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A8G7L2 (ASSY_PROM2) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 43. 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:P9215_19801
OrganismProchlorococcus marinus (strain MIT 9215) [Complete proteome] [HAMAP]
Taxonomic identifier93060 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaProchloralesProchlorococcaceaeProchlorococcus

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.

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 – 404404Argininosuccinate synthase HAMAP-Rule MF_00005
PRO_1000057041

Regions

Nucleotide binding10 – 189ATP By similarity

Sites

Binding site381ATP; via amide nitrogen and carbonyl oxygen By similarity
Binding site891Citrulline By similarity
Binding site1191ATP; via amide nitrogen By similarity
Binding site1211Aspartate By similarity
Binding site1251Aspartate By similarity
Binding site1251Citrulline By similarity
Binding site1261Aspartate By similarity
Binding site1291Citrulline By similarity
Binding site1771Citrulline By similarity
Binding site1861Citrulline By similarity
Binding site2621Citrulline By similarity
Binding site2741Citrulline By similarity

Sequences

Sequence LengthMass (Da)Tools
A8G7L2 [UniParc].

Last modified November 13, 2007. Version 1.
Checksum: 4CEB46AFE8989F87

FASTA40444,712
        10         20         30         40         50         60 
MQQVKKVVLA YSGGVDTSVC IPYLKKEYGI SEVITFVADL GQGEDLELIR QKALNSGASQ 

        70         80         90        100        110        120 
SIVGNLVNSF VERYAFPAIR ANALYLDKYP LSTALARPLI AENLVNIARE FSADAVAHGC 

       130        140        150        160        170        180 
TGKGNDQVRF DLAINALGPD LKIITPAREW NMSREEAIIY GEKFGIPAPV SKKSPYSIDV 

       190        200        210        220        230        240 
NLLGRSIEAG ILEDPMQEAP EDIFAMTSSI DNSPDSPLDI EIIFKNGFPV GINDEFLTPV 

       250        260        270        280        290        300 
EIIKKANVLA GEHGYGRIDM IEDRVVGIKS REIYETPGLL LLIKAHKELE SITLNPDIVD 

       310        320        330        340        350        360 
FKGIVEKKWG QIVYQGFWFG PLKDSLDAFI SSTQTSVNGR VKIRLYKGNA IVIGRMSENN 

       370        380        390        400 
SLYRDDLATY SKDDVFKHSL AEGFIYMWGM SNKIWAELNS KTTD 

« Hide

References

[1]"Patterns and implications of gene gain and loss in the evolution of Prochlorococcus."
Kettler G.C., Martiny A.C., Huang K., Zucker J., Coleman M.L., Rodrigue S., Chen F., Lapidus A., Ferriera S., Johnson J., Steglich C., Church G.M., Richardson P., Chisholm S.W.
PLoS Genet. 3:2515-2528(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: MIT 9215.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000825 Genomic DNA. Translation: ABV51593.1.
RefSeqYP_001485179.1. NC_009840.1.

3D structure databases

ProteinModelPortalA8G7L2.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING93060.P9215_19801.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABV51593; ABV51593; P9215_19801.
GeneID5615027.
KEGGpmh:P9215_19801.
PATRIC22993570. VBIProMar119824_2037.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCycPMAR93060:GI08-2045-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_PROM2
AccessionPrimary (citable) accession number: A8G7L2
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: November 13, 2007
Last modified: February 19, 2014
This is version 43 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