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

A1ATU4 (ASSY_PELPD) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 45. 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:Ppro_3171
OrganismPelobacter propionicus (strain DSM 2379) [Complete proteome] [HAMAP]
Taxonomic identifier338966 [NCBI]
Taxonomic lineageBacteriaProteobacteriaDeltaproteobacteriaDesulfuromonadalesPelobacteraceaePelobacter

Protein attributes

Sequence length408 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 – 408408Argininosuccinate synthase HAMAP-Rule MF_00005
PRO_1000000416

Regions

Nucleotide binding14 – 229ATP By similarity

Sites

Binding site411ATP; 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 site1811Citrulline By similarity
Binding site1901Citrulline By similarity
Binding site2661Citrulline By similarity
Binding site2781Citrulline By similarity

Sequences

Sequence LengthMass (Da)Tools
A1ATU4 [UniParc].

Last modified January 23, 2007. Version 1.
Checksum: A2EF9B029764DF1B

FASTA40846,135
        10         20         30         40         50         60 
MTQQKMDIKN VVLAYSGGLD TSIILKWLKN EYGCRVVAFS ADLGQGEELD PVREKALATG 

        70         80         90        100        110        120 
ADVVYIDDLR EEFVRDFVFP MFRANAIYEG HYLLGTSIAR PLIAKRQMEI AAKEGCDAVS 

       130        140        150        160        170        180 
HGSTGKGNDQ VRFELGYYHF NPNIKIVAPW RTWDLNSRQA LIDYAKKNGI PVPVTKKRPW 

       190        200        210        220        230        240 
SSDRNLLHIS FEGGILEDTW AEAPEEMYVL TTAPEKAPNK PQYVEIEFKN GNAVAVDGEK 

       250        260        270        280        290        300 
MTPAQLLAHL NYLGGQHGIG RVDLLENRSV GMKSRGVYET PGGTILREAH MAVEQITMDR 

       310        320        330        340        350        360 
EVMRIRDGLI PEYARLVYAG YWFSPEREML QALIDDSQKC VNGVARLKLY KGYCRTVGRK 

       370        380        390        400 
SDTDSLFNQD FATFEKDQVY NQADAEGFIR INSLRLRIRS MMQAAKKK 

« Hide

References

[1]"Complete sequence of chromosome of Pelobacter propionicus DSM 2379."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Saunders E., Brettin T., Bruce D., Han C., Tapia R., Schmutz J., Larimer F. expand/collapse author list , Land M., Hauser L., Kyrpides N., Kim E., Lovley D., Richardson P.
Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 2379.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000482 Genomic DNA. Translation: ABL00765.1.
RefSeqYP_902822.1. NC_008609.1.

3D structure databases

ProteinModelPortalA1ATU4.
SMRA1ATU4. Positions 11-403.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING338966.Ppro_3171.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABL00765; ABL00765; Ppro_3171.
GeneID4573273.
KEGGppd:Ppro_3171.
PATRIC22899483. VBIPelPro64470_3328.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCycPPRO338966:GHL0-3228-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_PELPD
AccessionPrimary (citable) accession number: A1ATU4
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: January 23, 2007
Last modified: February 19, 2014
This is version 45 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