Reviewed, UniProtKB/Swiss-Prot Q7P0S6 (SPEB_CHRVO)

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:	CV_0490

Organism

Chromobacterium violaceum [Complete proteome] [HAMAP]

Taxonomic identifier

536 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Betaproteobacteria › Neisseriales › Neisseriaceae › Chromobacterium

Protein attributes

Sequence length	322 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

General annotation (Comments)

Function	Catalyzes the formation of putrescine from agmatine By similarity.
Catalytic activity	Agmatine + H2O = putrescine + urea. HAMAP MF_01418
Cofactor	Manganese By similarity.
Pathway	Amine and polyamine biosynthesis; putrescine biosynthesis via agmatine pathway; putrescine from agmatine: step 1/1. HAMAP MF_01418
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
Gene Ontology (GO)
Biological process	putrescine biosynthetic process Inferred from electronic annotation. Source: HAMAP spermidine biosynthetic process Inferred from electronic annotation. Source: HAMAP
Molecular function	agmatinase activity Inferred from electronic annotation. Source: HAMAP manganese 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 – 322	322	Agmatinase HAMAP MF_01418		PRO_0000173730
Sites
	Metal binding	136	1	Manganese By similarity
	Metal binding	160	1	Manganese By similarity
	Metal binding	162	1	Manganese By similarity
	Metal binding	164	1	Manganese By similarity
	Metal binding	243	1	Manganese By similarity
	Metal binding	245	1	Manganese By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q7P0S6-1 [UniParc]. Last modified December 15, 2003. Version 1. Checksum: EC6BE7759F34D694	FASTA	322	34,861
	10 20 30 40 50 60 MSDEMIYGDG AIRRQGLYGS SIENTYAGVL SFMRRNYSRD LEGVDVAVSG IPLDLSVTFR 70 80 90 100 110 120 SGARMGPQAI RAASVQLAEL KPYPWGFDPF EDLAVVDYGD CWFDAHNPLT IKPSIIEHAR 130 140 150 160 170 180 TILASGAKML TFGGDHYVTY PLLIAHAEKY GKPLALLHFD AHCDTWPDDS PDSLNHGTMF 190 200 210 220 230 240 YKAVKEGLID PKKSVQVGIR TWNDDFMGLN VLGAPWVHDN GVDATIAEIK KTIGDAPVYV 250 260 270 280 290 300 TFDIDCLDPS AAPGTGTPVP GGLTTAQALK IIRNLGDLNI VGMDVVEVAP SYDQSEITAI 310 320 AAAHIACDML CLMRNKKVAG TL

References

[1]

"The complete genome sequence of Chromobacterium violaceum reveals remarkable and exploitable bacterial adaptability." Vasconcelos A.T.R., de Almeida D.F., Hungria M., Guimaraes C.T., Antonio R.V., Almeida F.C., de Almeida L.G.P., de Almeida R., Alves-Gomes J.A., Andrade E.M., Araripe J., de Araujo M.F.F., Astolfi-Filho S., Azevedo V., Baptista A.J., Bataus L.A.M., Batista J.S., Belo A. , van den Berg C., Bogo M., Bonatto S., Bordignon J., Brigido M.M., Brito C.A., Brocchi M., Burity H.A., Camargo A.A., Cardoso D.D.P., Carneiro N.P., Carraro D.M., Carvalho C.M.B., Cascardo J.C.M., Cavada B.S., Chueire L.M.O., Creczynski-Pasa T.B., Cunha-Junior N.C., Fagundes N., Falcao C.L., Fantinatti F., Farias I.P., Felipe M.S.S., Ferrari L.P., Ferro J.A., Ferro M.I.T., Franco G.R., Freitas N.S.A., Furlan L.R., Gazzinelli R.T., Gomes E.A., Goncalves P.R., Grangeiro T.B., Grattapaglia D., Grisard E.C., Hanna E.S., Jardim S.N., Laurino J., Leoi L.C.T., Lima L.F.A., Loureiro M.F., Lyra M.C.C.P., Madeira H.M.F., Manfio G.P., Maranhao A.Q., Martins W.S., di Mauro S.M.Z., de Medeiros S.R.B., Meissner R.V., Moreira M.A.M., Nascimento F.F., Nicolas M.F., Oliveira J.G., Oliveira S.C., Paixao R.F.C., Parente J.A., Pedrosa F.O., Pena S.D.J., Pereira J.O., Pereira M., Pinto L.S.R.C., Pinto L.S., Porto J.I.R., Potrich D.P., Ramalho-Neto C.E., Reis A.M.M., Rigo L.U., Rondinelli E., Santos E.B.P., Santos F.R., Schneider M.P.C., Seuanez H.N., Silva A.M.R., da Silva A.L.C., Silva D.W., Silva R., Simoes I.C., Simon D., Soares C.M.A., Soares R.B.A., Souza E.M., Souza K.R.L., Souza R.C., Steffens M.B.R., Steindel M., Teixeira S.R., Urmenyi T., Vettore A., Wassem R., Zaha A., Simpson A.J.G. Proc. Natl. Acad. Sci. U.S.A. 100:11660-11665(2003) [PubMed: 14500782] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 12472 / DSM 30191 / IFO 12614 / JCM 1249 / NCIB 9131.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AE016825 Genomic DNA. Translation: AAQ58167.1.
RefSeq	NP_900160.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	2550160.
GenomeReviews	Gene locus CV_0490 in contig AE016825_GR.
KEGG	cvi:CV_0490.
NMPDR	fig|243365.1.peg.490.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q7P0S6.
OMA	TWNDDFM.
Enzyme and pathway databases
BioCyc	CVIO243365:CV_0490-MON.
BRENDA	3.5.3.11. 415.
Family and domain databases
HAMAP	MF_01418. [Tree]
InterPro	IPR005925. Agmatinase. IPR006035. Ureohydrolase. [Graphical view]
Gene3D	G3DSA:3.40.800.10. Ureohydrolase. 1 hit.
PANTHER	PTHR11358. Ureohydrolase. 1 hit.
Pfam	PF00491. Arginase. 1 hit. [Graphical view]
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_CHRVO

Accession

Primary (citable) accession number: Q7P0S6

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 29, 2004
Last sequence update:	December 15, 2003
Last modified:	November 3, 2009
This is version 42 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)