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Q2N9H9 (ASSY_ERYLH) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 51. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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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:ELI_07850
OrganismErythrobacter litoralis (strain HTCC2594) [Complete proteome] [HAMAP]
Taxonomic identifier314225 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Alphaproteobacteria › Sphingomonadales › Erythrobacteraceae › Erythrobacter ›

Protein attributes

Sequence length404 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.

Subcellular location

Cytoplasm By similarity.

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: HAMAP

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: HAMAP

argininosuccinate synthase activity

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 404404Argininosuccinate synthase HAMAP-Rule MF_00005
PRO_0000321311

Regions

Nucleotide binding10 – 189ATP By similarity

Sites

Binding site371ATP; via amide nitrogen and carbonyl oxygen By similarity
Binding site901Citrulline By similarity
Binding site951Citrulline By similarity
Binding site1201ATP; via amide nitrogen By similarity
Binding site1221Aspartate By similarity
Binding site1261Aspartate By similarity
Binding site1261Citrulline By similarity
Binding site1271Aspartate By similarity
Binding site1301Citrulline By similarity
Binding site1811Citrulline By similarity
Binding site1901Citrulline By similarity
Binding site2661Citrulline By similarity
Binding site2781Citrulline By similarity

Sequences

Sequence LengthMass (Da)Tools
Q2N9H9 [UniParc].

Last modified February 7, 2006. Version 1.
Checksum: 2A352DEC5B6A2603

FASTA40445,157
        10         20         30         40         50         60 
MPDIKRVVLA YSGGLDTSVI AKWLEVERGL EVVTFTADLG QGEELEPARA KAQAMGIPDK 

        70         80         90        100        110        120 
HIFIEDLREE FVRDYVFPMM RANARYEGDY LLGTSIARPL ISKRLVEIAQ ETGADAIAHG 

       130        140        150        160        170        180 
ATGKGNDQVR FELSAYALDP DIKVIAPWRE WDLTSRTALI AWAEKHQIQV PKDKRGESPF 

       190        200        210        220        230        240 
STDANLLHTS SEGKVLEDPW EETPDYVYSR TVNPEDAPDE PEFITIDFER GDGIALNGEA 

       250        260        270        280        290        300 
MSPANLLTAL NELGRKHGIG RLDLVENRFV GMKSRGMYET PGGEIYARAH RGIEQITLDR 

       310        320        330        340        350        360 
GAAHLKDELM PKYAELIYNG FWFSPEREML QAAIDLSQDK VSGTVRLKLY KGNADVVGRK 

       370        380        390        400 
SPNSLYSEAH VTFEDDAGAY DQSDAEGFIR LNALRLKLLG KRDR

« Hide

References

[1]"Complete genome sequence of Erythrobacter litoralis HTCC2594."
Oh H.M., Giovannoni S.J., Ferriera S., Johnson J., Cho J.C.
J. Bacteriol. 191:2419-2420(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: HTCC2594.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000157 Genomic DNA. Translation: ABC63662.1.
RefSeqYP_458459.1. NC_007722.1.

3D structure databases

HSSPHSSP built from PDB template 1VL2 based on UniProtKB Q9X2A1.
ProteinModelPortalQ2N9H9.
SMRQ2N9H9. Positions 6-404.
ModBaseSearch...

Protein-protein interaction databases

STRING314225.ELI_07850.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABC63662; ABC63662; ELI_07850.
GeneID3870341.
KEGGeli:ELI_07850.
PATRIC21860270. VBIEryLit102657_1559.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0137.
HOGENOMHOG000230093.
KOK01940.
OMAIYNGYWW.
ProtClustDBPRK00509.

Enzyme and pathway databases

BioCycELIT314225:GHLE-1614-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]
PANTHERPTHR11587. PTHR11587. 1 hit.
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_ERYLH
AccessionPrimary (citable) accession number: Q2N9H9
Entry history
Integrated into UniProtKB/Swiss-Prot: February 26, 2008
Last sequence update: February 7, 2006
Last modified: May 1, 2013
This is version 51 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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