Reviewed, UniProtKB/Swiss-Prot Q9C0Y9 (SPEB3_SCHPO)

Names and origin

Protein names

Recommended name:
    Putative agmatinase 3
    EC=3.5.3.11
Alternative name(s):
    Agmatine ureohydrolase 3
      Short name=AUH 3

Gene names

ORF Names:

SPAPB24D3.03

Organism

Schizosaccharomyces pombe (Fission yeast) [Complete proteome]

Taxonomic identifier

4896 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces

Protein attributes

Sequence length	385 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level.

General annotation (Comments)

Catalytic activity	Agmatine + H2O = putrescine + urea.
Cofactor	Manganese By similarity.
Sequence similarities	Belongs to the arginase family.

Ontologies

Keywords
Ligand	Manganese Metal-binding
Molecular function	Hydrolase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	urea metabolic process Inferred by curator. Source: GeneDB_SPombe
Molecular function	agmatinase activity Inferred from electronic annotation. Source: EC 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 – 385	385	Putative agmatinase 3		PRO_0000311760
Sites
	Metal binding	175	1	Manganese 1 By similarity
	Metal binding	199	1	Manganese 1 By similarity
	Metal binding	199	1	Manganese 2 By similarity
	Metal binding	201	1	Manganese 2 By similarity
	Metal binding	203	1	Manganese 1 By similarity
	Metal binding	296	1	Manganese 1 By similarity
	Metal binding	296	1	Manganese 2 By similarity
	Metal binding	298	1	Manganese 2 By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9C0Y9-1 [UniParc]. Last modified June 1, 2001. Version 1. Checksum: 0326AD45036B859E	FASTA	385	42,485
	10 20 30 40 50 60 MGLGFQEKNP VFVKEKQSPF YAVPSNYEEV EFSSIVEPMY SGIATFGRLE NVECLSKRSE 70 80 90 100 110 120 DFDIAFIGMP FDTGTSYRPG ARFGPSSLRE GSRRINTKYG AVNVPLEINP FKSWAKLVDC 130 140 150 160 170 180 GDIPVTTYDI LKAMDQLESA YFQLIARKPS SFTDHDGFAK NDTVLPRVLS LGGDHTIVLP 190 200 210 220 230 240 ILRALHRVYG QPISVIHFDS HLDTWAPGLI GDGDEADGIN HGSYFYFASQ EGIMSKDANI 250 260 270 280 290 300 HAGIRTPISS FSDYDDDVDC GFKIIEAREI DDLGIDGIVK KIRDRVGDNL VYLSIDIDVL 310 320 330 340 350 360 DPAFAPATGT PETGGWSSRE MRAILRGLQG LKFVGADLVE VAPAYDVAEI TSLAGAQLLF 370 380 DIVSMMVKYP LVKEADLSRY MPIHK

References

[1]

"The genome sequence of Schizosaccharomyces pombe." Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M. , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P. Nature 415:871-880(2002) [PubMed: 11859360] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 38366 / 972.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CU329670 Genomic DNA. Translation: CAC36899.1.
RefSeq	NP_593990.1.
3D structure databases
HSSP	HSSP built from PDB template 1GQ6 based on UniProtKB P37819.
SMR	Q9C0Y9. Positions 37-368.
ModBase	Search...
Protein-protein interaction databases
STRING	Q9C0Y9.
Genome annotation databases
GeneID	2543569.
KEGG	spo:SPAPB24D3.03.
NMPDR	fig|4896.1.peg.3960.
Organism-specific databases
GeneDB_Spombe	SPAPB24D3.03.
Phylogenomic databases
eggNOG	fuNOG06303.
HOGENOM	HBG391953.
OMA	DAAMAND.
OrthoDB	EOG93V1BX.
PhylomeDB	Q9C0Y9.
Enzyme and pathway databases
BRENDA	3.5.3.11. 653.
Gene expression databases
ArrayExpress	Q9C0Y9.
Family and domain databases
InterPro	IPR005924. Arginase. IPR006035. Ureohydrolase. IPR020855. Ureohydrolase_Mn_BS. [Graphical view]
Gene3D	G3DSA:3.40.800.10. Ureohydrolase. 1 hit.
PANTHER	PTHR11358. Ureohydrolase. 1 hit.
Pfam	PF00491. Arginase. 1 hit. [Graphical view]
PRINTS	PR00116. ARGINASE.
PROSITE	PS01053. ARGINASE_1. 1 hit. PS51409. ARGINASE_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

SPEB3_SCHPO

Accession

Primary (citable) accession number: Q9C0Y9

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 13, 2007
Last sequence update:	June 1, 2001
Last modified:	January 19, 2010
This is version 56 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)