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P60651 (SPEB_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 81. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:b2937, JW2904
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length306 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the formation of putrescine from agmatine. Ref.6

Catalytic activity

Agmatine + H2O = putrescine + urea. HAMAP-Rule MF_01418

Cofactor

Manganese. Ref.5

Enzyme regulation

The expression of auh activity is antagonistically regulated by cyclic AMP and agmatine. In the presence of the cAMP receptor protein, cAMP represses the expression of AUH, while agmatine induces it. 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_0000173731

Sites

Metal binding1261Manganese 1 By similarity
Metal binding1491Manganese 1 By similarity
Metal binding1491Manganese 2 By similarity
Metal binding1511Manganese 2 By similarity
Metal binding1531Manganese 1 By similarity
Metal binding2301Manganese 1 By similarity
Metal binding2301Manganese 2 By similarity
Metal binding2321Manganese 2 By similarity
Site1631Important for catalytic activity

Experimental info

Mutagenesis1631H → F: Loss of activity. Ref.6

Sequences

Sequence LengthMass (Da)Tools
P60651 [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

« Hide 'large scale' references
[1]"Analysis and sequence of the speB gene encoding agmatine ureohydrolase, a putrescine biosynthetic enzyme in Escherichia coli."
Szumanski M.B.W., Boyle S.M.
J. Bacteriol. 172:538-547(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1462(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[3]"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[4]"Nucleotide sequence and analysis of the speA gene encoding biosynthetic arginine decarboxylase in Escherichia coli."
Moore R.C., Boyle S.M.
J. Bacteriol. 172:4631-4640(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-45.
[5]"Manganese is essential for catalytic activity of Escherichia coli agmatinase."
Carvajal N., Lopez V., Salas M., Uribe E., Herrera P., Cerpa J.
Biochem. Biophys. Res. Commun. 258:808-811(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: COFACTOR.
[6]"Evidence that histidine-163 is critical for catalytic activity, but not for substrate binding to Escherichia coli agmatinase."
Carvajal N., Olate J., Salas M., Lopez V., Cerpa J., Herrera P., Uribe E.
Biochem. Biophys. Res. Commun. 264:196-200(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, MUTAGENESIS OF HIS-163.
[7]"Influence of cyclic AMP, agmatine, and a novel protein encoded by a flanking gene on speB (agmatine ureohydrolase) in Escherichia coli."
Szumanski M.B.W., Boyle S.M.
J. Bacteriol. 174:758-764(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: REGULATION.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M32363 Genomic DNA. Translation: AAA83909.1.
U28377 Genomic DNA. Translation: AAA69104.1.
U00096 Genomic DNA. Translation: AAC75974.1.
AP009048 Genomic DNA. Translation: BAE77000.1.
M31770 Genomic DNA. Translation: AAA24647.1.
PIRC42604.
G85950.
RefSeqNP_417412.1. NC_000913.3.
YP_491136.1. NC_007779.1.

3D structure databases

ProteinModelPortalP60651.
SMRP60651. Positions 41-305.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-10906N.
IntActP60651. 7 interactions.
STRING511145.b2937.

2D gel databases

SWISS-2DPAGEP60651.

Proteomic databases

PaxDbP60651.
PRIDEP60651.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC75974; AAC75974; b2937.
BAE77000; BAE77000; BAE77000.
GeneID12931916.
947715.
KEGGecj:Y75_p2867.
eco:b2937.
PATRIC32121286. VBIEscCol129921_3031.

Organism-specific databases

EchoBASEEB0953.
EcoGeneEG10960. speB.

Phylogenomic databases

eggNOGCOG0010.
HOGENOMHOG000204320.
KOK01480.
OMAKPDYSLY.
OrthoDBEOG6R2GW5.
PhylomeDBP60651.
ProtClustDBPRK02190.

Enzyme and pathway databases

BioCycEcoCyc:AGMATIN-MONOMER.
ECOL316407:JW2904-MONOMER.
MetaCyc:AGMATIN-MONOMER.
UniPathwayUPA00534; UER00287.

Gene expression databases

GenevestigatorP60651.

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...

Other

PROP60651.

Entry information

Entry nameSPEB_ECOLI
AccessionPrimary (citable) accession number: P60651
Secondary accession number(s): P16936, Q2M9Q6
Entry history
Integrated into UniProtKB/Swiss-Prot: March 29, 2004
Last sequence update: March 29, 2004
Last modified: April 16, 2014
This is version 81 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

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene