Skip Header

 
Contribute Send feedback
Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot P70999 (SPEB_BACSU)

Last modified November 3, 2009. Version 55. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Agmatinase
    EC=3.5.3.11
Alternative name(s):
    Agmatine ureohydrolase
      Short name=AUH
Gene names
Name: speB
Synonyms: ywhG
Ordered Locus Names: BSU37490
OrganismBacillus subtilis [Complete proteome] [HAMAP]
Taxonomic identifier1423 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacillalesBacillaceaeBacillus

Protein attributes

Sequence length290 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Catalyzes the formation of putrescine from agmatine.

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. Ref.3

Sequence similarities

Belongs to the arginase family. Agmatinase subfamily.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 290290Agmatinase
PRO_0000173728

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
P70999-1 [UniParc].

Last modified February 1, 1997. Version 1.
Checksum: B14C4AAD1B1BC964

FASTA29032,417
        10         20         30         40         50         60 
MRFDEAYSGK VFIASRPEWE EADAILYGMP MDWTVSYRPG SRFGPSRIRE VSIGLEEYSP 

        70         80         90        100        110        120 
YLDRDLADLN FFDAGDIPLP FGNPQRSLDM IEEYVDSILE KGKFPMGMGG EHLVSWPVIK 

       130        140        150        160        170        180 
AMYKKYPDLA IIHFDAHTDL RVDYEGEPLS HSTPIRKAAE LIGPHNVYSF GIRSGMKEEF 

       190        200        210        220        230        240 
EWAKENGMHI SKFEVLEPLK EVLPKLAGRP VYVTIDIDVL DPAHAPGTGT VDAGGITSKE 

       250        260        270        280        290 
LLASVHEIAR SEVNVKGADL VEVAPVYDHS EQTANTASKI IREMLLGFVK 

« Hide

References

« Hide 'large scale' references
[1]"The Bacillus subtilis genome from gerBC (311 degrees) to licR (334 degrees)."
Presecan E., Moszer I., Boursier L., Cruz Ramos H., De La Fuente V., Hullo M.-F., Lelong C., Schleich S., Sekowska A., Song B.H., Villani G., Kunst F., Danchin A., Glaser P.
Microbiology 143:3313-3328(1997) [PubMed: 9353933] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 168.
[2]"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V. expand/collapse author list , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.
Nature 390:249-256(1997) [PubMed: 9384377] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 168.
[3]"Characterization of polyamine synthesis pathway in Bacillus subtilis 168."
Sekowska A., Bertin P., Danchin A.
Mol. Microbiol. 29:851-858(1998) [PubMed: 9723923] [Abstract]
Cited for: CHARACTERIZATION OF POLYAMINE PATHWAY.

Cross-references

Sequence databases

Z80360 Genomic DNA. Translation: CAB02517.1.
AL009126 Genomic DNA. Translation: CAB15776.1.
PIRH70057.
RefSeqNP_391629.1.

3D structure databases

HSSPHSSP built from PDB template 1GQ6 based on UniProtKB P37819.
ModBaseSearch...

Genome annotation databases

GeneID937205.
GenomeReviewsGene locus BSU37490 in contig AL009126_GR.
KEGGbsu:BSU37490.
NMPDRfig|224308.1.peg.3755.

Organism-specific databases

SubtiListBG12461. speB. [Micado]
CMRSearch...

Phylogenomic databases

HOGENOMP70999.
OMAMGGEHLV.

Enzyme and pathway databases

BioCycBSUB224308:BSU3746-MON.
MetaCyc:SPEBBACSU-MON.
BRENDA3.5.3.11. 150.

Family and domain databases

InterProIPR005925. Agmatinase.
IPR006035. Ureohydrolase.
[Graphical view]
Gene3DG3DSA:3.40.800.10. Ureohydrolase. 1 hit.
PANTHERPTHR11358. Ureohydrolase. 1 hit.
PfamPF00491. Arginase. 1 hit.
[Graphical view]
TIGRFAMsTIGR01230. agmatinase. 1 hit.
PROSITEPS01053. ARGINASE_1. 1 hit.
PS51409. ARGINASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSPEB_BACSU
AccessionPrimary (citable) accession number: P70999
Entry history
Integrated into UniProtKB/Swiss-Prot: March 15, 2004
Last sequence update: February 1, 1997
Last modified: November 3, 2009
This is version 55 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

Bacillus subtilis

Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents