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

C4Z9C9 (ASSY_EUBR3) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 36. 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:EUBREC_1607
OrganismEubacterium rectale (strain ATCC 33656 / VPI 0990) [Complete proteome] [HAMAP]
Taxonomic identifier515619 [NCBI]
Taxonomic lineageBacteriaFirmicutesClostridiaClostridialesEubacteriaceaeEubacterium

Protein attributes

Sequence length408 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 – 408408Argininosuccinate synthase HAMAP-Rule MF_00005
PRO_1000201682

Regions

Nucleotide binding8 – 169ATP By similarity

Sites

Binding site861Citrulline By similarity
Binding site1161ATP; via amide nitrogen By similarity
Binding site1181Aspartate By similarity
Binding site1221Aspartate By similarity
Binding site1221Citrulline By similarity
Binding site1231Aspartate By similarity
Binding site1261Citrulline By similarity
Binding site1771Citrulline By similarity
Binding site1861Citrulline By similarity
Binding site2631Citrulline By similarity
Binding site2751Citrulline By similarity

Sequences

Sequence LengthMass (Da)Tools
C4Z9C9 [UniParc].

Last modified July 28, 2009. Version 1.
Checksum: 720433B20FA92A8F

FASTA40845,484
        10         20         30         40         50         60 
MKDKVVLAYS GGLDTTAIIP WLKETYDYDV ICCCINCGQG EELDGLDERA KLSGASKLYI 

        70         80         90        100        110        120 
EDICDEFSED YIVPCVQAGA VYEHKYLLGT AMARPGIAKK LVEIARKEGA VAICHGATGK 

       130        140        150        160        170        180 
GNDQIRFELG IKALAPDIKV IAPWRQDNWK MDSREAEIEY CKAHGIDLPF GTDSSYSRDR 

       190        200        210        220        230        240 
NLWHISHEGL ELEDPSQEPN YDHLLVLSVT PEHAPDEGEY VTMTFEKGVP TSVNGKKMKV 

       250        260        270        280        290        300 
ADIIRELNRL GGKHGIGIID IVENRVVGMK SRGVYETPGG TILMEAHDQL EELCLDRATM 

       310        320        330        340        350        360 
EVKKEMGNKL AQVVYEGKWF TPLREAIQAF VESTQEYVTG EVKFKLYKGN IIKAGTTSPY 

       370        380        390        400 
SLYSESLASF TTGDLYDHHD ADGFITLFGL PLKVRAMKLL ELENKKNN 

« Hide

References

[1]"Characterizing a model human gut microbiota composed of members of its two dominant bacterial phyla."
Mahowald M.A., Rey F.E., Seedorf H., Turnbaugh P.J., Fulton R.S., Wollam A., Shah N., Wang C., Magrini V., Wilson R.K., Cantarel B.L., Coutinho P.M., Henrissat B., Crock L.W., Russell A., Verberkmoes N.C., Hettich R.L., Gordon J.I.
Proc. Natl. Acad. Sci. U.S.A. 106:5859-5864(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 33656 / VPI 0990.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001107 Genomic DNA. Translation: ACR75351.1.
RefSeqYP_002937485.1. NC_012781.1.

3D structure databases

ProteinModelPortalC4Z9C9.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING515619.EUBREC_1607.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACR75351; ACR75351; EUBREC_1607.
GeneID7964683.
KEGGere:EUBREC_1607.
PATRIC21871421. VBIEubRec107985_1359.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0137.
HOGENOMHOG000230093.
KOK01940.
OMAAPPEEAY.
OrthoDBEOG6K9QCV.

Enzyme and pathway databases

BioCycEREC515619:GHMX-1600-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_EUBR3
AccessionPrimary (citable) accession number: C4Z9C9
Entry history
Integrated into UniProtKB/Swiss-Prot: September 22, 2009
Last sequence update: July 28, 2009
Last modified: May 14, 2014
This is version 36 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