP MF_01107

PRO_0000112744

Regions

Region

108 – 109

Pyridoxal phosphate binding By similarity

Region

226 – 229

Pyridoxal phosphate binding By similarity

Sites

Binding site

141

Pyridoxal phosphate; via carbonyl oxygen By similarity

Binding site

144

N(2)-acetyl-L-ornithine By similarity

Binding site

283

N(2)-acetyl-L-ornithine By similarity

Binding site

284

Pyridoxal phosphate By similarity

Amino acid modifications

Modified residue

255

N6-(pyridoxal phosphate)lysine By similarity

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Sequences

Sequence

Length

Mass (Da)

Tools

P59317-1 [UniParc].

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

406

43,801

        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

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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.

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Cross-references

Sequence databases
EMBL GenBank DDBJ	AE014075 Genomic DNA. Translation: AAN82572.1.
RefSeq	NP_755998.1.
3D structure databases
SMR	P59317. Positions 18-404.
ModBase	Search...
Genome annotation databases
GeneID	1038036.
GenomeReviews	Gene locus c4134 in contig AE014075_GR.
KEGG	ecc:c4134.
NMPDR	fig\|199310.1.peg.4041.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG725944.
OMA	GVHGTTF.
Enzyme and pathway databases
BRENDA	2.6.1.11. 292881. 2.6.1.17. 292881.
Family and domain databases
HAMAP	MF_01107. ArgD_aminotrans_3. [Tree]
InterPro	IPR004636. AcOrn/succinylOrn_aminoTrfase. IPR005814. Aminotrans_3. IPR015424. PyrdxlP-dep_Trfase_major_dom. IPR015421. PyrdxlP-dep_Trfase_major_sub1. IPR017652. SuccinylOrn_transaminase. [Graphical view]
Gene3D	G3DSA:3.40.640.10. PyrdxlP-dep_Trfase_major_sub1. 1 hit.
PANTHER	PTHR11986. Aminotrans_3. 1 hit. PTHR11986:SF19. ArgD_aminotrans. 1 hit.
Pfam	PF00202. Aminotran_3. 1 hit. [Graphical view]
TIGRFAMs	TIGR03246. arg_catab_astC. 1 hit. TIGR00707. argD. 1 hit.
PROSITE	PS00600. AA_TRANSFER_CLASS_3. 1 hit. [Graphical view]
ProtoNet	Search...

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Entry information

Entry name

ARGD_ECOL6

Accession

Primary (citable) accession number: P59317

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 12, 2003
Last sequence update:	January 23, 2007
Last modified:	February 9, 2010
This is version 65 of the entry and version 2 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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Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Sequences

References

Cross-references

Sequence databases

3D structure databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents