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Protein

Agmatinase

Gene

speB

Organism
Escherichia coli O45:K1 (strain S88 / ExPEC)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Protein inferred from homologyi

Functioni

Catalyzes the formation of putrescine from agmatine.UniRule annotation

Catalytic activityi

Agmatine + H2O = putrescine + urea.UniRule annotation

Cofactori

Mn2+UniRule annotation

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi126 – 1261ManganeseUniRule annotation
Metal bindingi149 – 1491ManganeseUniRule annotation
Metal bindingi151 – 1511ManganeseUniRule annotation
Metal bindingi153 – 1531ManganeseUniRule annotation
Metal bindingi230 – 2301ManganeseUniRule annotation
Metal bindingi232 – 2321ManganeseUniRule annotation

GO - Molecular functioni

  1. agmatinase activity Source: UniProtKB-HAMAP
  2. manganese ion binding Source: InterPro

GO - Biological processi

  1. putrescine biosynthetic process from arginine Source: UniProtKB-UniPathway
  2. 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

BioCyciECOL585035:GJWP-3208-MONOMER.
UniPathwayiUPA00534; UER00287.

Names & Taxonomyi

Protein namesi
Recommended name:
AgmatinaseUniRule annotation (EC:3.5.3.11UniRule annotation)
Alternative name(s):
Agmatine ureohydrolaseUniRule annotation
Short name:
AUHUniRule annotation
Gene namesi
Name:speBUniRule annotation
Ordered Locus Names:ECS88_3219
OrganismiEscherichia coli O45:K1 (strain S88 / ExPEC)
Taxonomic identifieri585035 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000747 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 306306AgmatinasePRO_1000145607Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi585035.ECS88_3219.

Structurei

3D structure databases

ProteinModelPortaliB7MMC5.
SMRiB7MMC5. Positions 12-303.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the arginase family. Agmatinase subfamily.UniRule annotation

Phylogenomic databases

eggNOGiCOG0010.
HOGENOMiHOG000204320.
KOiK01480.
OMAiKPDYSLY.
OrthoDBiEOG6R2GW5.

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.

B7MMC5-1 [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 DIIAQVKQIV GDMPVYLTFD IDCLDPAFAP GTGTPVIGGL
260 270 280 290 300
TSDRAIKLVR GLKDLNIVGM DVVEVAPAYD QSEITALAAA TLALEMLYIQ

AAKKGE
Length:306
Mass (Da):33,571
Last modified:February 10, 2009 - v1
Checksum:i5B98B07164854B9F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU928161 Genomic DNA. Translation: CAR04454.1.
RefSeqiYP_002392841.1. NC_011742.1.

Genome annotation databases

EnsemblBacteriaiCAR04454; CAR04454; ECS88_3219.
GeneIDi7129561.
KEGGiecz:ECS88_3219.
PATRICi18414114. VBIEscCol91599_3160.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU928161 Genomic DNA. Translation: CAR04454.1.
RefSeqiYP_002392841.1. NC_011742.1.

3D structure databases

ProteinModelPortaliB7MMC5.
SMRiB7MMC5. Positions 12-303.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi585035.ECS88_3219.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAR04454; CAR04454; ECS88_3219.
GeneIDi7129561.
KEGGiecz:ECS88_3219.
PATRICi18414114. VBIEscCol91599_3160.

Phylogenomic databases

eggNOGiCOG0010.
HOGENOMiHOG000204320.
KOiK01480.
OMAiKPDYSLY.
OrthoDBiEOG6R2GW5.

Enzyme and pathway databases

UniPathwayiUPA00534; UER00287.
BioCyciECOL585035:GJWP-3208-MONOMER.

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]
ProtoNetiSearch...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: S88 / ExPEC.

Entry informationi

Entry nameiSPEB_ECO45
AccessioniPrimary (citable) accession number: B7MMC5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: February 10, 2009
Last modified: January 7, 2015
This is version 45 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

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.