Skip Header

Contribute Send feedback
Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot Q5BB37 (CARA_EMENI)

Last modified February 9, 2010. Version 34. 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: cpa-1
ORF Names: AN2243
OrganismEmericella nidulans (Aspergillus nidulans) [Complete proteome]
Taxonomic identifier162425 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesTrichocomaceaeEmericella

Protein attributes

Sequence length417 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level.

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 – 417417Carbamoyl-phosphate synthase arginine-specific small chain
PRO_0000290595

Regions

Domain219 – 369151Glutamine amidotransferase type-1
Compositional bias406 – 41712Poly-Ala

Sites

Active site2951Nucleophile By similarity
Active site3421 By similarity
Active site3441 By similarity

Experimental info

Sequence conflict141A → P in CAA11831. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q5BB37-1 [UniParc].

Last modified April 26, 2005. Version 1.
Checksum: 8A72EF69232C40AB

FASTA41745,622
        10         20         30         40         50         60 
MMFSRFFKAV PARAPAFSSP LPVYQARTMA TVRNQRPVER ATFTIRDGPI FHGKSFGART 

        70         80         90        100        110        120 
TISGEAVFTT SLVGYPESLT DPSYRGQILV FTQPLIGNYG VPSTERDRHG LLKYFESPNL 

       130        140        150        160        170        180 
QAAGVVVADV AEQYSHWTAV QSLGEWCARE GVPAISGVDT RAIVTYLREQ GSSLARITVG 

       190        200        210        220        230        240 
EEYDADQDEA FTDPEQIHLV RQVSTKAPFH VSAADPQCHV AVLDCGVKEN ILRSLVSRGA 

       250        260        270        280        290        300 
SITVFPFDYP IHKVAHHFDG VFISNGPGDP THCQDTTYHL RRLMETSQVP IFGICLGHQL 

       310        320        330        340        350        360 
LALAADASTL PSDWKPYFVN LNDSSNEGMI HKSRPIFSTQ FHPEAKGGPL DSSYLFDIYI 

       370        380        390        400        410 
DSVKKYKNSQ LAFHPSRETI PSPLLVDLLP KERVDVAPTI GMQNVAAAAA AAAAATA 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AACD01000036 Genomic DNA. Translation: EAA63928.1.
AJ224085 mRNA. Translation: CAA11831.1.
RefSeqXP_659847.1.

3D structure databases

HSSPHSSP built from PDB template 1CE8 based on UniProtKB P0A6F1.
SMRQ5BB37. Positions 39-369.
ModBaseSearch...

Genome annotation databases

GeneID2875485.
KEGGani:AN2243.2.

Phylogenomic databases

PhylomeDBQ5BB37.

Enzyme and pathway databases

BRENDA6.3.5.5. 3859.

Family and domain databases

InterProIPR001317. CarbamoylP_synth_GATase_dom.
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]
PRINTSPR00099. CPSGATASE.
PR00096. GATASE.
TIGRFAMsTIGR01368. CPSaseIIsmall. 1 hit.
PROSITEPS51273. GATASE_TYPE_1. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCARA_EMENI
AccessionPrimary (citable) accession number: Q5BB37
Secondary accession number(s): O42806
Entry history
Integrated into UniProtKB/Swiss-Prot: June 12, 2007
Last sequence update: April 26, 2005
Last modified: February 9, 2010
This is version 34 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