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A0LE34 (ASSY_MAGSM) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 48. 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:Mmc1_3742
OrganismMagnetococcus sp. (strain MC-1) [Complete proteome] [HAMAP]
Taxonomic identifier156889 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaMagnetococcalesMagnetococcaceaeMagnetococcus

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_1000057040

Regions

Nucleotide binding11 – 199ATP By similarity

Sites

Binding site381ATP; via amide nitrogen and carbonyl oxygen By similarity
Binding site891Citrulline By similarity
Binding site941Citrulline 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 site1801Citrulline By similarity
Binding site1891Citrulline By similarity
Binding site2651Citrulline By similarity
Binding site2771Citrulline By similarity

Sequences

Sequence LengthMass (Da)Tools
A0LE34 [UniParc].

Last modified December 12, 2006. Version 1.
Checksum: 6A1864EC9BCE2E68

FASTA40745,648
        10         20         30         40         50         60 
MSNGIDKVVL AYSGGLDTSI ILKWLQDEYQ CEVVAFCADL GQAEELEPAR AKAEKFGVKE 

        70         80         90        100        110        120 
IYIDDLKEEF VRDFVFPMYR ANTLYEGVYH LGTSIARPLI AKRQIEIANA TGAQAVSHGA 

       130        140        150        160        170        180 
TGKGNDQVRF ELGYYALRPD IRVIAPWREW DLTSRDKLFA YAEKHGIPVP TDKRGEVPYS 

       190        200        210        220        230        240 
MDRNLLHISF EGKALEDPWV EPDEEMFVLS VSPEKAPDQA TYVELTFRQG DLVAIDDQEM 

       250        260        270        280        290        300 
SPATLLAKLN QLGGRNGIGR LDLVENRYVG MKSRGVYETP GGTILGVAHR AMESLTLDRE 

       310        320        330        340        350        360 
VAHMKDELMP RYAKLIYNGY WFSPERAMLQ TMIDASQTFV NGKVRVKLYK GNVVVVGRQS 

       370        380        390        400 
ENSLFDPAIA TFEDDKGAYN QADADGFIKL NALRMRIAAM LRNGPKV 

« Hide

References

[1]"Complete sequence of Magnetococcus sp. MC-1."
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., Kiss H., Goodwin L.A., Brettin T., Bruce D., Han C., Tapia R., Gilna P. expand/collapse author list , Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Richardson P.
Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: MC-1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000471 Genomic DNA. Translation: ABK46227.1.
RefSeqYP_867633.1. NC_008576.1.

3D structure databases

ProteinModelPortalA0LE34.
SMRA0LE34. Positions 7-401.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING156889.Mmc1_3742.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABK46227; ABK46227; Mmc1_3742.
GeneID4483400.
KEGGmgm:Mmc1_3742.
PATRIC22434223. VBIMagSp23654_3829.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0137.
HOGENOMHOG000230093.
KOK01940.
OMAAPPEEAY.
OrthoDBEOG6K9QCV.

Enzyme and pathway databases

BioCycMSP156889:GH36-3797-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_MAGSM
AccessionPrimary (citable) accession number: A0LE34
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: December 12, 2006
Last modified: May 14, 2014
This is version 48 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