Agmatinase - Escherichia coli (strain 55989 / EAEC)

Preferred order of sections

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:	EC55989_3229

Organism

Escherichia coli (strain 55989 / EAEC) [Complete proteome] [HAMAP]

Taxonomic identifier

585055 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia ›

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. HAMAP-Rule MF_01418
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_1000184847

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)

Tools

B7LFJ6 [UniParc].

Last modified February 10, 2009. Version 1.
Checksum: 1A208A7CF478E3AB
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FASTA

306

33,542

        10         20         30         40         50         60 
MSTLGHQYDN SLVSNAFGFL RLPMNFQPYD SDADWVITGV PFDMATSGRA GGRHGPAAIR 

        70         80         90        100        110        120 
QVSTNLAWEH NRFPWNFDMR ERLNVVDCGD LVYAFGDARE MSEKLQAHAE KLLAAGKRML 

       130        140        150        160        170        180 
SFGGDHFVTL PLLRAHAKHF GKMALVHFDA HTDTYANGCE FDHGTMFYTA PKEGLIDPNH 

       190        200        210        220        230        240 
SVQIGIRTEF DIDNGFTVLD ACQVNDRSVD DVIAQVKQIV GDMPVYLTFD IDCLDPAFAP 

       250        260        270        280        290        300 
GTGTPVIGGL TSDRAIKLVR GLKDLNIVGM DVVEVAPAYD QSEITALAAA TLALEMLYIQ 


AAKKGE

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References

[1]

"Organised genome dynamics in the Escherichia coli species results in highly diverse adaptive paths."
Touchon M., Hoede C., Tenaillon O., Barbe V., Baeriswyl S., Bidet P., Bingen E., Bonacorsi S., Bouchier C., Bouvet O., Calteau A., Chiapello H., Clermont O., Cruveiller S., Danchin A., Diard M., Dossat C., Karoui M.E.

Denamur E.
PLoS Genet. 5:E1000344-E1000344(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 55989 / EAEC.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CU928145 Genomic DNA. Translation: CAU99217.1.
RefSeq	YP_002404201.1. NC_011748.1.
3D structure databases
ProteinModelPortal	B7LFJ6.
SMR	B7LFJ6. Positions 12-303.
ModBase	Search...
Protein-protein interaction databases
STRING	585055.EC55989_3229.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	CAU99217; CAU99217; EC55989_3229.
GeneID	7148863.
KEGG	eck:EC55989_3229.
PATRIC	38479998. VBIEscCol113220_3270.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0010.
HOGENOM	HOG000204320.
KO	K01480.
OMA	FIMANAS.
ProtClustDB	PRK02190.
Enzyme and pathway databases
BioCyc	ECOL585055:GJOM-3299-MONOMER.
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_ECO55

Accession

Primary (citable) accession number: B7LFJ6

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 28, 2009
Last sequence update:	February 10, 2009
Last modified:	May 1, 2013
This is version 34 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Sites

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents