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UniProtKB/Swiss-Prot entry Q9PHK7

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

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Entry information
Entry name ASSY_CAMJE
Primary accession number Q9PHK7
Secondary accession number Q0PAK8
Integrated into Swiss-Prot on April 23, 2003
Sequence was last modified on October 1, 2000 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 50)
Name and origin of the protein
Protein name Argininosuccinate synthase
Synonyms EC 6.3.4.5
Citrulline--aspartate ligase
Gene name
Name: argG
OrderedLocusNames: Cj0665c
From
Campylobacter jejuni [TaxID: 197] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; Campylobacteraceae; Campylobacter.
Protein existence 1: Evidence at protein level;
References
[1]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=NCTC 11168 / Serotype O:2;
DOI=10.1038/35001088; PubMed=10688204 [NCBI, ExPASy, EBI, Israel, Japan]
Parkhill J., Wren B.W., Mungall K.L., Ketley J.M., Churcher C.M., Basham D., Chillingworth T., Davies R.M., Feltwell T., Holroyd S., Jagels K., Karlyshev A.V., Moule S., Pallen M.J., Penn C.W., Quail M.A., Rajandream M.A., Rutherford K.M., van Vliet A.H.M., Whitehead S., Barrell B.G.;
"The genome sequence of the food-borne pathogen Campylobacter jejuni reveals hypervariable sequences.";
Nature 403:665-668(2000).
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
AL111168; CAL34806.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR C81415; C81415.
3D structure databases
ModBase Q9PHK7.
Protein-protein interaction databases
IntAct Q9PHK7; -.
Enzyme and pathway databases
BioCyc CJEJ192222:CJ0665C-MON; -.
Ontologies
GO
GO:0005737; Cellular component: cytoplasm (inferred from electronic annotation from HAMAP).
GO:0004055; Molecular function: argininosuccinate synthase activity (inferred from electronic annotation from HAMAP).
GO:0005524; Molecular function: ATP binding (inferred from electronic annotation from HAMAP).
GO:0005515; Molecular function: protein binding (inferred from physical interaction from IntAct).
GO:0006526; Biological process: arginine biosynthetic process (inferred from electronic annotation from HAMAP).
QuickGo view.
Family and domain databases
HAMAP MF_00005; -; 1.
PBIL [Tree]
InterPro IPR001518; Arginosuc_synth.
IPR014729; Rossmann-like_a/b/a_fold.
Graphical view of domain structure.
Gene3D G3DSA:3.40.50.620; Rossmann-like_a/b/a_fold; 1.
PANTHER PTHR11587; Arginosuc_synth; 1.
Pfam PF00764; Arginosuc_synth; 1.
Pfam graphical view of domain structure.
TIGRFAMs TIGR00032; argG; 1.
PROSITE PS00564; ARGININOSUCCIN_SYN_1; 1.
PS00565; ARGININOSUCCIN_SYN_2; 1.
ProtoNet Q9PHK7.
Genome annotation databases
GenomeReviews AL111168_GR; Cj0665c.
KEGG cje:Cj0665c; -.
CMR Q9PHK7; Cj0665c.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Amino-acid biosynthesis; Arginine biosynthesis; ATP-binding; Complete proteome; Cytoplasm; Ligase; Nucleotide-binding.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   406  406     Argininosuccinate synthase. PRO_0000148580
NP_BIND   11    19  9     ATP (By similarity). 
BINDING   38    38        ATP; via amide nitrogen and carbonyl oxygen (By similarity). 
BINDING   91    91        Citrulline (By similarity). 
BINDING   96    96        Citrulline (By similarity). 
BINDING   121   121        ATP; via amide nitrogen (By similarity). 
BINDING   123   123        Aspartate (By similarity). 
BINDING   127   127        Aspartate (By similarity). 
BINDING   127   127        Citrulline (By similarity). 
BINDING   128   128        Aspartate (By similarity). 
BINDING   131   131        Citrulline (By similarity). 
BINDING   181   181        Citrulline (By similarity). 
BINDING   190   190        Citrulline (By similarity). 
BINDING   266   266        Citrulline (By similarity). 
BINDING   278   278        Citrulline (By similarity). 
Sequence information
Length: 406 AA [This is the length of the unprocessed precursor] Molecular weight: 45578 Da [This is the MW of the unprocessed precursor] CRC64: 8A1E137AF30EC77F [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MKNEVKKVVL AYSGGLDTSI ILKWLQDEYN CEVVTFTADI GQGEELEPAR KKALSLGIKE 

        70         80         90        100        110        120 
ENIFIKDLRD EFVKDYVFPM FRANAIYEGE YLLGTSIARP LIAKTQAQIA LQTGADAVSH 

       130        140        150        160        170        180 
GATGKGNDQV RFELGYLAFS PDLKIIAPWR EWDLNSREKL LAYAQKHGID ISKKKGKSPY 

       190        200        210        220        230        240 
SMDANLLHIS YEGLVLEDPA HAPEEDMWRW SKSPKDAPNE SEIIELDFQK GDLVAINGEK 

       250        260        270        280        290        300 
LSPAGLLTKL NELGCKHGIG RLDIVENRYV GMKSRGCYET PGGTILLKAH RALESITLDR 

       310        320        330        340        350        360 
EAAHLKDELM PKYASLIYNG YWFSPERMML QALIDESQIH ANGRVKLELY KGNVMVIGRE 

       370        380        390        400 
SANDSLFNAA YCTFEEDEVY NQKDAAGFIK LNALRFIIAG KNGRKF
Q9PHK7 in FASTA format

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