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Reviewed, UniProtKB/Swiss-Prot Q2H132 (CARA_CHAGB)

Last modified June 16, 2009. Version 23. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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
ORF Names: CHGG_04514
OrganismChaetomium globosum (Soil fungus) [Complete proteome]
Taxonomic identifier38033 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesSordariomycetidaeSordarialesChaetomiaceaeChaetomium

Protein attributes

Sequence length461 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
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 HCO(3)(-): 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 – 461461Carbamoyl-phosphate synthase arginine-specific small chain
PRO_0000290592

Regions

Domain240 – 427188Glutamine amidotransferase type-1

Sites

Active site3161Nucleophile By similarity
Active site4001 By similarity
Active site4021 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q2H132-1 [UniParc].

Last modified March 21, 2006. Version 1.
Checksum: 733A877682E9348A

FASTA46150,215
        10         20         30         40         50         60 
MSFFFSRQSD ISFLLFSEST STTRNSSQAR LLSRLAVDGS KGRAMPVLNT TRATAAASGV 

        70         80         90        100        110        120 
DATLTIRDGP VFHGTAFGAN SNISGEAVFT TSLVGYPESM TDPSYRGQIL VFTQPLIGNY 

       130        140        150        160        170        180 
GVPSNQRDEY GLLKYFESPH IQCAGVVVAD VAEKYSHWTA VESLSEWCAR EGVPVISGVD 

       190        200        210        220        230        240 
TRAIVTHLRE QGSSLARISI GDEYDADEDE GFIDPGAINL VKRVSTKAPF VVSNPNATFH 

       250        260        270        280        290        300 
VALIDCGVKE NILRSLVSRG ASVTVFPYNY PIHKVADNFD GVFISNGPGD PTHCQETVYN 

       310        320        330        340        350        360 
LGRLMETSSV PIMGICLGHQ LLALAVGAQT IKLKYGNRAH NIPALDLTTG QCHITSQNHG 

       370        380        390        400        410        420 
YAVDASTLPS EFKEYFVNLN DGSNEGMMHK TRPIFSTQFH PEAKGGPMDS SYLFDKYLEN 

       430        440        450        460 
VQMYKDNSKV YRDNRPSQLM IDILSKERVG VEPSPLAANA I 

« Hide

References

Cross-references

Sequence databases

CH408032 Genomic DNA. Translation: EAQ87895.1.
RefSeqXP_001223728.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID4392718.

Enzyme and pathway databases

BRENDA6.3.5.5. 81575.

Family and domain databases

InterProIPR006220. Anth_synthII.
IPR001317. CarbamoylP_synth_GATase.
IPR006274. CarbamoylP_synth_ssu.
IPR002474. CarbamoylP_synth_ssu_N.
IPR011702. GATASE.
IPR017926. GATASE_1.
IPR000991. GATase_class1_C.
[Graphical view]
PANTHERPTHR11405:SF4. CarA_synth_small. 1 hit.
PfamPF00988. CPSase_sm_chain. 1 hit.
PF00117. GATase. 1 hit.
[Graphical view]
PRINTSPR00097. ANTSNTHASEII.
PR00099. CPSGATASE.
PR00096. GATASE.
TIGRFAMsTIGR01368. CPSaseIIsmall. 1 hit.
PROSITEPS51273. GATASE_TYPE_1. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCARA_CHAGB
AccessionPrimary (citable) accession number: Q2H132
Entry history
Integrated into UniProtKB/Swiss-Prot: June 12, 2007
Last sequence update: March 21, 2006
Last modified: June 16, 2009
This is version 23 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectFPAP (Fungal Proteome Annotation Project)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents