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

Q12SM7 (ASSY_SHEDO) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 53. 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:Sden_0253
OrganismShewanella denitrificans (strain OS217 / ATCC BAA-1090 / DSM 15013) [Complete proteome] [HAMAP]
Taxonomic identifier318161 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesShewanellaceaeShewanella

Protein attributes

Sequence length407 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 – 407407Argininosuccinate synthase HAMAP-Rule MF_00005
PRO_0000263969

Regions

Nucleotide binding16 – 249ATP By similarity

Sites

Binding site441ATP; via amide nitrogen and carbonyl oxygen By similarity
Binding site961Citrulline By similarity
Binding site1011Citrulline By similarity
Binding site1261ATP; via amide nitrogen By similarity
Binding site1281Aspartate By similarity
Binding site1321Aspartate By similarity
Binding site1321Citrulline By similarity
Binding site1331Aspartate By similarity
Binding site1361Citrulline By similarity
Binding site1851Citrulline By similarity
Binding site1941Citrulline By similarity
Binding site2701Citrulline By similarity
Binding site2821Citrulline By similarity

Sequences

Sequence LengthMass (Da)Tools
Q12SM7 [UniParc].

Last modified August 22, 2006. Version 1.
Checksum: 3E1A76B912BBFAE8

FASTA40744,615
        10         20         30         40         50         60 
MSSTVKKTGV KKVVLAYSGG LDTSAIIPWL KETYDDCEIV AFCADVGQGE EELVGLTEKA 

        70         80         90        100        110        120 
LASGASECHI VDLKEEFVKD YIYPTIATGA IYEGTYLLGT SMARPIIAKA QVEVARKVGA 

       130        140        150        160        170        180 
DALCHGCTGK GNDQVRFEGC FAALAPDLKV IAPWREWEMR SREDLLAYLA ARDIQTSASA 

       190        200        210        220        230        240 
TKIYSRDANA WHISHEGGEL EDPWNEPSKG VWTLTVAPED APDEAEYVAL SIKHGRVTHV 

       250        260        270        280        290        300 
NEQVLSPYNA LMKLNDIASK HGVGRIDITE NRLVGMKSRG CYETPGGTVM FAGLRAIEEL 

       310        320        330        340        350        360 
VLDKTSRTWR EQVAAQMAHL VYDGRWFTPL CNSLLAASES LAEAVNGDVV IKLYKGQATA 

       370        380        390        400 
VKKRSPNSLY SESFATFGED DVYDQKHAEG FIRLYSLASR IRAMNSN 

« Hide

References

[1]"Complete sequence of Shewanella denitrificans OS217."
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., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Kiss H., Schmutz J. expand/collapse author list , Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A., Richardson P.
Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: OS217 / ATCC BAA-1090 / DSM 15013.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000302 Genomic DNA. Translation: ABE53549.1.
RefSeqYP_561272.1. NC_007954.1.

3D structure databases

ProteinModelPortalQ12SM7.
SMRQ12SM7. Positions 12-405.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING318161.Sden_0253.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABE53549; ABE53549; Sden_0253.
GeneID4020364.
KEGGsdn:Sden_0253.
PATRIC23486114. VBISheDen79529_0273.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0137.
HOGENOMHOG000230093.
KOK01940.
OMAPWNEPTK.
OrthoDBEOG6K9QCV.

Enzyme and pathway databases

BioCycSDEN318161:GHKQ-266-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_SHEDO
AccessionPrimary (citable) accession number: Q12SM7
Entry history
Integrated into UniProtKB/Swiss-Prot: December 12, 2006
Last sequence update: August 22, 2006
Last modified: May 14, 2014
This is version 53 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