Skip Header

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

Q752N9 (CARA_ASHGO) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 68. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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:
Carbamoyl-phosphate synthase arginine-specific small chain

Short name=CPS-A
EC=6.3.5.5
Alternative name(s):
Arginine-specific carbamoyl-phosphate synthetase, glutamine chain
Gene names
Name:CPA1
Ordered Locus Names:AFR534W
OrganismAshbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056) (Yeast) (Eremothecium gossypii) [Complete proteome]
Taxonomic identifier284811 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeEremothecium

Protein attributes

Sequence length399 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

2 ATP + L-glutamine + HCO3- + H2O = 2 ADP + phosphate + L-glutamate + carbamoyl phosphate.

Pathway

Amino-acid biosynthesis; L-arginine biosynthesis; carbamoyl phosphate from bicarbonate: step 1/1.

Subunit structure

Composed of two chains; the small (or glutamine) chain promotes the hydrolysis of glutamine to ammonia, which is used by the large (or ammonia) chain to synthesize carbamoyl phosphate By similarity.

Subcellular location

Cytoplasm By similarity.

Sequence similarities

Belongs to the CarA family.

Contains 1 glutamine amidotransferase type-1 domain.

Ontologies

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

Inferred from electronic annotation. Source: UniProtKB-KW

glutamine metabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 399399Carbamoyl-phosphate synthase arginine-specific small chain
PRO_0000290585

Regions

Domain187 – 379193Glutamine amidotransferase type-1

Sites

Active site2671Nucleophile By similarity
Active site3521 By similarity
Active site3541 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q752N9 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: FEBA86DFDA1B2411

FASTA39943,842
        10         20         30         40         50         60 
MTSDEAKKAR FCLHGGPSYE GYSFGAPVSV GGEVVFTTSL VGYPDSMTDP SYKGQILVFT 

        70         80         90        100        110        120 
QPLIGNYGVP DGSVRDQYGL LKYMESSKVH VSAIVVAEYA WEYSHWTAVQ SLGDWCRKEG 

       130        140        150        160        170        180 
VAAIGGIDTR AVVQYLRESG STMGRVDVEG AAASARVVDP SKVNLVAQVS TKSPFYIPGK 

       190        200        210        220        230        240 
PSRVNYDVAL VDCGVKENIL RCLVVRGVNV TVFPYDYDVC SIAHHFDGVF ISNGPGDPIH 

       250        260        270        280        290        300 
YRNSTVANLR RLLQDPDLQQ VPIFGICMGH QLLALAAGAS TVKMKYGNRA HNIPALDLST 

       310        320        330        340        350        360 
GQCHITSQNH GYAVDAATLP RDEFVPLFVN LNDKSNEGII HVSRPIYSTQ FHPEGKGGPM 

       370        380        390 
DCSFLFDEYV ERMRCYRKLF RQEPFIRFPV IGLPKARVL 

« Hide

References

[1]"The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces cerevisiae genome."
Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S., Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A., Gaffney T.D., Philippsen P.
Science 304:304-307(2004) [PubMed: 15001715] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE016819 Genomic DNA. Translation: AAS53905.1.
RefSeqNP_986081.1. NM_212217.1.

3D structure databases

HSSPHSSP built from PDB template 1A9X based on UniProtKB P0A6F1.
ProteinModelPortalQ752N9.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ752N9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4622360.
GenomeReviewsGene locus AFR534W in contig AE016819_GR.
KEGGago:AGOS_AFR534W.
NMPDRfig|33169.1.peg.3726.

Organism-specific databases

AGDAFR534W.

Phylogenomic databases

eggNOGfuNOG04647.
HOGENOMHBG286341.
OMAGWNDEDS.
OrthoDBEOG4N8VDH.
PhylomeDBQ752N9.

Family and domain databases

InterProIPR006274. CarbamoylP_synth_ssu.
IPR002474. CarbamoylP_synth_ssu_N.
IPR017926. GATASE_1.
[Graphical view]
Gene3DG3DSA:3.50.30.20. G3DSA:3.50.30.20. 1 hit.
KOK01956.
PfamPF00988. CPSase_sm_chain. 1 hit.
PF00117. GATase. 1 hit.
[Graphical view]
SMARTSM01097. CPSase_sm_chain. 1 hit.
[Graphical view]
SUPFAMSSF52021. CP_synthsmall. 1 hit.
TIGRFAMsTIGR01368. CPSaseIIsmall. 1 hit.
PROSITEPS51273. GATASE_TYPE_1. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCARA_ASHGO
AccessionPrimary (citable) accession number: Q752N9
Entry history
Integrated into UniProtKB/Swiss-Prot: June 12, 2007
Last sequence update: July 5, 2004
Last modified: January 25, 2012
This is version 68 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families