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Q05FN6 (ASSY_CARRP) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 31. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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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:CRP_104
OrganismCarsonella ruddii (strain PV) [Complete proteome] [HAMAP]
Taxonomic identifier387662 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Candidatus Carsonella

Protein attributes

Sequence length393 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 MF_00005

Pathway

Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine from L-ornithine and carbamoyl phosphate: step 2/3. HAMAP MF_00005

Subunit structure

Homotetramer By similarity. HAMAP MF_00005

Subcellular location

Cytoplasm By similarity HAMAP 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-KW

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

argininosuccinate synthase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 393393Argininosuccinate synthase HAMAP MF_00005
PRO_1000000390

Regions

Nucleotide binding10 – 189ATP By similarity

Sites

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

Sequences

Sequence LengthMass (Da)Tools
Q05FN6 [UniParc].

Last modified November 14, 2006. Version 1.
Checksum: 1FDB21D282CD12F7

FASTA39345,320
        10         20         30         40         50         60 
MKIKEKIVLA YSGGLDTSVI VKWLQNELNF EVITFTADLG QGEEILLAKK KAKLLNIKNI 

        70         80         90        100        110        120 
FVKNLKKEFI KNFVFPFLRS SSTYENNYLL GTAIARPLIV KELMKISYYL NTNYVSHGAT 

       130        140        150        160        170        180 
GKGNDQIRFE LGFKYFNPKI KIIAPWRIWN LNSRNSLLNF CIKNNIKFDS KTKKYSIDKN 

       190        200        210        220        230        240 
LFHNSYEGGN LDNINYEPDE PMWEHTLSNY NSLDYPIYIS LTFKNGDPIK INNKNYNVEE 

       250        260        270        280        290        300 
LFLKLNNLGS IAGIGRLDII ENRLIGIKSR GCYESPGASI IMYARKKLES LILDKEIYSF 

       310        320        330        340        350        360 
KEEIALKYSK LVYNGYWWSP ERILLQKIID YTQTSINGII KLKIFKGQIN IASINSINSL 

       370        380        390 
FNSKNSSFDE ISNLFNQSDS SGFINIKSLR LII

« Hide

References

[1]"The 160-kilobase genome of the bacterial endosymbiont Carsonella."
Nakabachi A., Yamashita A., Toh H., Ishikawa H., Dunbar H.E., Moran N.A., Hattori M.
Science 314:267-267(2006) [PubMed: 17038615] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: PV.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AP009180 Genomic DNA. Translation: BAF35135.1.
RefSeqYP_802501.1. NC_008512.1.

3D structure databases

ProteinModelPortalQ05FN6.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ05FN6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4414925.
GenomeReviewsGene locus CRP_104 in contig AP009180_GR.
KEGGcrp:CRP_104.
PATRIC31966500. VBICanCar121052_0103.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG335267.
OMARANAIYE.

Enzyme and pathway databases

BioCycCCAR387662:CRP_104-MONOMER.

Family and domain databases

HAMAPMF_00005. Arg_succ_synth_type1.
[Tree]
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]
Gene3DG3DSA:3.90.1260.10. G3DSA:3.90.1260.10. 1 hit.
G3DSA:3.40.50.620. Rossmann-like_a/b/a_fold. 1 hit.
KOK01940.
PANTHERPTHR11587. Arginosuc_synth. 1 hit.
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_CARRP
AccessionPrimary (citable) accession number: Q05FN6
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: November 14, 2006
Last modified: January 25, 2012
This is version 31 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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