Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q0AKJ6 (ASSY_MARMM) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 50. 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:Mmar10_2916
OrganismMaricaulis maris (strain MCS10) [Complete proteome] [HAMAP]
Taxonomic identifier394221 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhodobacteralesHyphomonadaceaeMaricaulis

Protein attributes

Sequence length410 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 – 410410Argininosuccinate synthase HAMAP-Rule MF_00005
PRO_0000263937

Regions

Nucleotide binding13 – 219ATP By similarity

Sites

Binding site401ATP; via amide nitrogen and carbonyl oxygen By similarity
Binding site911Citrulline By similarity
Binding site961Citrulline By similarity
Binding site1211ATP; via amide nitrogen By similarity
Binding site1231Aspartate By similarity
Binding site1271Aspartate By similarity
Binding site1271Citrulline By similarity
Binding site1281Aspartate By similarity
Binding site1311Citrulline By similarity
Binding site1821Citrulline By similarity
Binding site1911Citrulline By similarity
Binding site2671Citrulline By similarity
Binding site2791Citrulline By similarity

Sequences

Sequence LengthMass (Da)Tools
Q0AKJ6 [UniParc].

Last modified October 17, 2006. Version 1.
Checksum: 0BF1B5A74638F954

FASTA41045,524
        10         20         30         40         50         60 
MSAKKPVKKV VLAYSGGLDT SVILKWLQDA YDAEVVTFTA DLGQGEELEP ARRKAEAAGV 

        70         80         90        100        110        120 
SEIFIEDLRE EFVRDFVYPM VRANAVYEGL YLLGTSIARP LIAKRLVEIA HATGADAVAH 

       130        140        150        160        170        180 
GATGKGNDQV RFELGVYALD PDLRVIAPWR EWDLNSRTKL IAYAEENGIE VAKDKRGEAP 

       190        200        210        220        230        240 
FSVDANLWHT SSEGKILEDP AEEAADIVYQ RTDAPEAAPD KPEYVTIAFE AGDAVAVNGE 

       250        260        270        280        290        300 
AMSPATLLTR LNALGRVHGV GRLDLVENRF VGMKSRGIYE TPGGTILMAA HRGIEQITLD 

       310        320        330        340        350        360 
RGACHLKDEL MPRYAKLLYE GFWFSPEREM LQAAIDHSQK DVTGEVRLKL YKGSVNVVGR 

       370        380        390        400        410 
SSEHSLYSLE HVTFEEDIVY DQKDAEGFIR LNALRLQLLA RRKRRLGHNE 

« Hide

References

[1]"Complete sequence of Maricaulis maris MCS10."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Saunders E., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J. expand/collapse author list , Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Viollier P., Stephens C., Richardson P.
Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: MCS10.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000449 Genomic DNA. Translation: ABI67197.1.
RefSeqYP_758135.1. NC_008347.1.

3D structure databases

ProteinModelPortalQ0AKJ6.
SMRQ0AKJ6. Positions 9-404.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING394221.Mmar10_2916.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABI67197; ABI67197; Mmar10_2916.
GeneID4283915.
KEGGmmr:Mmar10_2916.
PATRIC22454058. VBIMarMar77530_2995.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0137.
HOGENOMHOG000230093.
KOK01940.
OMAIYNGYWW.
OrthoDBEOG6K9QCV.

Enzyme and pathway databases

BioCycMMAR394221:GHNB-2969-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_MARMM
AccessionPrimary (citable) accession number: Q0AKJ6
Entry history
Integrated into UniProtKB/Swiss-Prot: December 12, 2006
Last sequence update: October 17, 2006
Last modified: February 19, 2014
This is version 50 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