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A7H4E9 (ASSY_CAMJD) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 42. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Argininosuccinate synthase

EC=6.3.4.5
Alternative name(s):
Citrulline--aspartate ligase
Gene names
Name:argG
Ordered Locus Names:JJD26997_1334
OrganismCampylobacter jejuni subsp. doylei (strain ATCC BAA-1458 / RM4099 / 269.97) [Complete proteome] [HAMAP]
Taxonomic identifier360109 [NCBI]
Taxonomic lineageBacteriaProteobacteriaEpsilonproteobacteriaCampylobacteralesCampylobacteraceaeCampylobacter

Protein attributes

Sequence length406 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

ATP + L-citrulline + L-aspartate = AMP + diphosphate + N(omega)-(L-arginino)succinate. HAMAP-Rule MF_00005

Pathway

Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine from L-ornithine and carbamoyl phosphate: step 2/3. HAMAP-Rule MF_00005

Subunit structure

Homotetramer By similarity. HAMAP-Rule MF_00005

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00005.

Sequence similarities

Belongs to the argininosuccinate synthase family. Type 1 subfamily.

Ontologies

Keywords
   Biological processAmino-acid biosynthesis
Arginine biosynthesis
   Cellular componentCytoplasm
   LigandATP-binding
Nucleotide-binding
   Molecular functionLigase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processarginine biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

argininosuccinate synthase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 406406Argininosuccinate synthase HAMAP-Rule MF_00005
PRO_1000000388

Regions

Nucleotide binding11 – 199ATP By similarity

Sites

Binding site381ATP; via amide nitrogen and carbonyl oxygen By similarity
Binding site911Citrulline By similarity
Binding site961Citrulline By similarity
Binding site1211ATP; via amide nitrogen By similarity
Binding site1231Aspartate By similarity
Binding site1271Aspartate By similarity
Binding site1271Citrulline By similarity
Binding site1281Aspartate By similarity
Binding site1311Citrulline By similarity
Binding site1811Citrulline By similarity
Binding site1901Citrulline By similarity
Binding site2661Citrulline By similarity
Binding site2781Citrulline By similarity

Sequences

Sequence LengthMass (Da)Tools
A7H4E9 [UniParc].

Last modified September 11, 2007. Version 1.
Checksum: 27C8D021980D7D7E

FASTA40645,627
        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 RFELGYLAFN PDLKIIAPWR EWDLNSREKL LAYAQKHGID ISKKKGKSPY 

       190        200        210        220        230        240 
SMDANLLHIS YEGLVLEDPA HAPEEDMWRW SKSPKDAPHE 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 KGNVMVIGRQ 

       370        380        390        400 
SANDSLFNAA YCTFEEDEVY NQKDAAGFIK LNALRFIIAG KNGRKF 

« Hide

References

[1]"Complete genome sequence of Campylobacter jejuni subsp doylei 269.97 isolated from human blood."
Fouts D.E., Mongodin E.F., Puiu D., Sebastian Y., Miller W.G., Mandrell R.E., Lastovica A.J., Nelson K.E.
Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-1458 / RM4099 / 269.97.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000768 Genomic DNA. Translation: ABS44547.1.
RefSeqYP_001398379.1. NC_009707.1.

3D structure databases

ProteinModelPortalA7H4E9.
SMRA7H4E9. Positions 7-401.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING360109.JJD26997_1334.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABS44547; ABS44547; JJD26997_1334.
GeneID5388595.
KEGGcjd:JJD26997_1334.
PATRIC20048338. VBICamJej122183_1324.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0137.
HOGENOMHOG000230093.
KOK01940.
OMAIYNGYWW.
OrthoDBEOG6K9QCV.
ProtClustDBPRK00509.

Enzyme and pathway databases

BioCycCJEJ360109:GJDG-1296-MONOMER.
UniPathwayUPA00068; UER00113.

Family and domain databases

Gene3D3.40.50.620. 1 hit.
3.90.1260.10. 1 hit.
HAMAPMF_00005. Arg_succ_synth_type1.
InterProIPR001518. Arginosuc_synth.
IPR018223. Arginosuc_synth_CS.
IPR023434. Arginosuc_synth_type_1_subfam.
IPR024074. AS_cat/multimer_dom_body.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view]
PfamPF00764. Arginosuc_synth. 1 hit.
[Graphical view]
TIGRFAMsTIGR00032. argG. 1 hit.
PROSITEPS00564. ARGININOSUCCIN_SYN_1. 1 hit.
PS00565. ARGININOSUCCIN_SYN_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameASSY_CAMJD
AccessionPrimary (citable) accession number: A7H4E9
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: September 11, 2007
Last modified: February 19, 2014
This is version 42 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways