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Q7UFW4 (ASSY_RHOBA) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 71. 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:RB8293
OrganismRhodopirellula baltica (strain SH1) [Reference proteome] [HAMAP]
Taxonomic identifier243090 [NCBI]
Taxonomic lineageBacteriaPlanctomycetesPlanctomycetiaPlanctomycetalesPlanctomycetaceaeRhodopirellula

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. HAMAP-Rule MF_00005

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00005.

Sequence similarities

Belongs to the argininosuccinate synthase family. Type 1 subfamily.

Sequence caution

The sequence CAD78565.1 differs from that shown. Reason: Erroneous initiation.

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 – 404404Argininosuccinate synthase HAMAP-Rule MF_00005
PRO_0000148631

Regions

Nucleotide binding7 – 159ATP By similarity

Sites

Binding site851Citrulline By similarity
Binding site901Citrulline By similarity
Binding site1151ATP; via amide nitrogen By similarity
Binding site1171Aspartate By similarity
Binding site1211Aspartate By similarity
Binding site1211Citrulline By similarity
Binding site1221Aspartate By similarity
Binding site1251Citrulline By similarity
Binding site1781Citrulline By similarity
Binding site1871Citrulline By similarity
Binding site2641Citrulline By similarity
Binding site2761Citrulline By similarity

Sequences

Sequence LengthMass (Da)Tools
Q7UFW4 [UniParc].

Last modified March 1, 2004. Version 2.
Checksum: 041AB18B6B3B2463

FASTA40444,949
        10         20         30         40         50         60 
MKSCVLAYSG GLDTSVILGW LQDQGYEVHC VYVDLGQPCE DRDAIMEKAR TCGAKSSRLV 

        70         80         90        100        110        120 
DVREELCRDF AFPVLAWQAK YEQIYLLGTS IARPLISKVC LEVAREVGAT AYAHGATGKG 

       130        140        150        160        170        180 
NDQCRFQLAA EALDPNIEMI APWRIKSFRD AFPGRTELIE YCDVKRIPVK ASTAKPYSSD 

       190        200        210        220        230        240 
ENVLHISYEA GKLEELDVNG VELVEFGMGV SPQDAPDKPE EVTIGFESGV PKTLNGKAVN 

       250        260        270        280        290        300 
ALEMVEQLND IAGRNGVGRI DMVENRFVGM KSRGVYESPG MTVLYDALMY VEQLTMDRDL 

       310        320        330        340        350        360 
MHLRDRMAPE VAEMVYYGFW YTPKMDALMS FIETAQRPVT GEVTLQLYKG NIMVSSRTSP 

       370        380        390        400 
NSLYDEEIAT MEGGGSYNQD DAEGFLRIQG LPSRVQGRVS PRKF 

« Hide

References

[1]"Complete genome sequence of the marine planctomycete Pirellula sp. strain 1."
Gloeckner F.O., Kube M., Bauer M., Teeling H., Lombardot T., Ludwig W., Gade D., Beck A., Borzym K., Heitmann K., Rabus R., Schlesner H., Amann R., Reinhardt R.
Proc. Natl. Acad. Sci. U.S.A. 100:8298-8303(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: SH1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BX294147 Genomic DNA. Translation: CAD78565.1. Different initiation.
RefSeqNP_868287.1. NC_005027.1.

3D structure databases

ProteinModelPortalQ7UFW4.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING243090.RB8293.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAD78565; CAD78565; RB8293.
GeneID1795790.
KEGGrba:RB8293.
PATRIC23249461. VBIRhoBal59814_3998.

Phylogenomic databases

eggNOGCOG0137.
HOGENOMHOG000230093.
KOK01940.
OrthoDBEOG6K9QCV.
ProtClustDBCLSK2759366.

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_RHOBA
AccessionPrimary (citable) accession number: Q7UFW4
Entry history
Integrated into UniProtKB/Swiss-Prot: March 1, 2004
Last sequence update: March 1, 2004
Last modified: February 19, 2014
This is version 71 of the entry and version 2 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