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P60652 (SPEB_ECO57) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 69. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

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:Z4281, ECs3812
OrganismEscherichia coli O157:H7 [Complete proteome] [HAMAP]
Taxonomic identifier83334 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length306 AA.
Sequence statusComplete.
Protein existenceInferred 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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 306306Agmatinase HAMAP-Rule MF_01418
PRO_0000173732

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
P60652 [UniParc].

Last modified March 29, 2004. 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]"Genome sequence of enterohaemorrhagic Escherichia coli O157:H7."
Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J., Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G., Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J., Davis N.W. expand/collapse author list , Lim A., Dimalanta E.T., Potamousis K., Apodaca J., Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A., Blattner F.R.
Nature 409:529-533(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: O157:H7 / EDL933 / ATCC 700927 / EHEC.
[2]"Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and genomic comparison with a laboratory strain K-12."
Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K., Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T. expand/collapse author list , Kuhara S., Shiba T., Hattori M., Shinagawa H.
DNA Res. 8:11-22(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: O157:H7 / Sakai / RIMD 0509952 / EHEC.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE005174 Genomic DNA. Translation: AAG58067.1.
BA000007 Genomic DNA. Translation: BAB37235.1.
PIRD91105.
RefSeqNP_289508.1. NC_002655.2.
NP_311839.1. NC_002695.1.

3D structure databases

ProteinModelPortalP60652.
SMRP60652. Positions 41-305.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING155864.Z4281.

Proteomic databases

PRIDEP60652.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAG58067; AAG58067; Z4281.
BAB37235; BAB37235; BAB37235.
GeneID916365.
958399.
KEGGece:Z4281.
ecs:ECs3812.
PATRIC18357115. VBIEscCol44059_3736.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0010.
HOGENOMHOG000204320.
KOK01480.
OMAKPDYSLY.
OrthoDBEOG6R2GW5.
ProtClustDBPRK02190.

Enzyme and pathway databases

BioCycECOL386585:GJFA-3779-MONOMER.
ECOO157:SPEB-MONOMER.
UniPathwayUPA00534; UER00287.

Family and domain databases

Gene3D3.40.800.10. 1 hit.
HAMAPMF_01418. SpeB.
InterProIPR023694. Agmatinase.
IPR005925. Agmatinase-rel.
IPR006035. Ureohydrolase.
IPR023696. Ureohydrolase_domain.
IPR020855. Ureohydrolase_Mn_BS.
[Graphical view]
PANTHERPTHR11358. PTHR11358. 1 hit.
PfamPF00491. Arginase. 1 hit.
[Graphical view]
PIRSFPIRSF036979. Arginase. 1 hit.
TIGRFAMsTIGR01230. agmatinase. 1 hit.
PROSITEPS01053. ARGINASE_1. 1 hit.
PS51409. ARGINASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSPEB_ECO57
AccessionPrimary (citable) accession number: P60652
Secondary accession number(s): P16936
Entry history
Integrated into UniProtKB/Swiss-Prot: March 29, 2004
Last sequence update: March 29, 2004
Last modified: February 19, 2014
This is version 69 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways