Reviewed, UniProtKB/Swiss-Prot P18335 (ARGD_ECOLI)

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, dtu
Ordered Locus Names:	b3359, JW3322

Organism

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

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	406 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Involved in both the arginine and lysine biosynthetic pathways. 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 Probable. 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 Probable. 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. HAMAP MF_01107
Sequence similarities	Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. ArgD subfamily.

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 Direct protein sequencing
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 Ref.5 Inferred from direct assay. Source: UniProtKB pyridoxal phosphate binding Inferred from electronic annotation. Source: InterPro succinyldiaminopimelate transaminase activity Ref.5 Inferred from direct assay. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed Ref.4 Ref.5
	Chain	2 – 406	405	Acetylornithine/succinyldiaminopimelate aminotransferase HAMAP MF_01107		PRO_0000112743
Regions
	Region	108 – 109	2	Pyridoxal phosphate binding By similarity
	Region	226 – 229	4	Pyridoxal phosphate binding By similarity
Sites
	Binding site	141	1	Pyridoxal phosphate; via carbonyl oxygen By similarity
	Binding site	144	1	N(2)-acetyl-L-ornithine By similarity
	Binding site	283	1	N(2)-acetyl-L-ornithine By similarity
	Binding site	284	1	Pyridoxal phosphate By similarity
Amino acid modifications
	Modified residue	255	1	N6-(pyridoxal phosphate)lysine By similarity
Experimental info
	Sequence conflict	245 – 247	3	GVT → ALA in AAA23480. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P18335-1 [UniParc]. Last modified January 23, 2007. Version 4. Checksum: 645AA1EBCA442214	FASTA	406	43,767
	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 FPISAMLTTA EIASAFHPGS HGSTYGGNPL ACAVAGAAFD 310 320 330 340 350 360 IINTPEVLEG IQAKRQRFVD HLQKIDQQYD VFSDIRGMGL LIGAELKPQY KGRARDFLYA 370 380 390 400 GAEAGVMVLN AGPDVMRFAP SLVVEDADID EGMQRFAHAV AKVVGA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Escherichia coli and Saccharomyces cerevisiae acetylornithine aminotransferase: evolutionary relationship with ornithine aminotransferase." Heimberg H., Boyen A., Crabeel M., Glansdorff N. Gene 90:69-78(1990) [PubMed: 2199330] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"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.
[3]	"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.
[4]	"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 2-13. Strain: K12 / EMG2.
[5]	"The dual biosynthetic capability of N-acetylornithine aminotransferase in arginine and lysine biosynthesis." Ledwidge R., Blanchard J.S. Biochemistry 38:3019-3024(1999) [PubMed: 10074354] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-27 AND 69-77, CHARACTERIZATION.

Cross-references

Sequence databases
EMBL GenBank DDBJ	M32796 Genomic DNA. Translation: AAA23480.1. U18997 Genomic DNA. Translation: AAA58156.1. U00096 Genomic DNA. Translation: AAC76384.1. AP009048 Genomic DNA. Translation: BAE77931.1.
PIR	B65130.
RefSeq	AP_004430.1. NP_417818.1.
3D structure databases
SMR	P18335. Positions 18-404.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-9138N.
STRING	P18335.
2-D gel databases
SWISS-2DPAGE	P18335.
2DBase-Ecoli	P18335.
Genome annotation databases
GeneID	947864.
GenomeReviews	Gene locus JW3322 in contig AP009048_GR. Gene locus b3359 in contig U00096_GR.
KEGG	ecj:JW3322. eco:b3359.
Organism-specific databases
EchoBASE	EB0064.
EcoGene	EG10066. argD.
CMR	Search...
Phylogenomic databases
eggNOG	COG4992.
HOGENOM	HBG725944.
OMA	ERTRVIT.
Enzyme and pathway databases
BioCyc	EcoCyc:ACETYLORNTRANSAM-MONOMER. ECOL168927:B3359-MONOMER. MetaCyc:ACETYLORNTRANSAM-MONOMER.
Gene expression databases
Genevestigator	P18335.
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...

Entry information

Entry name

ARGD_ECOLI

Accession

Primary (citable) accession number: P18335
Secondary accession number(s): Q2M725

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1990
Last sequence update:	January 23, 2007
Last modified:	February 9, 2010
This is version 95 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

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