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P22768 (ASSY_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 125. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Argininosuccinate synthase

EC=6.3.4.5
Alternative name(s):
Citrulline--aspartate ligase
Gene names
Name:ARG1
Ordered Locus Names:YOL058W
ORF Names:O1228
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length420 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the eighth step in arginine biosynthesis. Also has a catabolic function as the first enzyme of citrulline utilization as nitrogen source via arginine and the reactions involved in the arginase pathway. Ref.7

Catalytic activity

ATP + L-citrulline + L-aspartate = AMP + diphosphate + N(omega)-(L-arginino)succinate. HAMAP-Rule MF_00005

Pathway

Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine from L-ornithine and carbamoyl phosphate: step 2/3. HAMAP-Rule MF_00005

Subunit structure

Homotetramer. Ref.7

Subcellular location

Cytoplasm Ref.6 Ref.8.

Miscellaneous

Present with 1870 molecules/cell in log phase SD medium.

Sequence similarities

Belongs to the argininosuccinate synthase family. Type 1 subfamily.

Biophysicochemical properties

Kinetic parameters:

KM=0.1 mM for L-citrulline Ref.7

KM=0.03 mM for L-aspartate

KM=0.3 mM for ATP

pH dependence:

Optimum pH is 7.5-8.0 for the forward reaction and 6.0-6.5 for the reverse reaction.

Ontologies

Keywords
   Biological processAmino-acid biosynthesis
Arginine biosynthesis
   Cellular componentCytoplasm
   LigandATP-binding
Nucleotide-binding
   Molecular functionLigase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processarginine biosynthetic process

Inferred from mutant phenotype Ref.5. Source: SGD

   Cellular_componentcytosol

Inferred from direct assay Ref.6. Source: SGD

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

argininosuccinate synthase activity

Inferred from direct assay Ref.5. Source: SGD

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 420420Argininosuccinate synthase HAMAP-Rule MF_00005
PRO_0000148559

Regions

Nucleotide binding9 – 179ATP By similarity
Nucleotide binding114 – 1229ATP By similarity

Sites

Binding site351ATP; via amide nitrogen and carbonyl oxygen By similarity
Binding site861Citrulline By similarity
Binding site911Citrulline By similarity
Binding site1181Aspartate By similarity
Binding site1221Aspartate By similarity
Binding site1221Citrulline By similarity
Binding site1231Aspartate By similarity
Binding site1261Citrulline By similarity
Binding site1791Citrulline By similarity
Binding site1881Citrulline By similarity
Binding site2731Citrulline By similarity
Binding site2851Citrulline By similarity

Experimental info

Sequence conflict27 – 282GY → AT in AAA34437. Ref.1
Sequence conflict27 – 282GY → AT in CAA30106. Ref.5
Sequence conflict48 – 492EK → VL in AAA34437. Ref.1
Sequence conflict48 – 492EK → VL in CAA30106. Ref.5
Sequence conflict61 – 644VDCR → GGLS in AAA34437. Ref.1
Sequence conflict1691P → F in AAA34437. Ref.1
Sequence conflict3161F → L in AAA34437. Ref.1
Sequence conflict329 – 3324SYFT → FLLH in AAA34437. Ref.1
Sequence conflict329 – 3324SYFT → FLLH in CAA62528. Ref.2
Sequence conflict329 – 3324SYFT → FLLH in CAA99067. Ref.3

Sequences

Sequence LengthMass (Da)Tools
P22768 [UniParc].

Last modified September 21, 2011. Version 3.
Checksum: 155E1A4775B6FA9B

FASTA42046,928
        10         20         30         40         50         60 
MSKGKVCLAY SGGLDTSVIL AWLLDQGYEV VAFMANVGQE EDFDAAKEKA LKIGACKFVC 

        70         80         90        100        110        120 
VDCREDFVKD ILFPAVQVNA VYEDVYLLGT SLARPVIAKA QIDVAKQEGC FAVSHGCTGK 

       130        140        150        160        170        180 
GNDQIRFELS FYALKPDVKC ITPWRMPEFF ERFAGRKDLL DYAAQKGIPV AQTKAKPWST 

       190        200        210        220        230        240 
DENQAHISYE AGILEDPDTT PPKDMWKLIV DPMDAPDQPQ DLTIDFERGL PVKLTYTDNK 

       250        260        270        280        290        300 
TSKEVSVTKP LDVFLAASNL ARANGVGRID IVEDRYINLK SRGCYEQAPL TVLRKAHVDL 

       310        320        330        340        350        360 
EGLTLDKEVR QLRDSFVTPN YSRLIYNGSY FTPECEYIRS MIQPSQNSVN GTVRVRLYKG 

