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Reviewed, UniProtKB/Swiss-Prot A7MJQ1 (SPEB_ENTS8)

Last modified February 9, 2010. Version 20. 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: ESA_00403
OrganismEnterobacter sakazakii (strain ATCC BAA-894) [Complete proteome] [HAMAP]
Taxonomic identifier290339 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeCronobacter

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 MF_01418

Catalytic activity

Agmatine + H2O = putrescine + urea. HAMAP MF_01418

Cofactor

Manganese By similarity. HAMAP MF_01418

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_1000024281

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
A7MJQ1-1 [UniParc].

Last modified October 2, 2007. Version 1.
Checksum: 6D2EE74BFD75D248

FASTA30633,572
        10         20         30         40         50         60 
MNTLGHQYDN SLVSNAFGFL RLPLNFMPYD SDAEWVITGI PFDMATSGRS GSRFGPAAIR 

        70         80         90        100        110        120 
QVSTNLAWEG NRFPWNFDMR KRLNVVDCGD LVYAFGDARE MSEKLQAHAE KLLAAGKRML 

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

       190        200        210        220        230        240 
SVQIGIRTEF DKDNGFTVLD APQVNDRTVD DVVAQVKQIV GDMPVYLTFD IDCLDPAFAP 

       250        260        270        280        290        300 
GTGTPVIGGL TSDRALKLLR GIQDLNIVGM DIVEVAPAYD QSDITALAAA TLALEMLYIQ 


AAKKGE 

« Hide

References

[1]McClelland M., Sanderson E.K., Porwollik S., Spieth J., Clifton W.S., Fulton B., Wollam A., Shah N., Pepin K., Bhonagiri V., Nash W., Johnson M., Thiruvilangam P., Wilson R.
Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000783 Genomic DNA. Translation: ABU75701.1.
RefSeqYP_001436537.1.

3D structure databases

SMRA7MJQ1. Positions 18-301.
ModBaseSearch...

Protein-protein interaction databases

STRINGA7MJQ1.

Genome annotation databases

GeneID5549598.
GenomeReviewsGene locus ESA_00403 in contig CP000783_GR.
KEGGesa:ESA_00403.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0010.
HOGENOMHBG391953.
OMATNLAWEG.

Family and domain databases

HAMAPMF_01418. SpeB.
[Tree]
InterProIPR005925. Agmatinase.
IPR006035. Ureohydrolase.
IPR020855. Ureohydrolase_Mn_BS.
[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_ENTS8
AccessionPrimary (citable) accession number: A7MJQ1
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: October 2, 2007
Last modified: February 9, 2010
This is version 20 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