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B3QN91 (ASSY_CHLP8) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 42. 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:Cpar_0986
OrganismChlorobaculum parvum (strain NCIB 8327) (Chlorobium vibrioforme subsp. thiosulfatophilum (strain DSM 263 / NCIB 8327)) [Complete proteome] [HAMAP]
Taxonomic identifier517417 [NCBI]
Taxonomic lineageBacteriaChlorobiChlorobiaChlorobialesChlorobiaceaeChlorobaculum

Protein attributes

Sequence length401 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 – 401401Argininosuccinate synthase HAMAP-Rule MF_00005
PRO_1000089027

Regions

Nucleotide binding9 – 179ATP By similarity

Sites

Binding site881Citrulline By similarity
Binding site1181ATP; via amide nitrogen By similarity
Binding site1201Aspartate By similarity
Binding site1241Aspartate By similarity
Binding site1241Citrulline By similarity
Binding site1251Aspartate By similarity
Binding site1281Citrulline By similarity
Binding site1771Citrulline By similarity
Binding site1861Citrulline By similarity
Binding site2621Citrulline By similarity
Binding site2741Citrulline By similarity

Sequences

Sequence LengthMass (Da)Tools
B3QN91 [UniParc].

Last modified September 2, 2008. Version 1.
Checksum: A421E18051FED2EF

FASTA40144,304
        10         20         30         40         50         60 
MSKEKIAVAY SGGLDTSVMI KWLKDKYEGA EIVAVTGNLG QKMEVDNLEP KALATGAASF 

        70         80         90        100        110        120 
HFVDLRKTFV EDCIWKALKA GALYEDVYPL ATALGRPILA KALVDVALAE GCTMLTHGCT 

       130        140        150        160        170        180 
GKGNDQVRFE VTFASLAPHM KVVAPLREWE FTSREQEITY ALEHNIPVSA TKKNPYSIDE 

       190        200        210        220        230        240 
NIWGISIECG VLEDPMVPPP ADAYQITTSP EEAPDKPTVV DIDFVEGIPV ALDGQQMEGL 

       250        260        270        280        290        300 
DLIVKLNELG AMNGVGRLDM IENRVVGIKS REIYEAPAAT ILHFAHRELE RLTLEKSVFQ 

       310        320        330        340        350        360 
YKRNIGQDYA NIIYNGTWFS PMREALDAFV DVTQKPVTGM VRLKLYKGNV TLLGRTSPNS 

       370        380        390        400 
LYNEELATYT EADTFNHKAA EGFIQLYGLG LKTYSEVNLG K 

« Hide

References

[1]"Complete sequence of Chlorobaculum parvum NCIB 8327."
US DOE Joint Genome Institute
Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Bruce D., Goodwin L., Pitluck S., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Zhao F., Li T., Liu Z. expand/collapse author list , Overmann J., Bryant D.A., Richardson P.
Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: NCIB 8327.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001099 Genomic DNA. Translation: ACF11394.1.
RefSeqYP_001998594.1. NC_011027.1.

3D structure databases

ProteinModelPortalB3QN91.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING517417.Cpar_0986.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACF11394; ACF11394; Cpar_0986.
GeneID6419916.
KEGGcpc:Cpar_0986.
PATRIC21365225. VBIChlPar72705_0979.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0137.
HOGENOMHOG000230093.
KOK01940.
OMAYKALAPH.
OrthoDBEOG6K9QCV.

Enzyme and pathway databases

BioCycCPAR517417:GH95-1017-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_CHLP8
AccessionPrimary (citable) accession number: B3QN91
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: September 2, 2008
Last modified: May 14, 2014
This is version 42 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