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Q5FH27 (ASSY_EHRRG) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 63. 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:ERGA_CDS_03850
OrganismEhrlichia ruminantium (strain Gardel) [Complete proteome] [HAMAP]
Taxonomic identifier302409 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRickettsialesAnaplasmataceaeEhrlichia

Protein attributes

Sequence length394 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 – 394394Argininosuccinate synthase HAMAP-Rule MF_00005
PRO_0000263925

Regions

Nucleotide binding7 – 159ATP By similarity

Sites

Binding site341ATP; via amide nitrogen and carbonyl oxygen By similarity
Binding site851Citrulline By similarity
Binding site901Citrulline By similarity
Binding site1151ATP; via amide nitrogen By similarity
Binding site1171Aspartate By similarity
Binding site1211Aspartate By similarity
Binding site1211Citrulline By similarity
Binding site1221Aspartate By similarity
Binding site1251Citrulline By similarity
Binding site1761Citrulline By similarity
Binding site1851Citrulline By similarity
Binding site2611Citrulline By similarity
Binding site2731Citrulline By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5FH27 [UniParc].

Last modified March 1, 2005. Version 1.
Checksum: 6778BFEC73A33D1D

FASTA39444,673
        10         20         30         40         50         60 
MKKIVLAYSG GLDTSVILKW LQENYNCEVV VFTADIGQED DMSVIQKKAA ALNVKEIFIE 

        70         80         90        100        110        120 
DLKEEFVRDF VFPMFRANTI YEGYYLLGTS IARPLIAKRQ IEIAHLTGAD AVAHGATGKG 

       130        140        150        160        170        180 
NDQVRFEFGY YCCDPNIKVI APWRQWELTS RHSLIEYARK NNINVPLDKV NEPPYSIDAN 

       190        200        210        220        230        240 
LLHISYEGKS LEDPYVEPDY TMLSRSLTPE LASSIPEYIE ITFEQGDPIA INDIPLSPAN 

       250        260        270        280        290        300 
LLHQLNKIGG KHGIGIVDIV ENRYIGIKSR GIYETPGGTI LLHAHRAIES ITLDRESAHL 

       310        320        330        340        350        360 
KDEIMPKYAK LIYNGYWWTT ERKMLQSLID NHKKKFNGTV RIKLYKGSVV VVGRKSNNSL 

       370        380        390 
YSYNLASFDS ESQGYDHKDA EGFIKVNSLR LKKS 

« Hide

References

[1]"Comparative genomic analysis of three strains of Ehrlichia ruminantium reveals an active process of genome size plasticity."
Frutos R., Viari A., Ferraz C., Morgat A., Eychenie S., Kandassamy Y., Chantal I., Bensaid A., Coissac E., Vachiery N., Demaille J., Martinez D.
J. Bacteriol. 188:2533-2542(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Gardel.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CR925677 Genomic DNA. Translation: CAI27837.1.
RefSeqYP_196311.1. NC_006831.1.

3D structure databases

ProteinModelPortalQ5FH27.
SMRQ5FH27. Positions 3-393.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING302409.ERGA_CDS_03850.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAI27837; CAI27837; ERGA_CDS_03850.
GeneID3268229.
KEGGerg:ERGA_CDS_03850.
PATRIC20578504. VBIEhrRum72196_0412.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCycERUM302409:GHVW-406-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_EHRRG
AccessionPrimary (citable) accession number: Q5FH27
Entry history
Integrated into UniProtKB/Swiss-Prot: December 12, 2006
Last sequence update: March 1, 2005
Last modified: February 19, 2014
This is version 63 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