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Protein

Agmatinase

Gene

speB

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the formation of putrescine from agmatine.1 Publication

Catalytic activityi

Agmatine + H2O = putrescine + urea.

Cofactori

Mn2+1 Publication

Enzyme regulationi

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.

Pathwayi: putrescine biosynthesis via agmatine pathway

This protein is involved in step 1 of the subpathway that synthesizes putrescine from agmatine.
Proteins known to be involved in this subpathway in this organism are:
  1. Agmatinase (speB)
This subpathway is part of the pathway putrescine biosynthesis via agmatine pathway, which is itself part of Amine and polyamine biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes putrescine from agmatine, the pathway putrescine biosynthesis via agmatine pathway and in Amine and polyamine biosynthesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi126Manganese 1By similarity1
Metal bindingi149Manganese 1By similarity1
Metal bindingi149Manganese 2By similarity1
Metal bindingi151Manganese 2By similarity1
Metal bindingi153Manganese 1By similarity1
Sitei163Important for catalytic activity1
Metal bindingi230Manganese 1By similarity1
Metal bindingi230Manganese 2By similarity1
Metal bindingi232Manganese 2By similarity1

GO - Molecular functioni

  • agmatinase activity Source: EcoCyc
  • manganese ion binding Source: EcoCyc

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Polyamine biosynthesis, Putrescine biosynthesis, Spermidine biosynthesis

Keywords - Ligandi

Manganese, Metal-binding

Enzyme and pathway databases

BioCyciEcoCyc:AGMATIN-MONOMER.
ECOL316407:JW2904-MONOMER.
MetaCyc:AGMATIN-MONOMER.
UniPathwayiUPA00534; UER00287.

Names & Taxonomyi

Protein namesi
Recommended name:
Agmatinase (EC:3.5.3.11)
Alternative name(s):
Agmatine ureohydrolase
Short name:
AUH
Gene namesi
Name:speB
Ordered Locus Names:b2937, JW2904
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10960. speB.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: EcoCyc
Complete GO annotation...

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi163H → F: Loss of activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001737311 – 306AgmatinaseAdd BLAST306

Proteomic databases

EPDiP60651.
PaxDbiP60651.
PRIDEiP60651.

2D gel databases

SWISS-2DPAGEP60651.

Interactioni

Protein-protein interaction databases

BioGridi4260910. 13 interactors.
DIPiDIP-10906N.
IntActiP60651. 7 interactors.
STRINGi511145.b2937.

Structurei

3D structure databases

ProteinModelPortaliP60651.
SMRiP60651.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the arginase family. Agmatinase subfamily.Curated

Phylogenomic databases

eggNOGiENOG4105CYW. Bacteria.
COG0010. LUCA.
HOGENOMiHOG000204320.
InParanoidiP60651.
KOiK01480.
OMAiYELTTIM.
PhylomeDBiP60651.

Family and domain databases

Gene3Di3.40.800.10. 1 hit.
HAMAPiMF_01418. SpeB. 1 hit.
InterProiIPR023694. Agmatinase.
IPR005925. Agmatinase-rel.
IPR006035. Ureohydrolase.
IPR023696. Ureohydrolase_domain.
IPR020855. Ureohydrolase_Mn_BS.
[Graphical view]
PANTHERiPTHR11358. PTHR11358. 1 hit.
PfamiPF00491. Arginase. 1 hit.
[Graphical view]
PIRSFiPIRSF036979. Arginase. 1 hit.
TIGRFAMsiTIGR01230. agmatinase. 1 hit.
PROSITEiPS01053. ARGINASE_1. 1 hit.
PS51409. ARGINASE_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P60651-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSTLGHQYDN SLVSNAFGFL RLPMNFQPYD SDADWVITGV PFDMATSGRA
60 70 80 90 100
GGRHGPAAIR QVSTNLAWEH NRFPWNFDMR ERLNVVDCGD LVYAFGDARE
110 120 130 140 150
MSEKLQAHAE KLLAAGKRML SFGGDHFVTL PLLRAHAKHF GKMALVHFDA
160 170 180 190 200
HTDTYANGCE FDHGTMFYTA PKEGLIDPNH SVQIGIRTEF DKDNGFTVLD
210 220 230 240 250
ACQVNDRSVD DVIAQVKQIV GDMPVYLTFD IDCLDPAFAP GTGTPVIGGL
260 270 280 290 300
TSDRAIKLVR GLKDLNIVGM DVVEVAPAYD QSEITALAAA TLALEMLYIQ

AAKKGE
Length:306
Mass (Da):33,557
Last modified:March 29, 2004 - v1
Checksum:i48208BF2CF155570
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiC42604.
G85950.
RefSeqiNP_417412.1. NC_000913.3.
WP_000105566.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC75974; AAC75974; b2937.
BAE77000; BAE77000; BAE77000.
GeneIDi947715.
KEGGiecj:JW2904.
eco:b2937.
PATRICi32121286. VBIEscCol129921_3031.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiC42604.
G85950.
RefSeqiNP_417412.1. NC_000913.3.
WP_000105566.1. NZ_LN832404.1.

3D structure databases

ProteinModelPortaliP60651.
SMRiP60651.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4260910. 13 interactors.
DIPiDIP-10906N.
IntActiP60651. 7 interactors.
STRINGi511145.b2937.

2D gel databases

SWISS-2DPAGEP60651.

Proteomic databases

EPDiP60651.
PaxDbiP60651.
PRIDEiP60651.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC75974; AAC75974; b2937.
BAE77000; BAE77000; BAE77000.
GeneIDi947715.
KEGGiecj:JW2904.
eco:b2937.
PATRICi32121286. VBIEscCol129921_3031.

Organism-specific databases

EchoBASEiEB0953.
EcoGeneiEG10960. speB.

Phylogenomic databases

eggNOGiENOG4105CYW. Bacteria.
COG0010. LUCA.
HOGENOMiHOG000204320.
InParanoidiP60651.
KOiK01480.
OMAiYELTTIM.
PhylomeDBiP60651.

Enzyme and pathway databases

UniPathwayiUPA00534; UER00287.
BioCyciEcoCyc:AGMATIN-MONOMER.
ECOL316407:JW2904-MONOMER.
MetaCyc:AGMATIN-MONOMER.

Miscellaneous databases

PROiP60651.

Family and domain databases

Gene3Di3.40.800.10. 1 hit.
HAMAPiMF_01418. SpeB. 1 hit.
InterProiIPR023694. Agmatinase.
IPR005925. Agmatinase-rel.
IPR006035. Ureohydrolase.
IPR023696. Ureohydrolase_domain.
IPR020855. Ureohydrolase_Mn_BS.
[Graphical view]
PANTHERiPTHR11358. PTHR11358. 1 hit.
PfamiPF00491. Arginase. 1 hit.
[Graphical view]
PIRSFiPIRSF036979. Arginase. 1 hit.
TIGRFAMsiTIGR01230. agmatinase. 1 hit.
PROSITEiPS01053. ARGINASE_1. 1 hit.
PS51409. ARGINASE_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiSPEB_ECOLI
AccessioniPrimary (citable) accession number: P60651
Secondary accession number(s): P16936, Q2M9Q6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 29, 2004
Last sequence update: March 29, 2004
Last modified: November 2, 2016
This is version 97 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.