Q81JT1 (SPEB_BACAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Bacillus anthracis [Reference proteome] [HAMAP]

Taxonomic identifier

1392 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Firmicutes › Bacilli › Bacillales › Bacillaceae › Bacillus › Bacillus cereus group

Protein attributes

Sequence length	290 AA.
Sequence status	Complete.
Protein existence	Inferred 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.

Ontologies

Keywords
Biological process	Polyamine biosynthesis Putrescine biosynthesis Spermidine biosynthesis
Ligand	Manganese Metal-binding
Molecular function	Hydrolase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	putrescine biosynthetic process from arginine Inferred from electronic annotation. Source: UniProtKB-UniPathway spermidine biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	agmatinase activity Inferred from electronic annotation. Source: EC metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 290	290	Agmatinase		PRO_0000173725
Sites
	Metal binding	112	1	Manganese By similarity
	Metal binding	135	1	Manganese By similarity
	Metal binding	137	1	Manganese By similarity
	Metal binding	139	1	Manganese By similarity
	Metal binding	216	1	Manganese By similarity
	Metal binding	218	1	Manganese By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q81JT1 [UniParc]. Last modified June 1, 2003. Version 1. Checksum: 6F2F39ED33E38DE4	FASTA	290	32,390
	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

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. , 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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Ames / isolate Porton.
[2]	"The complete genome sequence of Bacillus anthracis Ames 'Ancestor'." Ravel J., Jiang L., Stanley S.T., Wilson M.R., Decker R.S., Read T.D., Worsham P., Keim P.S., Salzberg S.L., Fraser-Liggett C.M., Rasko D.A. J. Bacteriol. 191:445-446(2009) [PubMed] [Europe PMC] [Abstract] 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.

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.
RefSeq	NP_847769.1. NC_003997.3. YP_022289.1. NC_007530.2. YP_031457.1. NC_005945.1.
3D structure databases
ProteinModelPortal	Q81JT1.
ModBase	Search...
Protein-protein interaction databases
STRING	198094.BA_5617.
Protocols and materials databases
DNASU	1085325.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAP29255; AAP29255; BA_5617. AAT34764; AAT34764; GBAA_5617. AAT57507; AAT57507; BAS5218.
GeneID	1085325. 2817842. 2848265.
KEGG	ban:BA_5617. bar:GBAA_5617. bat:BAS5218.
Phylogenomic databases
eggNOG	COG0010.
HOGENOM	HOG000204321.
KO	K01480.
OMA	AKENGMH.
ProtClustDB	CLSK888062.
Enzyme and pathway databases
BioCyc	BANT260799:GJAJ-5293-MONOMER. BANT261594:GJ7F-5474-MONOMER.
UniPathway	UPA00534; UER00287.
Family and domain databases
Gene3D	3.40.800.10. 1 hit.
InterPro	IPR005925. Agmatinase-rel. IPR006035. Ureohydrolase. IPR023696. Ureohydrolase_domain. IPR020855. Ureohydrolase_Mn_BS. [Graphical view]
PANTHER	PTHR11358. PTHR11358. 1 hit.
Pfam	PF00491. Arginase. 1 hit. [Graphical view]
PIRSF	PIRSF036979. Arginase. 1 hit.
TIGRFAMs	TIGR01230. agmatinase. 1 hit.
PROSITE	PS01053. ARGINASE_1. 1 hit. PS51409. ARGINASE_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

SPEB_BACAN

Accession

Primary (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:	May 1, 2013
This is version 76 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program