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P60651

- SPEB_ECOLI

UniProt

P60651 - SPEB_ECOLI

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Protein

Agmatinase

Gene

speB

Organism
Escherichia coli (strain K12)
Status
Reviewed - 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

Manganese.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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi126 – 1261Manganese 1By similarity
Metal bindingi149 – 1491Manganese 1By similarity
Metal bindingi149 – 1491Manganese 2By similarity
Metal bindingi151 – 1511Manganese 2By similarity
Metal bindingi153 – 1531Manganese 1By similarity
Sitei163 – 1631Important for catalytic activity
Metal bindingi230 – 2301Manganese 1By similarity
Metal bindingi230 – 2301Manganese 2By similarity
Metal bindingi232 – 2321Manganese 2By similarity

GO - Molecular functioni

  1. agmatinase activity Source: EcoCyc
  2. manganese ion binding Source: EcoCyc

GO - Biological processi

  1. putrescine biosynthetic process Source: EcoCyc
  2. putrescine biosynthetic process from arginine Source: UniProtKB-UniPathway
  3. spermidine biosynthetic process Source: UniProtKB-HAMAP
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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG10960. speB.

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi163 – 1631H → F: Loss of activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 306306AgmatinasePRO_0000173731Add
BLAST

Proteomic databases

PaxDbiP60651.
PRIDEiP60651.

2D gel databases

SWISS-2DPAGEP60651.

Expressioni

Gene expression databases

GenevestigatoriP60651.

Interactioni

Protein-protein interaction databases

DIPiDIP-10906N.
IntActiP60651. 7 interactions.
STRINGi511145.b2937.

Structurei

3D structure databases

ProteinModelPortaliP60651.
SMRiP60651. Positions 41-305.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the arginase family. Agmatinase subfamily.Curated

Phylogenomic databases

eggNOGiCOG0010.
HOGENOMiHOG000204320.
InParanoidiP60651.
KOiK01480.
OMAiKPDYSLY.
OrthoDBiEOG6R2GW5.
PhylomeDBiP60651.

Family and domain databases

Gene3Di3.40.800.10. 1 hit.
HAMAPiMF_01418. SpeB.
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:
EMBL
GenBank
DDBJ
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.
YP_491136.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC75974; AAC75974; b2937.
BAE77000; BAE77000; BAE77000.
GeneIDi12931916.
947715.
KEGGiecj:Y75_p2867.
eco:b2937.
PATRICi32121286. VBIEscCol129921_3031.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 .
PIRi C42604.
G85950.
RefSeqi NP_417412.1. NC_000913.3.
YP_491136.1. NC_007779.1.

3D structure databases

ProteinModelPortali P60651.
SMRi P60651. Positions 41-305.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-10906N.
IntActi P60651. 7 interactions.
STRINGi 511145.b2937.

2D gel databases

SWISS-2DPAGE P60651.

Proteomic databases

PaxDbi P60651.
PRIDEi P60651.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAC75974 ; AAC75974 ; b2937 .
BAE77000 ; BAE77000 ; BAE77000 .
GeneIDi 12931916.
947715.
KEGGi ecj:Y75_p2867.
eco:b2937.
PATRICi 32121286. VBIEscCol129921_3031.

Organism-specific databases

EchoBASEi EB0953.
EcoGenei EG10960. speB.

Phylogenomic databases

eggNOGi COG0010.
HOGENOMi HOG000204320.
InParanoidi P60651.
KOi K01480.
OMAi KPDYSLY.
OrthoDBi EOG6R2GW5.
PhylomeDBi P60651.

Enzyme and pathway databases

UniPathwayi UPA00534 ; UER00287 .
BioCyci EcoCyc:AGMATIN-MONOMER.
ECOL316407:JW2904-MONOMER.
MetaCyc:AGMATIN-MONOMER.

Miscellaneous databases

PROi P60651.

Gene expression databases

Genevestigatori P60651.

Family and domain databases

Gene3Di 3.40.800.10. 1 hit.
HAMAPi MF_01418. SpeB.
InterProi IPR023694. Agmatinase.
IPR005925. Agmatinase-rel.
IPR006035. Ureohydrolase.
IPR023696. Ureohydrolase_domain.
IPR020855. Ureohydrolase_Mn_BS.
[Graphical view ]
PANTHERi PTHR11358. PTHR11358. 1 hit.
Pfami PF00491. Arginase. 1 hit.
[Graphical view ]
PIRSFi PIRSF036979. Arginase. 1 hit.
TIGRFAMsi TIGR01230. agmatinase. 1 hit.
PROSITEi PS01053. ARGINASE_1. 1 hit.
PS51409. ARGINASE_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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.

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: October 29, 2014
This is version 84 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

External Data

Dasty 3