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B0RHD5 (ASSY_CLAMS) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 41. 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:CMS1236
OrganismClavibacter michiganensis subsp. sepedonicus (strain ATCC 33113 / DSM 20744 / JCM 9667 / LMG 2889 / C-1) (Corynebacterium sepedonicum) [Complete proteome] [HAMAP]
Taxonomic identifier31964 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesMicrococcineaeMicrobacteriaceaeClavibacter

Protein attributes

Sequence length417 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 – 417417Argininosuccinate synthase HAMAP-Rule MF_00005
PRO_1000073816

Regions

Nucleotide binding8 – 169ATP By similarity

Sites

Binding site871Citrulline By similarity
Binding site1171ATP; via amide nitrogen By similarity
Binding site1191Aspartate By similarity
Binding site1231Aspartate By similarity
Binding site1231Citrulline By similarity
Binding site1241Aspartate By similarity
Binding site1271Citrulline By similarity
Binding site1751Citrulline By similarity
Binding site2591Citrulline By similarity
Binding site2711Citrulline By similarity

Sequences

Sequence LengthMass (Da)Tools
B0RHD5 [UniParc].

Last modified April 8, 2008. Version 1.
Checksum: 72C8C9211BC76BCE

FASTA41745,281
        10         20         30         40         50         60 
MAERVVLAYS GGLDTSVGIG WLKDATGKEV VALAVDVGQG GEDMEVIRQR ALDCGAVEAV 

        70         80         90        100        110        120 
VVDAKDEFAD DYIVPALKAN ALYQKRYPLV SGLSRPLIAK HLARVAHELG ANSVAHGCTG 

       130        140        150        160        170        180 
KGNDQVRFEA AVAALAPDLT SIAPVRDLAL TRDKAIVYAN EHDLPIEQSK KSPYSIDKNV 

       190        200        210        220        230        240 
WGRAVETGFL EDPWNGPIED LYEYTQDPDV LREATEVTIT FEAGVPVAID GIRYSPLRIV 

       250        260        270        280        290        300 
QELNAAAGAH GIGRIDVVED RLVGIKSREV YEAPAAMTLI EAHEELEALT IERDLGRYKR 

       310        320        330        340        350        360 
GVEKDWANLV YDGLWFSGLK RSLDAFIEDS QRHVSGDIRM TLRGGRAVVT GRRSETSLYD 

       370        380        390        400        410 
FDLATYDTGD TFDQSLSKGF IELWSLPSKI SARRDLAVEQ AALAADDATP AAAPAAE 

« Hide

References

[1]"Genome of the actinomycete plant pathogen Clavibacter michiganensis subsp. sepedonicus suggests recent niche adaptation."
Bentley S.D., Corton C., Brown S.E., Barron A., Clark L., Doggett J., Harris B., Ormond D., Quail M.A., May G., Francis D., Knudson D., Parkhill J., Ishimaru C.A.
J. Bacteriol. 190:2150-2160(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 33113 / DSM 20744 / JCM 9667 / LMG 2889 / C-1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AM849034 Genomic DNA. Translation: CAQ01352.1.
RefSeqYP_001709974.1. NC_010407.1.

3D structure databases

ProteinModelPortalB0RHD5.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING31964.CMS_1236.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAQ01352; CAQ01352; CMS1236.
GeneID6158604.
KEGGcms:CMS_1236.
PATRIC21459472. VBIClaMic4666_1298.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0137.
KOK01940.
OMAIYNGYWW.
OrthoDBEOG6K9QCV.
ProtClustDBPRK00509.

Enzyme and pathway databases

BioCycCMIC31964:GJBN-1245-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_CLAMS
AccessionPrimary (citable) accession number: B0RHD5
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: April 8, 2008
Last modified: February 19, 2014
This is version 41 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