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P24532 (ASSY_STRCO) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 116. 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:SCO7036
ORF Names:SC4G1.02
OrganismStreptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145) [Reference proteome] [HAMAP]
Taxonomic identifier100226 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesStreptomycineaeStreptomycetaceaeStreptomyces

Protein attributes

Sequence length481 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

ATP + L-citrulline + L-aspartate = AMP + diphosphate + N(omega)-(L-arginino)succinate. HAMAP-Rule MF_00581

Pathway

Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine from L-ornithine and carbamoyl phosphate: step 2/3. HAMAP-Rule MF_00581

Subunit structure

Homotetramer By similarity. HAMAP-Rule MF_00581

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00581.

Sequence similarities

Belongs to the argininosuccinate synthase family. Type 2 subfamily.

Sequence caution

The sequence BAA00691.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Biological processAmino-acid biosynthesis
Arginine biosynthesis
   Cellular componentCytoplasm
   LigandATP-binding
Nucleotide-binding
   Molecular functionLigase
   Technical termComplete proteome
Reference 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

Initiator methionine11Removed By similarity
Chain2 – 481480Argininosuccinate synthase HAMAP-Rule MF_00581
PRO_0000148708

Regions

Nucleotide binding17 – 259ATP By similarity

Sites

Binding site431ATP; via amide nitrogen and carbonyl oxygen By similarity
Binding site991Citrulline By similarity
Binding site1291ATP; via amide nitrogen By similarity
Binding site1311Aspartate By similarity
Binding site1311ATP By similarity
Binding site1351Aspartate By similarity
Binding site1351Citrulline By similarity
Binding site1361Aspartate By similarity
Binding site1361ATP By similarity
Binding site1391Citrulline By similarity
Binding site1921Citrulline By similarity
Binding site1941ATP By similarity
Binding site2011Citrulline By similarity
Binding site2031Citrulline By similarity
Binding site2801Citrulline By similarity

Experimental info

Sequence conflict75 – 839AALVEEGLA → RRWSRRGWG in BAA00691. Ref.1
Sequence conflict1811L → F in BAA00691. Ref.1
Sequence conflict265 – 2728NAVGGRHG → TPSAAGTA in BAA00691. Ref.1
Sequence conflict3261R → P in BAA00691. Ref.1
Sequence conflict426 – 4283LGL → SRF in BAA00691. Ref.1
Sequence conflict4351A → P in BAA00691. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P24532 [UniParc].

Last modified January 23, 2007. Version 4.
Checksum: 18E7DE4BEABF98B3

FASTA48152,270
        10         20         30         40         50         60 
MSKVLTSLPT GERVGIAFSG GLDTSVAVAW MRDKGAVPCT YTADIGQYDE PDIASVPDRA 

        70         80         90        100        110        120 
KTYGAEVARL VDCRAALVEE GLAALTCGAF HIRSGGRAYF NTTPLGRAVT GTLLVRAMLE 

       130        140        150        160        170        180 
DDVQIWGDGS TFKGNDIERF YRYGLLANPQ LRIYKPWLDA DFVTELGGRK EMSEWLVAHD 

       190        200        210        220        230        240 
LPYRDSTEKA YSTDANIWGA THEAKTLEHL DTGVETVEPI MGVRFWDPSV EIAPEDVTIG 

       250        260        270        280        290        300 
FDQGRPVTIN GKEFASAVDL VMEANAVGGR HGMGMSDQIE NRIIEAKSRG IYEAPGMALL 

       310        320        330        340        350        360 
HAAYERLVNA IHNEDTLAQY HTEGRRLGRL MYEGRWLDPQ SLMIRESLQR WVGSAVTGEV 

       370        380        390        400        410        420 
TLRLRRGEDY SILDTTGPAF SYHPDKLSME RTEDSAFGPV DRIGQLTMRN LDIADSRAKL 

       430        440        450        460        470        480 
EQYAGLGLIG TANPAIGAAQ AAATGLIGAM PEGGAQAIAS RGEVSADDEL LDRAAMESGT 


D 

« Hide

References

« Hide 'large scale' references
[1]"Nucleotide sequence of the gene encoding argininosuccinate synthetase in Streptomyces coelicolor A3(2)."
Ishihara H., Urabe H., Kasama H., Ogawara H.
Nihon Hosenkin Gakkaishi 5:14-17(1991)
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: A3(2) / NRRL B-16638.
[2]"Complete genome sequence of the model actinomycete Streptomyces coelicolor A3(2)."
Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L., Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D., Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A., Fraser A., Goble A. expand/collapse author list , Hidalgo J., Hornsby T., Howarth S., Huang C.-H., Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S., Rabbinowitsch E., Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Saunders D., Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A., Woodward J.R., Barrell B.G., Parkhill J., Hopwood D.A.
Nature 417:141-147(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-471 / A3(2) / M145.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D00799 Genomic DNA. Translation: BAA00691.1. Different initiation.
AL939130 Genomic DNA. Translation: CAC01534.1.
PIRAJSMRC. JQ1057.
RefSeqNP_631098.1. NC_003888.3.

3D structure databases

ProteinModelPortalP24532.
SMRP24532. Positions 2-432.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING100226.SCO7036.

Proteomic databases

PRIDEP24532.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAC01534; CAC01534; CAC01534.
GeneID1102474.
KEGGsco:SCO7036.
PATRIC23743995. VBIStrCoe124346_7140.

Phylogenomic databases

eggNOGCOG0137.
HOGENOMHOG000230094.
KOK01940.
OMAMRNLDIA.
OrthoDBEOG6K9QCV.
PhylomeDBP24532.
ProtClustDBPRK05370.

Enzyme and pathway databases

UniPathwayUPA00068; UER00113.

Family and domain databases

Gene3D1.10.287.400. 1 hit.
3.40.50.620. 1 hit.
3.90.1260.10. 1 hit.
HAMAPMF_00581. Arg_succ_synth_type2.
InterProIPR023437. Arg_succ_synth_type2_subfam.
IPR001518. Arginosuc_synth.
IPR018223. Arginosuc_synth_CS.
IPR024074. AS_cat/multimer_dom_body.
IPR024073. AS_multimer_C_tail.
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_STRCO
AccessionPrimary (citable) accession number: P24532
Secondary accession number(s): Q9FC47
Entry history
Integrated into UniProtKB/Swiss-Prot: March 1, 1992
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 116 of the entry and version 4 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