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P61522 (ASSY_DESVH) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 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:DVU_1095
OrganismDesulfovibrio vulgaris (strain Hildenborough / ATCC 29579 / NCIMB 8303) [Reference proteome] [HAMAP]
Taxonomic identifier882 [NCBI]
Taxonomic lineageBacteriaProteobacteriaDeltaproteobacteriaDesulfovibrionalesDesulfovibrionaceaeDesulfovibrio

Protein attributes

Sequence length396 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 – 396396Argininosuccinate synthase HAMAP-Rule MF_00005
PRO_0000148593

Regions

Nucleotide binding10 – 189ATP By similarity

Sites

Binding site371ATP; via amide nitrogen and carbonyl oxygen By similarity
Binding site881Citrulline By similarity
Binding site931Citrulline 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 site1761Citrulline By similarity
Binding site1851Citrulline By similarity
Binding site2611Citrulline By similarity
Binding site2731Citrulline By similarity

Sequences

Sequence LengthMass (Da)Tools
P61522 [UniParc].

Last modified May 24, 2004. Version 1.
Checksum: 1C53A441A6984BE3

FASTA39643,911
        10         20         30         40         50         60 
MSGIKKVVLA YSGGLDTSVI LKWLAVTYNC EVVTLTADLG QEEDLDGVDD KAMRTGASRA 

        70         80         90        100        110        120 
YVEDLQEEFA RDFIFPMMRA GAVYEGRYLL GTSIARPLIA KRLVEIARAE GAQAVAHGAT 

       130        140        150        160        170        180 
GKGNDQVRFE LAVNALAPDL RVIAPWREWD LRSRTQLNAF AEEHGIPISS SAKQYSMDRN 

       190        200        210        220        230        240 
MLHCSFEGGE LEDPWNEPGP NSYVMAVPME QAPDEAEYIS IDFEHGNPVA VNGERLSPAA 

       250        260        270        280        290        300 
LVKKLNSIGG RHGIGRLDMV ENRFVGIKSR GVYETPGGTL IHIAHRDLEG ICIDRETMHL 

       310        320        330        340        350        360 
RDAMLPRYAA AIYNGFWFAP EREAMQAMID VSQQRVTGTV RLKLYKGNAW PVGRQSPNTL 

       370        380        390 
YCHDLATFED CATYDHKDAA GFIKLQGLRI RGYKKG 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE017285 Genomic DNA. Translation: AAS95575.1.
RefSeqYP_010316.1. NC_002937.3.

3D structure databases

ProteinModelPortalP61522.
SMRP61522. Positions 6-391.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING882.DVU1095.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAS95575; AAS95575; DVU_1095.
GeneID2794339.
KEGGdvu:DVU1095.
PATRIC32062096. VBIDesVul119526_1033.

Phylogenomic databases

eggNOGCOG0137.
KOK01940.
OMAAPPEEAY.
OrthoDBEOG6K9QCV.
PhylomeDBP61522.

Enzyme and pathway databases

BioCycDVUL882:GJIL-1121-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_DESVH
AccessionPrimary (citable) accession number: P61522
Entry history
Integrated into UniProtKB/Swiss-Prot: May 24, 2004
Last sequence update: May 24, 2004
Last modified: July 9, 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