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Q4WU09 (CARA_ASPFU) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 54. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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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:AFUA_5G06780
OrganismNeosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus)
Taxonomic identifier330879 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › mitosporic Trichocomaceae › Aspergillus

Protein attributes

Sequence length453 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
Reference 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 – 453453Carbamoyl-phosphate synthase arginine-specific small chain
PRO_0000290587

Regions

Domain219 – 406188Glutamine amidotransferase type-1
Compositional bias443 – 45311Poly-Ala

Sites

Active site2951Nucleophile By similarity
Active site3791 By similarity
Active site3811 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q4WU09 [UniParc].

Last modified July 5, 2005. Version 1.
Checksum: 714FE9F43B65E5F7

FASTA45349,337
        10         20         30         40         50         60 
MFARVFKAMP ARASALTSVN ASIPARFMAT VRQQRPAHER ATFTIRDGPI FHGKSFGART 

        70         80         90        100        110        120 
NISGEAVFTT SLVGYPESLT DPSYRGQILV FTQPLIGNYG VPSAERDEHG LLKYFESPNL 

       130        140        150        160        170        180 
QAAGVVVADV AEQYSHWTAV ESLGEWCARE GVPAISGVDT RAIVTYLRER GSSLARITVG 

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

       250        260        270        280        290        300 
GITVFPFDYP IHKVAHHFDG VFISNGPGDP THCQETTYHL RRLMETSQVP IFGICLGHQL 

       310        320        330        340        350        360 
LALAAGARTI KLKYGNRAHN IPALDLSTGR CHITSQNHGY AVDASTLPSD WKPYFVNLND 

       370        380        390        400        410        420 
SSNEGMIHKS RPIFSTQFHP EAKGGPLDSS YLFDIYIDSV KKYKASQAAF YPQRDSLPSP 

       430        440        450 
LLVDLLAKER VGVQPTIGMQ NIAAAATAAA AAA

« Hide

References

[1]"Genomic sequence of the pathogenic and allergenic filamentous fungus Aspergillus fumigatus."
Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J., Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P., Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L. expand/collapse author list , Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N., Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K., Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E., Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H., Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A., Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L., Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D., O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L., Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U., Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M., Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C., Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F., Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R., Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N., Barrell B.G., Denning D.W.
Nature 438:1151-1156(2005) [PubMed: 16372009] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AAHF01000003 Genomic DNA. Translation: EAL91917.1.
RefSeqXP_753955.1. XM_748862.1.

3D structure databases

HSSPHSSP built from PDB template 1CS0 based on UniProtKB P0A6F1.
ProteinModelPortalQ4WU09.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ4WU09.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiCADAFUAT00006529; CADAFUAP00006529; CADAFUAG00006529.
GeneID3510728.
GenomeReviewsGene locus cpa1 in contig CM000173_GR.
KEGGafm:AFUA_5G06780.

Phylogenomic databases

eggNOGfuNOG04647.
GeneTreeEFGT00050000001199.
HOGENOMHBG286341.
OMAQNHSYVV.
OrthoDBEOG4N8VDH.

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_ASPFU
AccessionPrimary (citable) accession number: Q4WU09
Entry history
Integrated into UniProtKB/Swiss-Prot: June 12, 2007
Last sequence update: July 5, 2005
Last modified: January 25, 2012
This is version 54 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

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