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Q1IIZ2 (ASSY_KORVE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 51. 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:Acid345_4158
OrganismKoribacter versatilis (strain Ellin345) [Reference proteome] [HAMAP]
Taxonomic identifier204669 [NCBI]
Taxonomic lineageBacteriaAcidobacteriaCandidatus Koribacter

Protein attributes

Sequence length405 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
Reference 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 – 405405Argininosuccinate synthase HAMAP-Rule MF_00005
PRO_0000263903

Regions

Nucleotide binding8 – 169ATP By similarity

Sites

Binding site861Citrulline By similarity
Binding site911Citrulline By similarity
Binding site1161ATP; via amide nitrogen By similarity
Binding site1181Aspartate By similarity
Binding site1221Aspartate By similarity
Binding site1221Citrulline By similarity
Binding site1231Aspartate By similarity
Binding site1261Citrulline By similarity
Binding site1751Citrulline By similarity
Binding site1841Citrulline By similarity
Binding site2601Citrulline By similarity
Binding site2721Citrulline By similarity

Sequences

Sequence LengthMass (Da)Tools
Q1IIZ2 [UniParc].

Last modified June 13, 2006. Version 1.
Checksum: 603714E0DE921FEE

FASTA40544,366
        10         20         30         40         50         60 
MREKIVLAYS GGLDTSIIIP WLKENYSCDV IAMVGDVGQG DDIDAVVAKA HKTGASKVIV 

        70         80         90        100        110        120 
KDLREEFLTQ YVYPAISTGA VYEHKYLLGT SLARPPIAKA QVEVALAEGA TAVSHGCTGK 

       130        140        150        160        170        180 
GNDQVRFEHA FQALAPELKI IAPWREWTLK SREDCLDYAE AHGISVAQSR EKIHSRDRNL 

       190        200        210        220        230        240 
LHVSHEGGEL EDPNNAPLDT TWTWTKSPQE APDRVEEVTI GFEGGVPVSI NGMKLEPLAL 

       250        260        270        280        290        300 
IELLNEIGAR NAIGRIDLVE NRFVGIKSRG CYETPGGSLL LAAHRELEAL CLDRDTLHYK 

       310        320        330        340        350        360 
QEVALKWAEL VYFGLWFTPL RESLDAFVAS TQKNIAGAVK LALYKGNIAV AGRTSPKSLY 

       370        380        390        400 
RPDIASFTMG AGYDQKDAEG FIRILGLPAR SRALIENAGK EKVSK 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000360 Genomic DNA. Translation: ABF43158.1.
RefSeqYP_593232.1. NC_008009.1.

3D structure databases

ProteinModelPortalQ1IIZ2.
SMRQ1IIZ2. Positions 4-396.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING204669.Acid345_4158.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABF43158; ABF43158; Acid345_4158.
GeneID4072117.
KEGGaba:Acid345_4158.
PATRIC31985640. VBICanKor57425_4441.

Phylogenomic databases

eggNOGCOG0137.
HOGENOMHOG000230093.
KOK01940.
OMAPWNEPTK.
OrthoDBEOG6K9QCV.

Enzyme and pathway databases

BioCycKVER204669:GHL8-4195-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_KORVE
AccessionPrimary (citable) accession number: Q1IIZ2
Entry history
Integrated into UniProtKB/Swiss-Prot: December 12, 2006
Last sequence update: June 13, 2006
Last modified: May 14, 2014
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

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways