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Q814Q2

- SPEB_BACCR

UniProt

Q814Q2 - SPEB_BACCR

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Protein

Agmatinase

Gene

speB

Organism
Bacillus cereus (strain ATCC 14579 / DSM 31)
Status
Reviewed - Annotation score: 2 out of 5- Protein inferred from homologyi

Functioni

Catalyzes the formation of putrescine from agmatine.By similarity

Catalytic activityi

Agmatine + H2O = putrescine + urea.

Cofactori

Manganese.PROSITE-ProRule annotation

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi112 – 1121ManganesePROSITE-ProRule annotation
Metal bindingi135 – 1351ManganesePROSITE-ProRule annotation
Metal bindingi137 – 1371ManganesePROSITE-ProRule annotation
Metal bindingi139 – 1391ManganesePROSITE-ProRule annotation
Metal bindingi216 – 2161ManganesePROSITE-ProRule annotation
Metal bindingi218 – 2181ManganesePROSITE-ProRule annotation

GO - Molecular functioni

  1. agmatinase activity Source: UniProtKB-EC
  2. metal ion binding Source: UniProtKB-KW

GO - Biological processi

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

BioCyciBCER226900:GJEU-5362-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:BC_5370
OrganismiBacillus cereus (strain ATCC 14579 / DSM 31)
Taxonomic identifieri226900 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillusBacillus cereus group
ProteomesiUP000001417: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 290290AgmatinasePRO_0000173726Add
BLAST

Proteomic databases

PRIDEiQ814Q2.

Interactioni

Protein-protein interaction databases

STRINGi226900.BC5370.

Structurei

3D structure databases

ProteinModelPortaliQ814Q2.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the arginase family. Agmatinase subfamily.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0010.
KOiK01480.
OMAiSPPYDPF.
OrthoDBiEOG6R2GW5.

Family and domain databases

Gene3Di3.40.800.10. 1 hit.
InterProiIPR005925. 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.

Q814Q2-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MRFDEAYSGK VFIKSHPSFE ESKVVIYGMP MDWTVSYRPG SRFGPARIRE
60 70 80 90 100
VSIGLEEYSP YLDRELEEVK YFDAGDIPLP FGNAQRSLDM IEEYVSKLLD
110 120 130 140 150
ADKFPLGLGG EHLVSWPIFK AMAKKYPDLA IIHMDAHTDL RESYEGEPLS
160 170 180 190 200
HSTPIRKVCD LIGPENVYSF GIRSGMKEEF EWAKEVGMNL YKFDVLEPLK
210 220 230 240 250
EVLPKLAGRP VYVTIDIDVL DPAHAPGTGT LEAGGITSKE LLDSIVAIAN
260 270 280 290
SNINVVGADL VEVAPVYDHS DQTPVAASKF VREMLLGWVK
Length:290
Mass (Da):32,389
Last modified:June 1, 2003 - v1
Checksum:iD538E9EBDE734B5B
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE016877 Genomic DNA. Translation: AAP12232.1.
RefSeqiNP_835031.1. NC_004722.1.

Genome annotation databases

EnsemblBacteriaiAAP12232; AAP12232; BC_5370.
GeneIDi1207710.
KEGGibce:BC5370.
PATRICi32606948. VBIBacCer54481_5545.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE016877 Genomic DNA. Translation: AAP12232.1 .
RefSeqi NP_835031.1. NC_004722.1.

3D structure databases

ProteinModelPortali Q814Q2.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 226900.BC5370.

Proteomic databases

PRIDEi Q814Q2.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAP12232 ; AAP12232 ; BC_5370 .
GeneIDi 1207710.
KEGGi bce:BC5370.
PATRICi 32606948. VBIBacCer54481_5545.

Phylogenomic databases

eggNOGi COG0010.
KOi K01480.
OMAi SPPYDPF.
OrthoDBi EOG6R2GW5.

Enzyme and pathway databases

UniPathwayi UPA00534 ; UER00287 .
BioCyci BCER226900:GJEU-5362-MONOMER.

Family and domain databases

Gene3Di 3.40.800.10. 1 hit.
InterProi 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

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 14579 / DSM 31.

Entry informationi

Entry nameiSPEB_BACCR
AccessioniPrimary (citable) accession number: Q814Q2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 15, 2004
Last sequence update: June 1, 2003
Last modified: October 1, 2014
This is version 75 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. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3