       370        380        390        400        410        420 
NVIILGRSTK TEKLYDPTES SMDELTGFLP TDTTGFIAIQ AIRIKKYGES KKTKGEELTL 

« Hide

References

« Hide 'large scale' references
[1]"Sequences of the genes encoding argininosuccinate synthetase in Escherichia coli and Saccharomyces cerevisiae: comparison with methanogenic archaebacteria and mammals."
van Vliet F., Crabeel M., Boyen A., Tricot C., Stalon V., Falmagne P., Nakamura Y., Baumberg S., Glansdorff N.
Gene 95:99-104(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Analysis of a 26 kb region on the left arm of yeast chromosome XV."
Mannhaupt G., Vetter I., Schwarzlose C., Mitzel S., Feldmann H.
Yeast 12:67-76(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 90843 / S288c / FY73.
[3]"The nucleotide sequence of Saccharomyces cerevisiae chromosome XV."
Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J., Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A., Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B., Dang V.-D. expand/collapse author list , de Haan M., Delius H., Durand P., Fairhead C., Feldmann H., Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E., Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U., Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B., Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A., Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C., Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G., Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B., Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F., Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E., Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I., Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H., Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.
Nature 387:98-102(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[4]"The reference genome sequence of Saccharomyces cerevisiae: Then and now."
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.
G3 (Bethesda) 4:389-398(2014) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION, SEQUENCE REVISION TO 329-332.
Strain: ATCC 204508 / S288c.
[5]"Arginine repression of the Saccharomyces cerevisiae ARG1 gene. Comparison of the ARG1 and ARG3 control regions."
Crabeel M., Seneca S., Devos K., Glansdorff N.
Curr. Genet. 13:113-124(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-57.
[6]"Arginine metabolism in Saccharomyces cerevisiae: subcellular localization of the enzymes."
Jauniaux J.-C., Urrestarazu L.A., Wiame J.-M.
J. Bacteriol. 133:1096-1107(1978) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[7]"Yeast argininosuccinate synthetase. Purification; structural and kinetic properties."
Hilger F., Simon J.-P., Stalon V.
Eur. J. Biochem. 94:153-163(1979) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES.
[8]"Global analysis of protein localization in budding yeast."
Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K.
Nature 425:686-691(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[9]"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] [Europe PMC] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M35237 Genomic DNA. Translation: AAA34437.1.
X91067 Genomic DNA. Translation: CAA62528.1.
Z74800 Genomic DNA. Translation: CAA99067.1.
X07070 Genomic DNA. Translation: CAA30106.1.
BK006948 Genomic DNA. Translation: DAA10725.2.
PIRAJBYRS. S59291.
RefSeqNP_014583.2. NM_001183313.2.

3D structure databases

ProteinModelPortalP22768.
SMRP22768. Positions 3-405.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid34343. 17 interactions.
DIPDIP-1660N.
IntActP22768. 4 interactions.
MINTMINT-393127.
STRING4932.YOL058W.

Proteomic databases

MaxQBP22768.
PaxDbP22768.
PeptideAtlasP22768.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYOL058W; YOL058W; YOL058W.
GeneID854096.
KEGGsce:YOL058W.

Organism-specific databases

CYGDYOL058w.
SGDS000005419. ARG1.

Phylogenomic databases

eggNOGCOG0137.
GeneTreeENSGT00390000004524.
HOGENOMHOG000230093.
KOK01940.
OMAPECEYIR.
OrthoDBEOG7KSXJR.

Enzyme and pathway databases

BioCycYEAST:YOL058W-MONOMER.
UniPathwayUPA00068; UER00113.

Gene expression databases

GenevestigatorP22768.

Family and domain databases

Gene3D3.40.50.620. 1 hit.
3.90.1260.10. 1 hit.
HAMAPMF_00005. Arg_succ_synth_type1.
InterProIPR001518. Arginosuc_synth.
IPR018223. Arginosuc_synth_CS.
IPR023434. Arginosuc_synth_type_1_subfam.
IPR024074. AS_cat/multimer_dom_body.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view]
PfamPF00764. Arginosuc_synth. 1 hit.
[Graphical view]
TIGRFAMsTIGR00032. argG. 1 hit.
PROSITEPS00564. ARGININOSUCCIN_SYN_1. 1 hit.
PS00565. ARGININOSUCCIN_SYN_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio975761.
PROP22768.

Entry information

Entry nameASSY_YEAST
AccessionPrimary (citable) accession number: P22768
Secondary accession number(s): D6W209
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: September 21, 2011
Last modified: May 14, 2014
This is version 125 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome XV

Yeast (Saccharomyces cerevisiae) chromosome XV: entries and gene names

Yeast

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

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways