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A0RJM4 (ASSY_BACAH) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 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:BALH_4210
OrganismBacillus thuringiensis (strain Al Hakam) [Complete proteome] [HAMAP]
Taxonomic identifier412694 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillusBacillus cereus group

Protein attributes

Sequence length401 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.

Sequence caution

The sequence ABK87417.1 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
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 – 401401Argininosuccinate synthase HAMAP-Rule MF_00005
PRO_0000321302

Regions

Nucleotide binding9 – 179ATP 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 site1741Citrulline By similarity
Binding site1831Citrulline By similarity
Binding site2591Citrulline By similarity
Binding site2711Citrulline By similarity

Sequences

Sequence LengthMass (Da)Tools
A0RJM4 [UniParc].

Last modified February 26, 2008. Version 2.
Checksum: D3E21C76DC5D4AD0

FASTA40144,670
        10         20         30         40         50         60 
MEKKKVVLAY SGGLDTSVAI KWLQEKNYDI IALCLDLGEG KDLAFVKEKA LSVGAIKSYM 

        70         80         90        100        110        120 
IDVQEEFANE YALMAMQAHT LYEGKYPLVS ALSRPLIAKK LVEIAEQEGA TAVAHGCTGK 

       130        140        150        160        170        180 
GNDQVRFEVS IQALNPYLEV IAPVREWKWS REEEIAYAKE NNVPIPINLD SPFSIDQNLW 

       190        200        210        220        230        240 
GRSNECGILE DPWAAPPEDA YEMTLALEDT PNKPEFVEIG FEAGVPTTLN GTAYPLSELI 

       250        260        270        280        290        300 
KTLNALAGKH GVGRIDHVEN RLVGIKSREV YECPAAMTLI TAHKELEDLT LVKEVAHFKP 

       310        320        330        340        350        360 
MIEQKITELI YNGLWFSPLK QALNAFLQET QKNVTGTVRV KLFKGHAIVE GRKSEYSLYD 

       370        380        390        400 
EKLATYTAQD EFNHDAAVGF ISLFGLPTKV YSQVNQKKVE A 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000485 Genomic DNA. Translation: ABK87417.1. Different initiation.
RefSeqYP_896924.1. NC_008600.1.

3D structure databases

ProteinModelPortalA0RJM4.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING412694.BALH_4210.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABK87417; ABK87417; BALH_4210.
GeneID4544007.
KEGGbtl:BALH_4210.
PATRIC19001346. VBIBacThu63319_4669.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0137.
HOGENOMHOG000230093.
KOK01940.
OrthoDBEOG6K9QCV.
ProtClustDBPRK00509.

Enzyme and pathway databases

BioCycBTHU412694:GH1W-4112-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_BACAH
AccessionPrimary (citable) accession number: A0RJM4
Entry history
Integrated into UniProtKB/Swiss-Prot: February 26, 2008
Last sequence update: February 26, 2008
Last modified: February 19, 2014
This is version 48 of the entry and version 2 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