Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P60657 (SPEB_SHIFL) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 72. 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:SF2927, S3129
OrganismShigella flexneri [Complete proteome] [HAMAP]
Taxonomic identifier623 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeShigella

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_0000173743

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
P60657 [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 Shigella flexneri 2a: insights into pathogenicity through comparison with genomes of Escherichia coli K12 and O157."
Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J., Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L., Xue Y. expand/collapse author list , Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H., Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.
Nucleic Acids Res. 30:4432-4441(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 301 / Serotype 2a.
[2]"Complete genome sequence and comparative genomics of Shigella flexneri serotype 2a strain 2457T."
Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G., Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T., Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.
Infect. Immun. 71:2775-2786(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 700930 / 2457T / Serotype 2a.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE005674 Genomic DNA. Translation: AAN44408.1.
AE014073 Genomic DNA. Translation: AAP18231.1.
RefSeqNP_708701.1. NC_004337.2.
NP_838421.1. NC_004741.1.

3D structure databases

ProteinModelPortalP60657.
SMRP60657. Positions 41-305.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING198214.SF2927.

Proteomic databases

PaxDbP60657.
PRIDEP60657.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAN44408; AAN44408; SF2927.
AAP18231; AAP18231; S3129.
GeneID1025911.
1077797.
KEGGsfl:SF2927.
sfx:S3129.
PATRIC18707951. VBIShiFle31049_3425.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

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_SHIFL
AccessionPrimary (citable) accession number: P60657
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 72 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