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

A5UFF8 (ASSY_HAEIG) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 47. 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:CGSHiGG_02370
OrganismHaemophilus influenzae (strain PittGG) [Complete proteome] [HAMAP]
Taxonomic identifier374931 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPasteurellalesPasteurellaceaeHaemophilus

Protein attributes

Sequence length444 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_00581

Pathway

Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine from L-ornithine and carbamoyl phosphate: step 2/3. HAMAP-Rule MF_00581

Subunit structure

Homotetramer By similarity. HAMAP-Rule MF_00581

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00581.

Sequence similarities

Belongs to the argininosuccinate synthase family. Type 2 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 – 444444Argininosuccinate synthase HAMAP-Rule MF_00581
PRO_1000025427

Regions

Nucleotide binding18 – 269ATP By similarity

Sites

Binding site441ATP By similarity
Binding site1001Citrulline By similarity
Binding site1301ATP; via amide nitrogen By similarity
Binding site1321Aspartate By similarity
Binding site1321ATP By similarity
Binding site1361Aspartate By similarity
Binding site1361Citrulline By similarity
Binding site1371Aspartate By similarity
Binding site1371ATP By similarity
Binding site1401Citrulline By similarity
Binding site1931Citrulline By similarity
Binding site1951ATP By similarity
Binding site2021Citrulline By similarity
Binding site2041Citrulline By similarity
Binding site2811Citrulline By similarity

Sequences

Sequence LengthMass (Da)Tools
A5UFF8 [UniParc].

Last modified July 10, 2007. Version 1.
Checksum: F833EDD718199098

FASTA44449,289
        10         20         30         40         50         60 
MSNTILQNLP KGQKVGIAFS GGLDTSAALL WMRQKGAVPY AYTANLGQPD EDDYNAIPKK 

        70         80         90        100        110        120 
AMAYGAENAR LIDCRAQLAH EGIAAIQCGA FHISTGGIPY FNTTPLGRAV TGTMLVAAMK 

       130        140        150        160        170        180 
EDDVNIWGDG STFKGNDIER FYRYGLLTNP NLKIYKPWLD VQFIEELGGR LEMSQFLIEN 

       190        200        210        220        230        240 
GFDYKMSVEK AYSTDSNMLG ATHEAKDLEQ LSTGMKIVKP IMGVAFWDEK VEIKPETVTV 

       250        260        270        280        290        300 
TFEDGVPVAL NGKHFDNAVD LILEANRIGG RHGLGMSDQI ENRIIEAKSR GIYEAPGMAL 

       310        320        330        340        350        360 
LHIAYERLVT GIHNEDTIEQ YRINGIRLGR LLYQGRWFDP QALMLRETAQ RWVAKAITGT 

       370        380        390        400        410        420 
VTLELRRGND FTILNTESPN LTYEAERLSM EKVEDAPFDP IDRIGQLTMR NLDVSDTRGK 

       430        440 
LGIYAQTGLL SAIKDSVLPQ LGKK 

« Hide

References

[1]"Characterization and modeling of the Haemophilus influenzae core and supragenomes based on the complete genomic sequences of Rd and 12 clinical nontypeable strains."
Hogg J.S., Hu F.Z., Janto B., Boissy R., Hayes J., Keefe R., Post J.C., Ehrlich G.D.
Genome Biol. 8:R103.1-R103.18(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: PittGG.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000672 Genomic DNA. Translation: ABQ99513.1.
RefSeqYP_001291897.1. NC_009567.1.

3D structure databases

ProteinModelPortalA5UFF8.
SMRA5UFF8. Positions 4-441.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING374931.CGSHiGG_02370.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABQ99513; ABQ99513; CGSHiGG_02370.
GeneID5226989.
KEGGhiq:CGSHiGG_02370.
PATRIC20185102. VBIHaeInf102487_0475.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0137.
HOGENOMHOG000230094.
KOK01940.
OMAMRNLDIA.
OrthoDBEOG6K9QCV.
ProtClustDBPRK05370.

Enzyme and pathway databases

BioCycHINF374931:GJA4-391-MONOMER.
UniPathwayUPA00068; UER00113.

Family and domain databases

Gene3D1.10.287.400. 1 hit.
3.40.50.620. 1 hit.
3.90.1260.10. 1 hit.
HAMAPMF_00581. Arg_succ_synth_type2.
InterProIPR023437. Arg_succ_synth_type2_subfam.
IPR001518. Arginosuc_synth.
IPR018223. Arginosuc_synth_CS.
IPR024074. AS_cat/multimer_dom_body.
IPR024073. AS_multimer_C_tail.
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_HAEIG
AccessionPrimary (citable) accession number: A5UFF8
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: July 10, 2007
Last modified: February 19, 2014
This is version 47 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