ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!
Search for

UniProtKB/Swiss-Prot entry Q8F6R2


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

Note: most headings are clickable, even if they don't appear as links. They link to the user manual or other documents.
Entry information
Entry name CARA_LEPIN
Primary accession number Q8F6R2
Secondary accession numbers None
Integrated into Swiss-Prot on June 6, 2003
Sequence was last modified on March 1, 2003 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 45)
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: LA_1239
From
Leptospira interrogans [TaxID: 173] [HAMAP proteome]
Taxonomy Bacteria; Spirochaetes; Spirochaetales; Leptospiraceae; Leptospira.
Protein existence 3: Inferred from homology;
References
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=56601 / Serogroup Icterohaemorrhagiae / Serovar lai;
DOI=10.1038/nature01597; PubMed=12712204 [NCBI, ExPASy, EBI, Israel, Japan]
Ren S.-X., Fu G., Jiang X.-G., Zeng R., Miao Y.-G., Xu H., Zhang Y.-X., Xiong H., Lu G., Lu L.-F., Jiang H.-Q., Jia J., Tu Y.-F., Jiang J.-X., Gu W.-Y., Zhang Y.-Q., Cai Z., Sheng H.-H., Yin H.-F., Zhang Y., Zhu G.-F., Wan M., Huang H.-L., Qian Z., Wang S.-Y., Ma W., Yao Z.-J., Shen Y., Qiang B.-Q., Xia Q.-C., Guo X.-K., Danchin A., Saint Girons I., Somerville R.L., Wen Y.-M., Shi M.-H., Chen Z., Xu J.-G., Zhao G.-P.;
"Unique physiological and pathogenic features of Leptospira interrogans revealed by whole-genome sequencing.";
Nature 422:888-893(2003).
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
AE010300; AAN48438.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_711420.1; -.
3D structure databases
HSSP P00907; 1M6V. [HSSP ENTRY / PDB]
ModBase Q8F6R2.
Enzyme and pathway databases
BioCyc LINT189518:LA1239-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 1150582; -.
GenomeReviews AE010300_GR; LA_1239.
KEGG lil:LA1239; -.
NMPDR fig|189518.1.peg.1239; -.
Phylogenomic databases
HOGENOM Q8F6R2; -.
Genome annotation databases
CMR Q8F6R2; LA_1239.
Other
ProtoNet Q8F6R2.
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   363  363     Carbamoyl-phosphate synthase small chain. PRO_0000112289
DOMAIN   177   363  187     Glutamine amidotransferase type-1. 
REGION   1   173  173     CPSase. 
ACT_SITE   253   253        Nucleophile (By similarity). 
ACT_SITE   336   336        By similarity. 
ACT_SITE   338   338        By similarity. 
Sequence information
Length: 363 AA [This is the length of the unprocessed precursor] Molecular weight: 40261 Da [This is the MW of the unprocessed precursor] CRC64: 58BD2BB8F43D0BEE [This is a checksum on the sequence]
        10         20         30         40         50         60 
MMKAFLVLDN GTIFEGESFG YETESVGEIV FNTSMAGYQE ILTDPSYCNQ IITLTYPMIG 

        70         80         90        100        110        120 
NYGIHPDNME SSKIQASGLI VKEYVDLPSN FKSEKTLSQF LKEYKIPAIQ GIDTRKLTRF 

       130        140        150        160        170        180 
IRTNGSPNGG IFVASEYSPS FLEKVKSFPG IINADLAKVV TTSSKYIFGT HTGKKFKLAV 

       190        200        210        220        230        240 
YDYGVKTNIL RLLDANGFAV TVYPAKTPSE EIMKEGTDAF FLSNGPGDPA PLDYAIASTQ 

       250        260        270        280        290        300 
KIMEKRYPLF GICLGHQIIG LSLGKKTEKM KFGHRGGNQP VKNLETGQVE ITSQNHGFAV 

       310        320        330        340        350        360 
IDDQKQDEPI SFLNLNDHTV EGILKSGYPL LTVQYHPESA PGPNDSRYLF QKFYDLVEKT 


KKG 

Q8F6R2 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

BLAST logo BLAST submission on ExPASy/SIB
or at NCBI (USA)
Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
PROSITE logo ScanProsite, MotifScan SWISS-MODEL Submit a homology modeling request to SWISS-MODEL
NPSA logo NPSA Sequence analysis tools

ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
 Hosted by ca flag CBR Canada Mirror sites: Australia  Brazil  China  Korea  Switzerland
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!