Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

A0RP84 (ASSY_CAMFF) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 50. 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:CFF8240_0842
OrganismCampylobacter fetus subsp. fetus (strain 82-40) [Complete proteome] [HAMAP]
Taxonomic identifier360106 [NCBI]
Taxonomic lineageBacteriaProteobacteriaEpsilonproteobacteriaCampylobacteralesCampylobacteraceaeCampylobacter

Protein attributes

Sequence length407 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 – 407407Argininosuccinate synthase HAMAP-Rule MF_00005
PRO_0000321305

Regions

Nucleotide binding12 – 209ATP By similarity

Sites

Binding site391ATP; via amide nitrogen and carbonyl oxygen By similarity
Binding site921Citrulline By similarity
Binding site971Citrulline By similarity
Binding site1221ATP; via amide nitrogen By similarity
Binding site1241Aspartate By similarity
Binding site1281Aspartate By similarity
Binding site1281Citrulline By similarity
Binding site1291Aspartate By similarity
Binding site1321Citrulline By similarity
Binding site1821Citrulline By similarity
Binding site1911Citrulline By similarity
Binding site2671Citrulline By similarity
Binding site2791Citrulline By similarity

Sequences

Sequence LengthMass (Da)Tools
A0RP84 [UniParc].

Last modified January 9, 2007. Version 1.
Checksum: DB134F74F23EF276

FASTA40745,898
        10         20         30         40         50         60 
MQKKDVKKVV LAYSGGLDTS IILKWLQDEY KCEVVTFTAD IGQGEEVEPA RKKAISLGIK 

        70         80         90        100        110        120 
PENIFIEDLR EEFVKDFVFP MFRANAIYEG EYLLGTSIAR PLIAKRLVEI AAATKADCVS 

       130        140        150        160        170        180 
HGATGKGNDQ VRFEIGAYAL NPNIKVIAPW REWDLNSREK LLAYAEKNGI DISKKKGKSP 

       190        200        210        220        230        240 
YSMDANLLHI SYEGLVLEDP NHAPEEDMWR WSVSPKNAPD ESDIIEIEYK NGDPVAINAK 

       250        260        270        280        290        300 
SMKPHEILTE LNRLGAKHGI GRLDIVENRY VGMKSRGCYE TPGGTIMLKA HRAIESITMD 

       310        320        330        340        350        360 
REAAHLKDEL MPKYASLVYN GYWFSPERKM LQAAIDESQK NVNGTVRVEL YKGNVMVIGR 

       370        380        390        400 
DSKTDNLFNE AYCTFEEDSV YDQKDANGFI KLNALRFIIA GKNGRKF 

« Hide

References

[1]"Sequence of Campylobacter fetus subsp. fetus 82-40."
Fouts D.E., Nelson K.E.
Submitted (NOV-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 82-40.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000487 Genomic DNA. Translation: ABK82085.1.
RefSeqYP_892017.1. NC_008599.1.

3D structure databases

ProteinModelPortalA0RP84.
SMRA0RP84. Positions 8-402.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING360106.CFF8240_0842.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABK82085; ABK82085; CFF8240_0842.
GeneID4538985.
KEGGcff:CFF8240_0842.
PATRIC20036198. VBICamFet25865_0815.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCycCFET360106:GHTH-841-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_CAMFF
AccessionPrimary (citable) accession number: A0RP84
Entry history
Integrated into UniProtKB/Swiss-Prot: February 26, 2008
Last sequence update: January 9, 2007
Last modified: February 19, 2014
This is version 50 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