Q9KNT5 (ARGE_VIBCH) 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:	VC_2645

Organism

Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961) [Reference proteome] [HAMAP]

Taxonomic identifier

243277 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Vibrionales › Vibrionaceae › Vibrio › Vibrio cholerae › Vibrio cholerae O1 › Vibrio cholerae O1 biovar El Tor

Protein attributes

Sequence length	378 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Catalytic activity	N(2)-acetyl-L-ornithine + H2O = acetate + L-ornithine. HAMAP-Rule 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-Rule MF_01108
Subunit structure	Homodimer By similarity.
Subcellular location	Cytoplasm By similarity.
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 Reference proteome
Gene Ontology (GO)
Biological_process	arginine biosynthetic process Inferred from sequence or structural similarity Ref.1. Source: TIGR proteolysis Inferred from electronic annotation. Source: InterPro
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	acetylornithine deacetylase activity Inferred from sequence or structural similarity Ref.1. Source: TIGR 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: HAMAP
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 378	378	Acetylornithine deacetylase HAMAP-Rule MF_01108		PRO_0000185251
Sites
	Active site	78	1	By similarity
	Active site	140	1	Proton acceptor By similarity
	Metal binding	76	1	Cobalt or zinc 1 By similarity
	Metal binding	108	1	Cobalt or zinc 1 By similarity
	Metal binding	108	1	Cobalt or zinc 2 By similarity
	Metal binding	141	1	Cobalt or zinc 2 By similarity
	Metal binding	165	1	Cobalt or zinc 1 By similarity
	Metal binding	351	1	Cobalt or zinc 2 By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9KNT5 [UniParc]. Last modified October 1, 2000. Version 1. Checksum: F0CC5EC1892ECE8D	FASTA	378	41,964
	10 20 30 40 50 60 MPLPSFLEVY EGLISTSSIS STDARWDEGN EQVIAKLADW LSALGFSIQI EQVAPNKQNL 70 80 90 100 110 120 IAKLGSGEGG LLLAGHSDTV PFDEGRWNYN PHALTQVNNR FYGLGTADMK GFFAFIYEAV 130 140 150 160 170 180 KNVDWSKQTK PLYVLATCDE ETTMLGARHF TENAPFKPDY CIIGEPTSLV PIRAHKGHVA 190 200 210 220 230 240 NAIRVTGKSG HSSNPALGVN AIEIMHEVLF ALMQLRDRLI KEYHHPGFEI PTPTLNLGHI 250 260 270 280 290 300 HGGDSPNRIC GCCELHYDVR PLPGISLDGL DNLMHDALRE VQQKWPGRIE LVPLHDPIPG 310 320 330 340 350 360 YECAHDHPFI HGISEICEQE AQTVNYCTEA PFLQQVCPTL VLGPGSIDQA HQPDEFLAFE 370 FIDPTVRVLS RAMQKYCF

References

[1]

"DNA sequence of both chromosomes of the cholera pathogen Vibrio cholerae." Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L., Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R., Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D., Vamathevan J.J., Bass S. , Qin H., Dragoi I., Sellers P., McDonald L.A., Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L., Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M. Nature 406:477-483(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 39315 / El Tor Inaba N16961.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE003852 Genomic DNA. Translation: AAF95786.1.
PIR	C82049.
RefSeq	NP_232273.1. NC_002505.1.
3D structure databases
ProteinModelPortal	Q9KNT5.
ModBase	Search...
Protein-protein interaction databases
STRING	243277.VC2645.
Protein family/group databases
MEROPS	M20.974.
Protocols and materials databases
DNASU	2615662.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAF95786; AAF95786; VC_2645.
GeneID	2615662.
KEGG	vch:VC2645.
PATRIC	20084314. VBIVibCho83274_2523.
Phylogenomic databases
eggNOG	COG0624.
KO	K01438.
OMA	CAHQPGE.
ProtClustDB	PRK05111.
Enzyme and pathway databases
UniPathway	UPA00068; UER00110.
Family and domain databases
HAMAP	MF_01108. ArgE.
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_VIBCH

Accession

Primary (citable) accession number: Q9KNT5

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 23, 2003
Last sequence update:	October 1, 2000
Last modified:	May 1, 2013
This is version 81 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program