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

C1A3S5 (ASSY_GEMAT) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 38. 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:GAU_0110
OrganismGemmatimonas aurantiaca (strain T-27 / DSM 14586 / JCM 11422 / NBRC 100505) [Complete proteome] [HAMAP]
Taxonomic identifier379066 [NCBI]
Taxonomic lineageBacteriaGemmatimonadetesGemmatimonadalesGemmatimonadaceaeGemmatimonas

Protein attributes

Sequence length445 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_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.

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 – 445445Argininosuccinate synthase HAMAP-Rule MF_00581
PRO_1000212130

Regions

Nucleotide binding17 – 259ATP By similarity

Sites

Binding site431ATP 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

Sequences

Sequence LengthMass (Da)Tools
C1A3S5 [UniParc].

Last modified May 26, 2009. Version 1.
Checksum: 8AEBDCB678E6C6B4

FASTA44549,602
        10         20         30         40         50         60 
MANILQRLPI GEKVGIAFSG GLDTSAALHW MRAKGAVPYA YTANLGQPDE SDYEEIPRKA 

        70         80         90        100        110        120 
MAYGAEKARL VECRSQLVAE GLAALQCGAF HVSTAGQTYF NTTPLGRAVT GTMLVAAMRE 

       130        140        150        160        170        180 
DDVNIWGDGS TFKGNDIERF YRYGLLTNPN LRVYKPWLDQ QFIDELGGRT EMAEYLIASG 

       190        200        210        220        230        240 
FEYKMSVEKA YSTDSNILGA THEAKDLEFL NKGMHIVHPI MGVAFWRDEV KIEKETVTIR 

       250        260        270        280        290        300 
FEEGYPVSIN GREFGSALEL FTEANVIGGR HGLGMSDQIE NRIIEAKSRG IYEAPGLALL 

       310        320        330        340        350        360 
FIAYERLVTG IHNEDTIEQY RINGKKLGRL LYQGRWLDPQ SLMLRESAQR WVAKAVTGEV 

       370        380        390        400        410        420 
TVELRRGNDY SIMDTSSANL TYKPERLTME KGQEYFSPLD RIGQLTMRNL DIIDTRDKLS 

       430        440 
IYVSAGLLRG SSTTGVPQLP SGSDE 

« Hide

References

[1]"Complete genome sequence of Gemmatimonas aurantiaca T-27 that represents a novel phylum Gemmatimonadetes."
Takasaki K., Ichikawa N., Miura H., Matsushita S., Watanabe Y., Oguchi A., Ankai A., Yashiro I., Takahashi M., Terui Y., Fukui S., Yokoyama H., Tanikawa S., Hanada S., Kamagata Y., Fujita N.
Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: T-27 / DSM 14586 / JCM 11422 / NBRC 100505.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AP009153 Genomic DNA. Translation: BAH37152.1.
RefSeqYP_002759622.1. NC_012489.1.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING379066.GAU_0110.

Proteomic databases

PRIDEC1A3S5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAH37152; BAH37152; GAU_0110.
GeneID7705143.
KEGGgau:GAU_0110.
PATRIC21952972. VBIGemAur55831_0111.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0137.
HOGENOMHOG000230094.
KOK01940.
OrthoDBEOG6K9QCV.

Enzyme and pathway databases

BioCycGAUR379066:GI3W-111-MONOMER.
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_GEMAT
AccessionPrimary (citable) accession number: C1A3S5
Entry history
Integrated into UniProtKB/Swiss-Prot: September 22, 2009
Last sequence update: May 26, 2009
Last modified: May 14, 2014
This is version 38 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