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P70999 (SPEB_BACSU) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 84. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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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
Synonyms:ywhG
Ordered Locus Names:BSU37490
OrganismBacillus subtilis (strain 168) [Reference proteome] [HAMAP]
Taxonomic identifier224308 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacilli › Bacillales › Bacillaceae › Bacillus ›

Protein attributes

Sequence length290 AA.
Sequence statusComplete.
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 [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION OF POLYAMINE PATHWAY.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		Z80360 Genomic DNA. Translation: CAB02517.1.
AL009126 Genomic DNA. Translation: CAB15776.1.
PIRH70057.
RefSeqNP_391629.1. NC_000964.3.

3D structure databases

ProteinModelPortalP70999.
SMRP70999. Positions 18-290.
ModBaseSearch...

Protein-protein interaction databases

STRING224308.BSU37490.

Proteomic databases

PaxDbP70999.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAB15776; CAB15776; BSU37490.
GeneID937205.
KEGGbsu:BSU37490.
PATRIC18979534. VBIBacSub10457_3929.

Organism-specific databases

GenoListBSU37490. [Micado]

Phylogenomic databases

eggNOGCOG0010.
HOGENOMHOG000204321.
KOK01480.
OMAAKENGMH.
ProtClustDBCLSK888062.

Enzyme and pathway databases

BioCycBSUB:BSU37490-MONOMER.
MetaCyc:SPEBBACSU-MONOMER.
UniPathwayUPA00534; UER00287.

Family and domain databases

Gene3D3.40.800.10. 1 hit.
InterProIPR005925. Agmatinase-rel.
IPR006035. Ureohydrolase.
IPR023696. Ureohydrolase_domain.
IPR020855. Ureohydrolase_Mn_BS.
[Graphical view]
PANTHERPTHR11358. PTHR11358. 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_BACSU
AccessionPrimary (citable) accession number: P70999
Entry history
Integrated into UniProtKB/Swiss-Prot: March 15, 2004
Last sequence update: February 1, 1997
Last modified: May 1, 2013
This is version 84 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

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

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents