P60655 (SPEB_SALTI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Agmatinase
EC=3.5.3.11

Alternative name(s):
Agmatine ureohydrolase
Short name=AUH

Gene names

Name:	speB
Ordered Locus Names:	STY3238, t2998

Organism

Salmonella typhi [Complete proteome] [HAMAP]

Taxonomic identifier

90370 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Salmonella › Salmonella choleraesuis › Salmonella enterica I

Protein attributes

Sequence length	306 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Catalyzes the formation of putrescine from agmatine By similarity. HAMAP-Rule MF_01418
Catalytic activity	Agmatine + H2O = putrescine + urea. HAMAP-Rule MF_01418
Cofactor	Manganese By similarity.
Pathway	Amine and polyamine biosynthesis; putrescine biosynthesis via agmatine pathway; putrescine from agmatine: step 1/1. HAMAP-Rule MF_01418
Sequence similarities	Belongs to the arginase family. Agmatinase subfamily.

Ontologies

Keywords
Biological process	Polyamine biosynthesis Putrescine biosynthesis Spermidine biosynthesis
Ligand	Manganese Metal-binding
Molecular function	Hydrolase
Technical term	Complete proteome
Gene Ontology (GO)
Biological_process	putrescine biosynthetic process from arginine Inferred from electronic annotation. Source: UniProtKB-UniPathway spermidine biosynthetic process Inferred from electronic annotation. Source: HAMAP
Molecular_function	agmatinase activity Inferred from electronic annotation. Source: HAMAP manganese 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 – 306	306	Agmatinase HAMAP-Rule MF_01418		PRO_0000173741
Sites
	Metal binding	126	1	Manganese By similarity
	Metal binding	149	1	Manganese By similarity
	Metal binding	151	1	Manganese By similarity
	Metal binding	153	1	Manganese By similarity
	Metal binding	230	1	Manganese By similarity
	Metal binding	232	1	Manganese By similarity

Sequences

	Sequence		Length	Mass (Da)
	P60655 [UniParc]. Last modified March 29, 2004. Version 1. Checksum: 6C26A30691F2C3D3	FASTA	306	33,603
	10 20 30 40 50 60 MSTLGHQYDN SLVSNAFGFL RLPMNFQPYD SDADWVITGV PFDMATSGRA GGRHGPAAIR 70 80 90 100 110 120 QVSTNLAWEH HRFPWNFDMR ERLNVVDCGD LVYAFGDARE MSEKLQAHAE KLLSAGKRML 130 140 150 160 170 180 SFGGDHFVTL PLLRAHAKHF GKMALVHFDA HTDTYANGCE FDHGTMFYTA PKEGLIDPHH 190 200 210 220 230 240 SVQIGIRTEF DKDNGFTVLD ACQVNDRGVD DILAQVKQIV GDMPVYLTFD IDCLDPAFAP 250 260 270 280 290 300 GTGTPVIGGL TSDRAIKLVR GLKDLNIVGM DVVEVAPAYD QSEITALAAA TLALEMLYIQ AAKKGE

References

[1]

"Comparative genomics of Salmonella enterica serovar Typhi strains Ty2 and CT18." Deng W., Liou S.-R., Plunkett G. III, Mayhew G.F., Rose D.J., Burland V., Kodoyianni V., Schwartz D.C., Blattner F.R. J. Bacteriol. 185:2330-2337(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 700931 / Ty2.

[2]

"Complete genome sequence of a multiple drug resistant Salmonella enterica serovar Typhi CT18." Parkhill J., Dougan G., James K.D., Thomson N.R., Pickard D., Wain J., Churcher C.M., Mungall K.L., Bentley S.D., Holden M.T.G., Sebaihia M., Baker S., Basham D., Brooks K., Chillingworth T., Connerton P., Cronin A., Davis P. , Davies R.M., Dowd L., White N., Farrar J., Feltwell T., Hamlin N., Haque A., Hien T.T., Holroyd S., Jagels K., Krogh A., Larsen T.S., Leather S., Moule S., O'Gaora P., Parry C., Quail M.A., Rutherford K.M., Simmonds M., Skelton J., Stevens K., Whitehead S., Barrell B.G. Nature 413:848-852(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: CT18.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE014613 Genomic DNA. Translation: AAO70550.1. AL627277 Genomic DNA. Translation: CAD02910.1.
RefSeq	NP_806690.1. NC_004631.1.
3D structure databases
ProteinModelPortal	P60655.
ModBase	Search...
Protein-protein interaction databases
STRING	220341.STY3238.
Proteomic databases
PRIDE	P60655.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAO70550; AAO70550; t2998. CAD02910; CAD02910; CAD02910.
GeneID	1068566.
KEGG	stt:t2998.
PATRIC	18544550. VBISalEnt120419_3301.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HOG000204320.
KO	K01480.
OMA	MRRKYTK.
ProtClustDB	PRK02190.
Enzyme and pathway databases
UniPathway	UPA00534; UER00287.
Family and domain databases
Gene3D	3.40.800.10. 1 hit.
HAMAP	MF_01418. SpeB.
InterPro	IPR023694. Agmatinase. IPR005925. Agmatinase-rel. IPR006035. Ureohydrolase. IPR023696. Ureohydrolase_domain. IPR020855. Ureohydrolase_Mn_BS. [Graphical view]
PANTHER	PTHR11358. PTHR11358. 1 hit.
Pfam	PF00491. Arginase. 1 hit. [Graphical view]
PIRSF	PIRSF036979. Arginase. 1 hit.
TIGRFAMs	TIGR01230. agmatinase. 1 hit.
PROSITE	PS01053. ARGINASE_1. 1 hit. PS51409. ARGINASE_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

SPEB_SALTI

Accession

Primary (citable) accession number: P60655
Secondary accession number(s): Q8XG05

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 29, 2004
Last sequence update:	March 29, 2004
Last modified:	May 1, 2013
This is version 65 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program