Skip Header

 
Contribute Send feedback
Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot A7ZR59 (SPEB_ECO24)

Last modified November 3, 2009. Version 17. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Agmatinase
    EC=3.5.3.11
Alternative name(s):
    Agmatine ureohydrolase
      Short name=AUH
Gene names
Name: speB
Ordered Locus Names: EcE24377A_3279
OrganismEscherichia coli O139:H28 (strain E24377A / ETEC) [Complete proteome] [HAMAP]
Taxonomic identifier331111 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length306 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

General annotation (Comments)

Function

Catalyzes the formation of putrescine from agmatine By similarity.

Catalytic activity

Agmatine + H2O = putrescine + urea. HAMAP MF_01418

Cofactor

Manganese By similarity.

Pathway

Amine and polyamine biosynthesis; putrescine biosynthesis via agmatine pathway; putrescine from agmatine: step 1/1. HAMAP MF_01418

Sequence similarities

Belongs to the arginase family. Agmatinase subfamily.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 306306Agmatinase HAMAP MF_01418
PRO_1000068494

Sites

Metal binding1261Manganese By similarity
Metal binding1491Manganese By similarity
Metal binding1511Manganese By similarity
Metal binding1531Manganese By similarity
Metal binding2301Manganese By similarity
Metal binding2321Manganese By similarity

Sequences

Sequence LengthMass (Da)Tools
A7ZR59-1 [UniParc].

Last modified October 23, 2007. Version 1.
Checksum: 48208BF2CF155570

FASTA30633,557
        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 DKDNGFTVLD ACQVNDRSVD DVIAQVKQIV GDMPVYLTFD IDCLDPAFAP 

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


AAKKGE 

« Hide

References

[1]"The pangenome structure of Escherichia coli: comparative genomic analysis of E. coli commensal and pathogenic isolates."
Rasko D.A., Rosovitz M.J., Myers G.S.A., Mongodin E.F., Fricke W.F., Gajer P., Crabtree J., Sebaihia M., Thomson N.R., Chaudhuri R., Henderson I.R., Sperandio V., Ravel J.
J. Bacteriol. 190:6881-6893(2008) [PubMed: 18676672] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

CP000800 Genomic DNA. Translation: ABV21194.1.
RefSeqYP_001464288.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGA7ZR59.

Genome annotation databases

GeneID5589638.
GenomeReviewsGene locus EcE24377A_3279 in contig CP000800_GR.
KEGGecw:EcE24377A_3279.

Organism-specific databases

CMRSearch...

Phylogenomic databases

OMACAQITAL.

Family and domain databases

HAMAPMF_01418.
[Tree]
InterProIPR005925. Agmatinase.
IPR006035. Ureohydrolase.
[Graphical view]
Gene3DG3DSA:3.40.800.10. Ureohydrolase. 1 hit.
PANTHERPTHR11358. Ureohydrolase. 1 hit.
PfamPF00491. Arginase. 1 hit.
[Graphical view]
TIGRFAMsTIGR01230. agmatinase. 1 hit.
PROSITEPS01053. ARGINASE_1. 1 hit.
PS51409. ARGINASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSPEB_ECO24
AccessionPrimary (citable) accession number: A7ZR59
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: October 23, 2007
Last modified: November 3, 2009
This is version 17 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents