Reviewed, UniProtKB/Swiss-Prot Q9K4Z2 (ARGE_MORAB)

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

Organism

Moritella abyssi

Taxonomic identifier

111292 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Alteromonadales › Moritellaceae › Moritella

Protein attributes

Sequence length	382 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

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
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 – 382	382	Acetylornithine deacetylase HAMAP MF_01108		PRO_0000185243
Sites
	Active site	80	1	By similarity
	Active site	142	1	Proton acceptor By similarity
	Metal binding	78	1	Cobalt or zinc 1 By similarity
	Metal binding	110	1	Cobalt or zinc 1 By similarity
	Metal binding	110	1	Cobalt or zinc 2 By similarity
	Metal binding	143	1	Cobalt or zinc 2 By similarity
	Metal binding	167	1	Cobalt or zinc 1 By similarity
	Metal binding	354	1	Cobalt or zinc 2 By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9K4Z2-1 [UniParc]. Last modified October 1, 2000. Version 1. Checksum: 26120A6B43F42A3D	FASTA	382	41,980
	10 20 30 40 50 60 MQLPQFSELY KSLILIPSIS SLEKELDISN KPVIDLLSGW FSELGFSINI TSVPETNGKF 70 80 90 100 110 120 NLVATYGQGD GGLLLAGHTD TVPFDDDLWT KDPFKLTEKD DKWYGLGTID MKGFFAFVLE 130 140 150 160 170 180 ACKNIDLTKL DKPLRILATA DEETTMAGAR AIAAAQSFRP DYAVIGEPTG MVPVFMHKGH 190 200 210 220 230 240 MSEAIRITGR SGHSSDPANG INAIEIMHQV TGQLLQLQRK LKEQYACDHF VIPQPTLNFG 250 260 270 280 290 300 HVHGGDSPNR ICGSCELHID MRPIPGVNPD ELFMLLNQAL LPIIKQWPGA VDVYHLHEPI 310 320 330 340 350 360 PAYACNTDSA LIKLAEKLTG EAVIPVNYCT EAPFIQQLGC DTIVMGPGSI NQAHQPDEYL 370 380 DLSAIKPTQA IIQKLIEETC KN

References

[1]

"Evolution of arginine biosynthesis in the bacterial domain: novel gene-enzyme relationships from psychrophilic Moritella strains (Vibrionaceae) and evolutionary significance of N-alpha-acetyl ornithinase." Xu Y., Liang Z., Legrain C., Ruger H.J., Glansdorff N. J. Bacteriol. 182:1609-1615(2000) [PubMed: 10692366] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], CHARACTERIZATION. Strain: 2693.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AJ252021 Genomic DNA. Translation: CAB95019.1.
3D structure databases
ModBase	Search...
Protein family/group databases
MEROPS	M20.974.
Enzyme and pathway databases
BRENDA	3.5.1.16. 277322.
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_MORAB

Accession

Primary (citable) accession number: Q9K4Z2

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 23, 2003
Last sequence update:	October 1, 2000
Last modified:	June 16, 2009
This is version 53 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)