Reviewed, UniProtKB/Swiss-Prot P59085 (ARGE_BUCAP)

Names and origin

Protein names

Recommended name:
    Acetylornithine deacetylase
      Short name=Acetylornithinase
      Short name=AO
    EC=3.5.1.16
Alternative name(s):
    N-acetylornithinase
      Short name=NAO

Gene names

Name:	argE
Ordered Locus Names:	BUsg_044

Organism

Buchnera aphidicola subsp. Schizaphis graminum [Complete proteome] [HAMAP]

Taxonomic identifier

98794 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Buchnera

Protein attributes

Sequence length	381 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

General annotation (Comments)

Catalytic activity	N(2)-acetyl-L-ornithine + H2O = acetate + L-ornithine. HAMAP MF_01108
Cofactor	Binds 2 zinc or cobalt ions per subunit By similarity. Glutathione By similarity.
Pathway	Amino-acid biosynthesis; L-arginine biosynthesis; L-ornithine from N(2)-acetyl-L-ornithine (linear): step 1/1. HAMAP MF_01108
Subunit structure	Homodimer By similarity.
Subcellular location	Cytoplasm Probable.
Sequence similarities	Belongs to the peptidase M20A family. ArgE subfamily.

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Arginine biosynthesis
Cellular component	Cytoplasm
Ligand	Cobalt Metal-binding Zinc
Molecular function	Hydrolase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	arginine biosynthetic process Inferred from electronic annotation. Source: HAMAP proteolysis Inferred from electronic annotation. Source: InterPro
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	acetylornithine deacetylase activity Inferred from electronic annotation. Source: HAMAP cobalt ion binding Inferred from electronic annotation. Source: UniProtKB-KW metallopeptidase activity Inferred from electronic annotation. Source: InterPro protein dimerization activity Inferred from electronic annotation. Source: InterPro zinc ion binding Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 381	381	Acetylornithine deacetylase HAMAP MF_01108		PRO_0000185239
Sites
	Active site	81	1	By similarity
	Active site	143	1	Proton acceptor By similarity
	Metal binding	79	1	Cobalt or zinc 1 By similarity
	Metal binding	111	1	Cobalt or zinc 1 By similarity
	Metal binding	111	1	Cobalt or zinc 2 By similarity
	Metal binding	144	1	Cobalt or zinc 2 By similarity
	Metal binding	168	1	Cobalt or zinc 1 By similarity
	Metal binding	354	1	Cobalt or zinc 2 By similarity

Sequences

	Sequence		Length	Mass (Da)
	P59085-1 [UniParc]. Last modified November 8, 2002. Version 1. Checksum: 1CB8904C4B88DB9E	FASTA	381	43,122
	10 20 30 40 50 60 MIRKIPSFIK IYESLIKIPT ISSLNNKLDQ SNKVLIDLLS NYFSELNFLI NIKNIPNTNK 70 80 90 100 110 120 FNMLASFGDG KGGILFSGHT DTVDFDEHLW TKDPFKLTEK NNKLYGLGTV DMKGFFAFIL 130 140 150 160 170 180 DALCSINIKS IKKPIYILAT ANEETDMSGA RYFIQSSSIK PDFIIIGEPT SLKLVKAHKG 190 200 210 220 230 240 HVSYSIDVVG NTGHSSNPAN GINSIEIMHL VIKKLLKLKI YLREKYFHKD FSIGYPTMNF 250 260 270 280 290 300 SSINGGNAIN RICALCNLKF EIRPTPGLTL TQIEILIQEM LQAIFKKWPN RIFLKNLFFS 310 320 330 340 350 360 VPPYEFPKEK KIIKKIENSC QLKPTTANYC TEAPFLGKIG PTLILGPGSI QQAHNADEYL 370 380 DCSFIKPTKK IIRKLIKNFC Y

References

[1]

"50 million years of genomic stasis in endosymbiotic bacteria." Tamas I., Klasson L., Canbaeck B., Naeslund A.K., Eriksson A.-S., Wernegreen J.J., Sandstroem J.P., Moran N.A., Andersson S.G.E. Science 296:2376-2379(2002) [PubMed: 12089438] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	AE013218 Genomic DNA. Translation: AAM67615.1.
RefSeq	NP_660404.1.
3D structure databases
ModBase	Search...
Protein family/group databases
MEROPS	M20.974.
Genome annotation databases
GeneID	1005860.
GenomeReviews	Gene locus BUsg_044 in contig AE013218_GR.
KEGG	bas:BUsg044.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	P59085.
OMA	QPLMILA.
Enzyme and pathway databases
BioCyc	BAPH198804:BUSG044-MON.
Family and domain databases
HAMAP	MF_01108. [Tree]
InterPro	IPR010169. AcOrn-deacetyl. IPR001261. ArgE/DapE_CS. IPR002933. Peptidase_M20. IPR011650. Peptidase_M20_dimer. [Graphical view]
Pfam	PF07687. M20_dimer. 1 hit. PF01546. Peptidase_M20. 1 hit. [Graphical view]
TIGRFAMs	TIGR01892. AcOrn-deacetyl. 1 hit.
PROSITE	PS00758. ARGE_DAPE_CPG2_1. 1 hit. PS00759. ARGE_DAPE_CPG2_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ARGE_BUCAP

Accession

Primary (citable) accession number: P59085

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 8, 2002
Last sequence update:	November 8, 2002
Last modified:	November 3, 2009
This is version 55 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)