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UniProtKB/Swiss-Prot entry Q8K9Z6

[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name CARA_BUCAP
Primary accession number Q8K9Z6
Secondary accession numbers None
Integrated into Swiss-Prot on November 8, 2002
Sequence was last modified on October 1, 2002 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 51)
Name and origin of the protein
Protein name Carbamoyl-phosphate synthase small chain
Synonyms EC 6.3.5.5
Carbamoyl-phosphate synthetase glutamine chain
Gene name
Name: carA
OrderedLocusNames: BUsg_138
From
Buchnera aphidicola subsp. Schizaphis graminum [TaxID: 98794] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; Enterobacteriaceae; Buchnera.
Protein existence 3: Inferred from homology;
References
[1]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1126/science.1071278; PubMed=12089438 [NCBI, ExPASy, EBI, Israel, Japan]
Tamas I., Klasson L., Canbaeck B., Naeslund A.K., Eriksson A.-S., Wernegreen J.J., Sandstroem J.P., Moran N.A., Andersson S.G.E.;
"50 million years of genomic stasis in endosymbiotic bacteria.";
Science 296:2376-2379(2002).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AE013218; AAM67706.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_660495.1; -.
3D structure databases
HSSP P00907; 1CE8. [HSSP ENTRY / PDB]
ModBase Q8K9Z6.
Enzyme and pathway databases
BioCyc BAPH198804:BUSG138-MON; -.
Ontologies
GO
GO:0005524; Molecular function: ATP binding (inferred from electronic annotation from HAMAP).
GO:0004088; Molecular function: carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity (inferred from electronic annotation from HAMAP).
GO:0006526; Biological process: arginine biosynthetic process (inferred from electronic annotation from HAMAP).
GO:0006541; Biological process: glutamine metabolic process (inferred from electronic annotation from InterPro).
GO:0006221; Biological process: pyrimidine nucleotide biosynthetic process (inferred from electronic annotation from HAMAP).
QuickGo view.
Family and domain databases
HAMAP MF_01209; -; 1.
PBIL [Tree]
InterPro IPR006220; Anth_synthII.
IPR001317; CarbamoylP_synth_GATase.
IPR006274; CarbamoylP_synth_ssu.
IPR002474; CarbamoylP_synth_ssu_N.
IPR011702; GATASE.
IPR012998; GATase_1_AS.
IPR000991; GATase_class1_C.
Graphical view of domain structure.
PANTHER PTHR11405:SF4; CarA_synth_small; 1.
Pfam PF00988; CPSase_sm_chain; 1.
PF00117; GATase; 1.
Pfam graphical view of domain structure.
PRINTS PR00097; ANTSNTHASEII.
PR00099; CPSGATASE.
PR00096; GATASE.
TIGRFAMs TIGR01368; CPSaseIIsmall; 1.
PROSITE PS51273; GATASE_TYPE_1; 1.
PROSITE graphical view of domain structure (profiles).
Genome annotation databases
GeneID 1005955; -.
GenomeReviews AE013218_GR; BUsg_138.
KEGG bas:BUsg138; -.
Phylogenomic databases
HOGENOM Q8K9Z6; -.
Genome annotation databases
CMR Q8K9Z6; BUsg_138.
Other
ProtoNet Q8K9Z6.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Amino-acid biosynthesis; Arginine biosynthesis; Complete proteome; Glutamine amidotransferase; Ligase; Pyrimidine biosynthesis.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   385  385     Carbamoyl-phosphate synthase small chain. PRO_0000112262
DOMAIN   197   384  188     Glutamine amidotransferase type-1. 
REGION   1   193  193     CPSase. 
ACT_SITE   273   273        Nucleophile (By similarity). 
ACT_SITE   357   357        By similarity. 
ACT_SITE   359   359        By similarity. 
Sequence information
Length: 385 AA [This is the length of the unprocessed precursor] Molecular weight: 42790 Da [This is the MW of the unprocessed precursor] CRC64: 496864F8283BDE54 [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MEDALGQLAV LVLEDGTRFH GRSIGAKGTT VGEVVFNTSI TGYQEIITDP SYSHQIVTLT 

        70         80         90        100        110        120 
HPHIGNIGTN CNDEESSKIH IRGLIIRDMS PISSNYRSEK SFSSYLKENN IVAISDIDTR 

       130        140        150        160        170        180 
KLTRILRTKG SQNGCIIEDK KENYSVAYQK AKKFLSLQGL DLAKKVSTKF IYNWDKGSFF 

       190        200        210        220        230        240 
INKSKSKLEK KKKFLFHIVV YDFGVKRNIL RMLVDRGCYL TVVPAKTDPK IALNLNPDGI 

       250        260        270        280        290        300 
FLSNGPGDPR PCDYAIHAIQ CFLKKNIPIF GICLGHQLLA LASGANIIKM KFGHHGGNHP 

       310        320        330        340        350        360 
VKEIKTNRVI ITSQNHSFTV DAKNMPNNIA ITHSSLFDGT LQGLCLTDKL AFSFQGHPEA 

       370        380 
SPGPHDASSL FDHFIKLLNQ VKFSN
Q8K9Z6 in FASTA format

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