Skip Header

Contribute Send feedback
Read comments (?) or add your own

P00812 (ARGI_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 117. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Arginase

EC=3.5.3.1
Gene names
Name:CAR1
Ordered Locus Names:YPL111W
ORF Names:LPH15W
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length333 AA.
Sequence statusComplete.
Protein existenceEvidence at protein 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.

Induction

By arginine or homoarginine.

Miscellaneous

Present with 42800 molecules/cell in log phase SD medium. Ref.6

Sequence similarities

Belongs to the arginase family.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

ARG3P051504EBI-2856,EBI-12712

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 333333Arginase
PRO_0000173711

Regions

Region148 – 1525Substrate binding By similarity
Region159 – 1613Substrate binding By similarity

Sites

Metal binding1231Manganese 1 By similarity
Metal binding1461Manganese 1 By similarity
Metal binding1461Manganese 2 By similarity
Metal binding1481Manganese 2 By similarity
Metal binding1501Manganese 1 By similarity
Metal binding2561Manganese 1 By similarity
Metal binding2561Manganese 2 By similarity
Metal binding2581Manganese 2 By similarity
Binding site2051Substrate By similarity
Binding site3011Substrate By similarity

Amino acid modifications

Modified residue761Phosphothreonine Ref.7
Modified residue771Phosphothreonine Ref.7
Modified residue801Phosphoserine Ref.7
Modified residue2701Phosphothreonine Ref.7

Sequences

Sequence LengthMass (Da)Tools
P00812 [UniParc].

Last modified July 21, 1986. Version 1.
Checksum: A5979DC9F1FDFF2E

FASTA33335,662
        10         20         30         40         50         60 
METGPHYNYY KNRELSIVLA PFSGGQGKLG VEKGPKYMLK HGLQTSIEDL GWSTELEPSM 

        70         80         90        100        110        120 
DEAQFVGKLK MEKDSTTGGS SVMIDGVKAK RADLVGEATK LVYNSVSKVV QANRFPLTLG 

       130        140        150        160        170        180 
GDHSIAIGTV SAVLDKYPDA GLLWIDAHAD INTIESTPSG NLHGCPVSFL MGLNKDVPHC 

       190        200        210        220        230        240 
PESLKWVPGN LSPKKIAYIG LRDVDAGEKK ILKDLGIAAF SMYHVDKYGI NAVIEMAMKA 

       250        260        270        280        290        300 
VHPETNGEGP IMCSYDVDGV DPLYIPATGT PVRGGLTLRE GLFLVERLAE SGNLIALDVV 

       310        320        330 
ECNPDLAIHD IHVSNTISAG CAIARCALGE TLL 

« Hide

References

« Hide 'large scale' references
[1]"Nucleotide sequence of the Saccharomyces cerevisiae arginase gene (CAR1) and its transcription under various physiological conditions."
Sumrada R.A., Cooper T.G.
J. Bacteriol. 160:1078-1087(1984) [PubMed: 6094498] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI."
Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W., Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D., Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E., Churcher C.M. expand/collapse author list , Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H., DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N., Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K., Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M., Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A., Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S., Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D., Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S., Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B., Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A., Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R., Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A., Vo D.H., Hani J.
Nature 387:103-105(1997) [PubMed: 9169875] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204511 / S288c / AB972.
[3]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[4]"Point mutation generates constitutive expression of an inducible eukaryotic gene."
Sumrada R.A., Cooper T.G.
Proc. Natl. Acad. Sci. U.S.A. 82:643-647(1985) [PubMed: 2983306] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-11.
[5]"Roles of metal ions in the maintenance of the tertiary and quaternary structure of arginase from Saccharomyces cerevisiae."
Green S.M., Ginsburg A., Lewis M.S., Hensley P.
J. Biol. Chem. 266:21474-21481(1991) [PubMed: 1939179] [Abstract]
Cited for: METAL-BINDING.
[6]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed: 14562106] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[7]"A multidimensional chromatography technology for in-depth phosphoproteome analysis."
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed: 18407956] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-76; THR-77; SER-80 AND THR-270, MASS SPECTROMETRY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M10414 Genomic DNA. Translation: AAA34470.1.
U43503 Genomic DNA. Translation: AAB68250.1.
M10110 Genomic DNA. Translation: AAA34469.1.
BK006949 Genomic DNA. Translation: DAA11322.1.
PIRWZBYR. A01008.
RefSeqNP_015214.1. NM_001183925.1.

3D structure databases

ProteinModelPortalP00812.
SMRP00812. Positions 12-330.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-1224N.
IntActP00812. 18 interactions.
MINTMINT-409717.
STRINGP00812.

2D gel databases

UCD-2DPAGEP00812.

Proteomic databases

PeptideAtlasP00812.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYPL111W; YPL111W; YPL111W.
GeneID855993.
KEGGsce:YPL111W.
NMPDRfig|4932.3.peg.6346.

Organism-specific databases

CYGDYPL111w.
SGDS000006032. CAR1.

Phylogenomic databases

eggNOGfuNOG04820.
GeneTreeEFGT00050000003865.
HOGENOMHBG391953.
OMAKYGIGKV.
OrthoDBEOG432471.

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-11546.

Gene expression databases

ArrayExpressP00812.
GenevestigatorP00812.
GermOnlineYPL111W. Saccharomyces cerevisiae.

Family and domain databases

InterProIPR014033. Arginase_subgr.
IPR006035. Ureohydrolase.
IPR023696. Ureohydrolase_domain.
IPR020855. Ureohydrolase_Mn_BS.
[Graphical view]
Gene3DG3DSA:3.40.800.10. Ureohydrolase. 1 hit.
KOK01476.
PANTHERPTHR11358:SF2. Arginase_sub. 1 hit.
PTHR11358. Ureohydrolase. 1 hit.
PfamPF00491. Arginase. 1 hit.
[Graphical view]
PIRSFPIRSF036979. Arginase. 1 hit.
PRINTSPR00116. ARGINASE.
TIGRFAMsTIGR01229. RocF_arginase. 1 hit.
PROSITEPS01053. ARGINASE_1. 1 hit.
PS51409. ARGINASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio980848.

Entry information

Entry nameARGI_YEAST
AccessionPrimary (citable) accession number: P00812
Secondary accession number(s): D6W3Q6
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: December 14, 2011
This is version 117 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families