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P61521 (ASSY_CORDI) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 72. 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:DIP1173
OrganismCorynebacterium diphtheriae (strain ATCC 700971 / NCTC 13129 / Biotype gravis) [Complete proteome] [HAMAP]
Taxonomic identifier257309 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeCorynebacteriaceaeCorynebacterium

Protein attributes

Sequence length399 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 – 399399Argininosuccinate synthase HAMAP-Rule MF_00005
PRO_0000148588

Regions

Nucleotide binding8 – 169ATP By similarity

Sites

Binding site871Citrulline By similarity
Binding site1171ATP; via amide nitrogen By similarity
Binding site1191Aspartate By similarity
Binding site1231Aspartate By similarity
Binding site1231Citrulline By similarity
Binding site1241Aspartate By similarity
Binding site1271Citrulline By similarity
Binding site1751Citrulline By similarity
Binding site2591Citrulline By similarity
Binding site2711Citrulline By similarity

Sequences

Sequence LengthMass (Da)Tools
P61521 [UniParc].

Last modified May 24, 2004. Version 1.
Checksum: B83FD37285891D64

FASTA39944,082
        10         20         30         40         50         60 
MTNRVVLAYS GGLDTSVAIP YLAKMTGGEV VAVSLDLGQG GEDMESVRQR ALDCGAVESI 

        70         80         90        100        110        120 
VIDAKDEFAN DYCLPTIKAN GMYMKQYPLV SAISRPLIVK HLVEAAKKHG GTHVSHGCTG 

       130        140        150        160        170        180 
KGNDQVRFEV GFRNLAPELQ IIAPARDYAW TRDKAIAFAE EINLPIEQSK KSPFSIDQNV 

       190        200        210        220        230        240 
WGRAVETGFL EDLWNPPTKD LYSYTEDPAL GNAPDEIIIS FKAGVPVAID GRPVTVLEAI 

       250        260        270        280        290        300 
EEMNRRAGAQ GIGRLDMVED RLVGIKSREV YEAPGAIALI TAHQAMEDVT IERELARYKR 

       310        320        330        340        350        360 
GIDARWSEEV YDGLWYAPLK RSLDAFIENT QEHVTGDIRM VMHAGKCTVN GRRSEHSLYD 

       370        380        390 
FDLATYDTGD TFDQTLAKGF VELHGLSSKI SNKRDREAQ 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BX248357 Genomic DNA. Translation: CAE49693.1.
RefSeqNP_939530.1. NC_002935.2.

3D structure databases

ProteinModelPortalP61521.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING257309.DIP1173.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAE49693; CAE49693; DIP1173.
GeneID2649725.
KEGGcdi:DIP1173.
PATRIC21483535. VBICorDip47633_1156.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

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_CORDI
AccessionPrimary (citable) accession number: P61521
Entry history
Integrated into UniProtKB/Swiss-Prot: May 24, 2004
Last sequence update: May 24, 2004
Last modified: February 19, 2014
This is version 72 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