Q5LQM1 (Q5LQM1_SILPO) Unreviewed, UniProtKB/TrEMBL

Names and origin

Protein names

Submitted name:
Agmatinase EMBL AAV95721.1
EC=3.5.3.11 EMBL AAV95721.1

Gene names

Name:	speB-3 EMBL AAV95721.1
Ordered Locus Names:	SPO2467

Organism

Silicibacter pomeroyi (strain ATCC 700808 / DSM 15171 / DSS-3) [Complete proteome] [HAMAP]

Taxonomic identifier

246200 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Rhodobacterales › Rhodobacteraceae › Ruegeria

Protein attributes

Sequence length	327 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Cofactor	Manganese By similarity. RuleBase RU003684
Sequence similarities	Belongs to the arginase family. RuleBase RU003684

Ontologies

Keywords
Ligand	Manganese RuleBase RU003684 Metal-binding RuleBase RU003684 SAAS SAAS005925
Molecular function	Hydrolase SAAS SAAS005925 RuleBase RU003684 EMBL AAV95721.1
Technical term	Complete proteome
Gene Ontology (GO)
Molecular function	agmatinase activity Inferred from electronic annotation. Source: EC metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequences

	Sequence		Length	Mass (Da)
	Q5LQM1 [UniParc]. Last modified February 1, 2005. Version 1. Checksum: 057C52E168249594	FASTA	327	34,635
	10 20 30 40 50 60 MKVALEDAKK QVDEAFTNPE LKGLSFENTF GGATSFLRRL YTKNLTGVDI AVTGVPFDQA 70 80 90 100 110 120 VTNRPGTRLG PRAIREASAL QSPDAPYGWP FDALSELAIV DYGDVAYDYA NIPAFPDTLS 130 140 150 160 170 180 DHIRTILAAD VASVTLGGDH YISFPILKAY AEKYGPMSLL QFDAHTDTWA DDDMSRVDHG 190 200 210 220 230 240 TMFYKAVKSG IVDPARSVQI GIRTTNEDTL GVNIIDAREV HESGPAAVAQ KVRAILGDSP 250 260 270 280 290 300 VYLTFDIDAL DPAFAPGTGT PVWGGLSSAQ AQIILRDIAG INIKGGDVVE VSPPFDPSGA 310 320 TAIAGAHVAT QIICLLGWNK LGGAAAG

References

[1]

"Genome sequence of Silicibacter pomeroyi reveals adaptations to the marine environment." Moran M.A., Buchan A., Gonzalez J.M., Heidelberg J.F., Whitman W.B., Kiene R.P., Henriksen J.R., King G.M., Belas R., Fuqua C., Brinkac L.M., Lewis M., Johri S., Weaver B., Pai G., Eisen J.A., Rahe E., Sheldon W.M. , Ye W., Miller T.R., Carlton J., Rasko D.A., Paulsen I.T., Ren Q., Daugherty S.C., DeBoy R.T., Dodson R.J., Durkin A.S., Madupu R., Nelson W.C., Sullivan S.A., Rosovitz M.J., Haft D.H., Selengut J., Ward N. Nature 432:910-913(2004) [PubMed: 15602564] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 700808 / DSM 15171 / DSS-3.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000031 Genomic DNA. Translation: AAV95721.1.
RefSeq	YP_167684.1. NC_003911.11.
3D structure databases
ProteinModelPortal	Q5LQM1.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	3193270.
GenomeReviews	Gene locus SPO2467 in contig CP000031_GR.
KEGG	sil:SPO2467.
NMPDR	fig|246200.3.peg.2858.
PATRIC	23378331. VBIRuePom114501_2516.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG391953.
OMA	AHNPLTI.
ProtClustDB	PRK02190.
Enzyme and pathway databases
BioCyc	RPOM246200:SPO_2467-MONOMER.
Family and domain databases
InterPro	IPR005925. Agmatinase-rel. IPR006035. Ureohydrolase. IPR023696. Ureohydrolase_domain. IPR020855. Ureohydrolase_Mn_BS. [Graphical view]
Gene3D	G3DSA:3.40.800.10. Ureohydrolase. 1 hit.
KO	K01480.
PANTHER	PTHR11358. Ureohydrolase. 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

Q5LQM1_SILPO

Accession

Primary (citable) accession number: Q5LQM1

Entry history

Integrated into UniProtKB/TrEMBL:	February 1, 2005
Last sequence update:	February 1, 2005
Last modified:	December 14, 2011
This is version 47 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)