Reviewed, UniProtKB/Swiss-Prot P37818 (ARGI1_SCHPO)

Names and origin

Protein names

Recommended name:
    Arginase
    EC=3.5.3.1

Gene names

Name:	car1
ORF Names:	SPBP26C9.02c

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	323 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at transcript level.

General annotation (Comments)

Catalytic activity	L-arginine + H2O = L-ornithine + urea.
Cofactor	Binds 2 manganese ions per subunit By similarity.
Pathway	Nitrogen metabolism; urea cycle; L-ornithine and urea from L-arginine: step 1/1.
Subunit structure	Homotrimer By similarity.
Sequence similarities	Belongs to the arginase family.

Ontologies

Keywords
Biological process	Arginine metabolism Urea cycle
Ligand	Manganese Metal-binding
Molecular function	Hydrolase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	arginine catabolic process to ornithine Ref.1 Inferred from genetic interaction. Source: GeneDB_SPombe urea cycle Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytosol Inferred from direct assay. Source: GeneDB_SPombe nucleus Inferred from direct assay. Source: GeneDB_SPombe
Molecular function	arginase activity Inferred from genetic interaction. Source: GeneDB_SPombe 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 – 323	323	Arginase		PRO_0000173709
Regions
	Region	144 – 148	5	Substrate binding By similarity
	Region	155 – 157	3	Substrate binding By similarity
Sites
	Metal binding	119	1	Manganese 1 By similarity
	Metal binding	142	1	Manganese 1 By similarity
	Metal binding	142	1	Manganese 2 By similarity
	Metal binding	144	1	Manganese 2 By similarity
	Metal binding	146	1	Manganese 1 By similarity
	Metal binding	247	1	Manganese 1 By similarity
	Metal binding	247	1	Manganese 2 By similarity
	Metal binding	249	1	Manganese 2 By similarity
	Binding site	198	1	Substrate By similarity
	Binding site	292	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	P37818-1 [UniParc]. Last modified October 1, 1994. Version 1. Checksum: 874D8861319F2190	FASTA	323	35,721
	10 20 30 40 50 60 MSPHKIPEVH RHIMSSRYME GNAVSIINMP FSGGQPKDGA ELAPEMIEAA GLPEDLERLG 70 80 90 100 110 120 YSVNVVQNPK FKSRPLKEGP NQALMKNPLY VSNVTRQVRN IVQQELEKQR IAVNIGGDHS 130 140 150 160 170 180 LAIGTVEGVQ AVYDDACVLW IDAHADINTP DSSPSKNLHG CPLSFSLGYA EPLPEEFAWT 190 200 210 220 230 240 RRVIEERRLA FIGLRDLDPM ERAFLRERSI TAYTMHDVDK YGIARVVEMA LEHINPGRRR 250 260 270 280 290 300 PIHLSFDVDA CDPIVAPATG TRVPGGLTFR EAMYICESVA ETGSLVAVDV MEVNPLLGNK 310 320 EEAKTTVDLA RSIVRTCLGQ TLL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning and sequencing of Schizosaccharomyces pombe car1 gene encoding arginase. Expression of the arginine anabolic and catabolic genes in response to arginine and related metabolites." van Huffel C.H., Dubois E., Messenguy F. Yeast 10:923-933(1994) [PubMed: 7985419] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 38366 / 972.
[2]	van Huffel C.H. Thesis (1993), Universite Libre de Bruxelles, Belgium Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 38366 / 972.
[3]	"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
EMBLGenBankDDBJ	X75559 Genomic DNA. Translation: CAA53236.1. CU329671 Genomic DNA. Translation: CAC08237.1.
PIR	S45455.
RefSeq	NP_595133.1.
3D structure databases
HSSP	HSSP built from PDB template 1PQ3 based on UniProtKB P78540.
ModBase	Search...
Protein-protein interaction databases
STRING	P37818.
Genome annotation databases
GeneID	2541313.
GenomeReviews	Gene locus car1 in contig CU329671_GR.
KEGG	spo:SPBP26C9.02c.
NMPDR	fig|4896.1.peg.999.
Organism-specific databases
GeneDB_Spombe	SPBP26C9.02c.
Phylogenomic databases
OMA	HVDRYGI.
Enzyme and pathway databases
BioCyc	SPOM-XXX-01:SPOM-XXX-01-003231-MON.
BRENDA	3.5.3.1. 653.
Gene expression databases
ArrayExpress	P37818.
Family and domain databases
InterPro	IPR005924. Arginase. IPR014033. Arginase_sub. IPR006035. Ureohydrolase. [Graphical view]
Gene3D	G3DSA:3.40.800.10. Ureohydrolase. 1 hit.
PANTHER	PTHR11358:SF2. Arginase_sub. 1 hit. PTHR11358. Ureohydrolase. 1 hit.
Pfam	PF00491. Arginase. 1 hit. [Graphical view]
PRINTS	PR00116. ARGINASE.
TIGRFAMs	TIGR01229. rocF_arginase. 1 hit.
PROSITE	PS01053. ARGINASE_1. 1 hit. PS51409. ARGINASE_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ARGI1_SCHPO

Accession

Primary (citable) accession number: P37818

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1994
Last sequence update:	October 1, 1994
Last modified:	November 3, 2009
This is version 74 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)