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Q81JT1 (SPEB_BACAN) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 64. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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:BA_5617, GBAA_5617, BAS5218
OrganismBacillus anthracis
Taxonomic identifier1392 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacillalesBacillaceaeBacillusBacillus cereus group

Protein attributes

Sequence length290 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the formation of putrescine from agmatine By similarity.

Catalytic activity

Agmatine + H2O = putrescine + urea.

Cofactor

Manganese By similarity.

Pathway

Amine and polyamine biosynthesis; putrescine biosynthesis via agmatine pathway; putrescine from agmatine: step 1/1.

Sequence similarities

Belongs to the arginase family. Agmatinase subfamily.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 290290Agmatinase
PRO_0000173725

Sites

Metal binding1121Manganese By similarity
Metal binding1351Manganese By similarity
Metal binding1371Manganese By similarity
Metal binding1391Manganese By similarity
Metal binding2161Manganese By similarity
Metal binding2181Manganese By similarity

Sequences

Sequence LengthMass (Da)Tools
Q81JT1 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: 6F2F39ED33E38DE4

FASTA29032,390
        10         20         30         40         50         60 
MRFDEAYSGK VFIKSHPSFE ESEVVIYGMP MDWTVSYRPG SRFGPARIRE VSIGLEEYSP 

        70         80         90        100        110        120 
YLDRELEEVK YFDAGDIPLP FGNAQRSLDM IEEYVSKLLD AGKFPLGLGG EHLVSWPIFK 

       130        140        150        160        170        180 
AMAKKYPDLA IIHMDAHTDL RESYEGEPLS HSTPIRKVCD LIGPENVYSF GIRSGMKEEF 

       190        200        210        220        230        240 
EWAKEVGMNL YKFDVLEPLK EVLPKLEGRP VYVTIDIDVL DPAHAPGTGT LEAGGITSKE 

       250        260        270        280        290 
LLDSIVAIAN SNINVVGADL VEVAPVYDHS DQTPVAASKF VREMLLGWVK 

« Hide

References

[1]"The genome sequence of Bacillus anthracis Ames and comparison to closely related bacteria."
Read T.D., Peterson S.N., Tourasse N.J., Baillie L.W., Paulsen I.T., Nelson K.E., Tettelin H., Fouts D.E., Eisen J.A., Gill S.R., Holtzapple E.K., Okstad O.A., Helgason E., Rilstone J., Wu M., Kolonay J.F., Beanan M.J., Dodson R.J. expand/collapse author list , Brinkac L.M., Gwinn M.L., DeBoy R.T., Madpu R., Daugherty S.C., Durkin A.S., Haft D.H., Nelson W.C., Peterson J.D., Pop M., Khouri H.M., Radune D., Benton J.L., Mahamoud Y., Jiang L., Hance I.R., Weidman J.F., Berry K.J., Plaut R.D., Wolf A.M., Watkins K.L., Nierman W.C., Hazen A., Cline R.T., Redmond C., Thwaite J.E., White O., Salzberg S.L., Thomason B., Friedlander A.M., Koehler T.M., Hanna P.C., Kolstoe A.-B., Fraser C.M.
Nature 423:81-86(2003) [PubMed: 12721629] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Ames / isolate Porton.
[2]"Bacillus anthracis comparative genomics."
Ravel J., Rasko D.A., Shumway M.F., Jiang L., Cer R.Z., Federova N.B., Wilson M., Stanley S., Decker S., Read T.D., Salzberg S.L., Fraser C.M.
Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Ames ancestor.
[3]"Complete genome sequence of Bacillus anthracis Sterne."
Brettin T.S., Bruce D., Challacombe J.F., Gilna P., Han C., Hill K., Hitchcock P., Jackson P., Keim P., Longmire J., Lucas S., Okinaka R., Richardson P., Rubin E., Tice H.
Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Sterne.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE016879 Genomic DNA. Translation: AAP29255.1.
AE017334 Genomic DNA. Translation: AAT34764.1.
AE017225 Genomic DNA. Translation: AAT57507.1.
RefSeqNP_847769.1. NC_003997.3.
YP_022289.1. NC_007530.2.
YP_031457.1. NC_005945.1.

3D structure databases

ProteinModelPortalQ81JT1.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBBACT00000008654; EBBACP00000008410; EBBACG00000008646.
EBBACT00000014000; EBBACP00000013621; EBBACG00000013992.
EBBACT00000020632; EBBACP00000020117; EBBACG00000020623.
GeneID1085325.
2817842.
2848265.
GenomeReviewsGene locus BA_5617 in contig AE016879_GR.
Gene locus BAS5218 in contig AE017225_GR.
Gene locus GBAA_5617 in contig AE017334_GR.
KEGGban:BA_5617.
bar:GBAA_5617.
bat:BAS5218.
TIGRBA_5617.
GBAA_5617.

Phylogenomic databases

GeneTreeEBGT00050000001627.
HOGENOMHBG391953.
OMAREMLLGF.
ProtClustDBCLSK888062.

Enzyme and pathway databases

BioCycBANT260799:BAS5218-MONOMER.
BANT261594:GBAA5617-MONOMER.

Family and domain databases

InterProIPR005925. Agmatinase-rel.
IPR006035. Ureohydrolase.
IPR023696. Ureohydrolase_domain.
IPR020855. Ureohydrolase_Mn_BS.
[Graphical view]
Gene3DG3DSA:3.40.800.10. Ureohydrolase. 1 hit.
KOK01480.
PANTHERPTHR11358. Ureohydrolase. 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...

Entry information

Entry nameSPEB_BACAN
AccessionPrimary (citable) accession number: Q81JT1
Secondary accession number(s): Q6HQD1, Q6KJQ8
Entry history
Integrated into UniProtKB/Swiss-Prot: March 15, 2004
Last sequence update: June 1, 2003
Last modified: November 16, 2011
This is version 64 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families