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P61520 (ASSY_BACC1) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 57. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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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:BCE_4765
OrganismBacillus cereus (strain ATCC 10987) [Complete proteome] [HAMAP]
Taxonomic identifier222523 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus › Bacillus 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 MF_00005

Pathway

Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine from L-ornithine and carbamoyl phosphate: step 2/3. HAMAP MF_00005

Subunit structure

Homotetramer By similarity. HAMAP MF_00005

Subcellular location

Cytoplasm By similarity HAMAP 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-KW

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

argininosuccinate synthase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 401401Argininosuccinate synthase HAMAP MF_00005
PRO_0000148565

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
P61520 [UniParc].

Last modified May 24, 2004. Version 1.
Checksum: 021E41D096DB91BF

FASTA40144,701
        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 NDVPIPINLD 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 QKNVTGMVRV KLFKGHAIVE GRKSEYSLYD 

       370        380        390        400 
EKLATYTAQD EFNHDAAVGF ISLFGLPTKV YSQVNQKKVE A

« Hide

References

[1]"The genome sequence of Bacillus cereus ATCC 10987 reveals metabolic adaptations and a large plasmid related to Bacillus anthracis pXO1."
Rasko D.A., Ravel J., Oekstad O.A., Helgason E., Cer R.Z., Jiang L., Shores K.A., Fouts D.E., Tourasse N.J., Angiuoli S.V., Kolonay J.F., Nelson W.C., Kolstoe A.-B., Fraser C.M., Read T.D.
Nucleic Acids Res. 32:977-988(2004) [PubMed: 14960714] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 10987.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE017194 Genomic DNA. Translation: AAS43666.1.
RefSeqNP_981058.1. NC_003909.8.

3D structure databases

ProteinModelPortalP61520.
ModBaseSearch...

Protein-protein interaction databases

STRINGP61520.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBBACT00000028377; EBBACP00000027727; EBBACG00000028368.
GeneID2751019.
GenomeReviewsGene locus BCE_4765 in contig AE017194_GR.
KEGGbca:BCE_4765.
NMPDRfig|222523.1.peg.4730.
PATRIC18858142. VBIBacCer118379_4566.
TIGRBCE_4765.

Phylogenomic databases

eggNOGCOG0137.
GeneTreeEBGT00050000002857.
HOGENOMHBG335267.
OMALATYDTG.
ProtClustDBPRK00509.

Enzyme and pathway databases

BioCycBCER405917:BCE_4765-MONOMER.

Family and domain databases

HAMAPMF_00005. Arg_succ_synth_type1.
[Tree]
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]
Gene3DG3DSA:3.90.1260.10. G3DSA:3.90.1260.10. 1 hit.
G3DSA:3.40.50.620. Rossmann-like_a/b/a_fold. 1 hit.
KOK01940.
PANTHERPTHR11587. Arginosuc_synth. 1 hit.
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_BACC1
AccessionPrimary (citable) accession number: P61520
Entry history
Integrated into UniProtKB/Swiss-Prot: May 24, 2004
Last sequence update: May 24, 2004
Last modified: January 25, 2012
This is version 57 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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