B4F192 (ARGE_PROMH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Acetylornithine deacetylase
Short name=AO
Short name=Acetylornithinase
EC=3.5.1.16

Alternative name(s):
N-acetylornithinase
Short name=NAO

Gene names

Name:	argE
Ordered Locus Names:	PMI3236

Organism

Proteus mirabilis (strain HI4320) [Complete proteome] [HAMAP]

Taxonomic identifier

529507 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Proteus

Protein attributes

Sequence length	387 AA.
Sequence status	Complete.
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. HAMAP MF_01108 Glutathione By similarity. HAMAP MF_01108
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. HAMAP MF_01108
Subcellular location	Cytoplasm By similarity HAMAP MF_01108.
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: UniProtKB-KW 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: EC cobalt ion binding Inferred from electronic annotation. Source: InterPro metallopeptidase activity Inferred from electronic annotation. Source: InterPro zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 387	387	Acetylornithine deacetylase HAMAP MF_01108		PRO_1000137072
Sites
	Active site	82	1	By similarity
	Active site	144	1	By similarity
	Metal binding	80	1	Cobalt or zinc 1 By similarity
	Metal binding	112	1	Cobalt or zinc 1 By similarity
	Metal binding	112	1	Cobalt or zinc 2 By similarity
	Metal binding	145	1	Cobalt or zinc 2 By similarity
	Metal binding	169	1	Cobalt or zinc 1 By similarity
	Metal binding	355	1	Cobalt or zinc 2 By similarity

Sequences

	Sequence		Length	Mass (Da)
	B4F192 [UniParc]. Last modified September 23, 2008. Version 1. Checksum: 29F087B497C6F3EE	FASTA	387	42,600
	10 20 30 40 50 60 MNIKLPTFIE LYRQLIATPS ISATDAKTDQ SNEALINLLA NWLETLGFSI EIQPVPETRG 70 80 90 100 110 120 KFNLLATLGS GTGGLLLCGH TDTVPFDEGR WTQDPFTLTE KEGKLYGLGT ADMKGFFAFI 130 140 150 160 170 180 IDALRDIDTS QLTHPLYILA TADEETSMAG ARYFAANTAI RPDFAIIGEP TSLQPIRAHK 190 200 210 220 230 240 GHLSNAIRIT GQSGHSSDPE KGVNAIELMH ESITHLSTLR DRLKTRYNNP AFVIPYPTMN 250 260 270 280 290 300 FGYINGGDAA NRICACCELH MDIRPLPGLT LQDLDDLLHE TLAPVKARWP GRLSVEALHE 310 320 330 340 350 360 PIPGYECPTD HKMVAVIEKL LGEKAQTVNY CTEAPFIQAL CPTLVLGPGS IEQAHQPDEF 370 380 IDMAFIEPTR ELMGQLIENF CLAEKAK

References

[1]

"Complete genome sequence of uropathogenic Proteus mirabilis, a master of both adherence and motility." Pearson M.M., Sebaihia M., Churcher C., Quail M.A., Seshasayee A.S., Luscombe N.M., Abdellah Z., Arrosmith C., Atkin B., Chillingworth T., Hauser H., Jagels K., Moule S., Mungall K., Norbertczak H., Rabbinowitsch E., Walker D., Whithead S. , Thomson N.R., Rather P.N., Parkhill J., Mobley H.L.T. J. Bacteriol. 190:4027-4037(2008) [PubMed: 18375554] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: HI4320.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AM942759 Genomic DNA. Translation: CAR46337.1.
RefSeq	YP_002152921.1. NC_010554.1.
3D structure databases
ProteinModelPortal	B4F192.
ModBase	Search...
Protein-protein interaction databases
STRING	B4F192.
Protein family/group databases
MEROPS	M20.974.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	6802079.
GenomeReviews	Gene locus PMI3236 in contig AM942759_GR.
PATRIC	20521150. VBIProMir120933_3163.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG728841.
OMA	DIACAHQ.
ProtClustDB	PRK05111.
Family and domain databases
HAMAP	MF_01108. ArgE. [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]
SUPFAM	SSF55031. Peptidase_M20_dimer. 1 hit.
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_PROMH

Accession

Primary (citable) accession number: B4F192

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 14, 2009
Last sequence update:	September 23, 2008
Last modified:	January 25, 2012
This is version 26 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program