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Q2YPQ8 (ASSY_BRUA2) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 37. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:BAB1_0071
OrganismBrucella abortus (strain 2308) [Complete proteome] [HAMAP]
Taxonomic identifier359391 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Brucellaceae › Brucella

Protein attributes

Sequence length406 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 – 406406Argininosuccinate synthase HAMAP MF_00005
PRO_0000263908

Regions

Nucleotide binding13 – 219ATP By similarity

Sites

Binding site401ATP; via amide nitrogen and carbonyl oxygen By similarity
Binding site911Citrulline By similarity
Binding site961Citrulline By similarity
Binding site1211ATP; via amide nitrogen By similarity
Binding site1231Aspartate By similarity
Binding site1271Aspartate By similarity
Binding site1271Citrulline By similarity
Binding site1281Aspartate By similarity
Binding site1311Citrulline By similarity
Binding site1821Citrulline By similarity
Binding site1911Citrulline By similarity
Binding site2671Citrulline By similarity
Binding site2791Citrulline By similarity

Sequences

Sequence LengthMass (Da)Tools
Q2YPQ8 [UniParc].

Last modified February 7, 2006. Version 1.
Checksum: 534F07859F1B8F7D

FASTA40645,273
        10         20         30         40         50         60 
MSKWKDVKKV VLAYSGGLDT SIILKWLQTE LGAEVVTFTA DLGQGEELEP ARKKAEMLGI 

        70         80         90        100        110        120 
KEIFIEDVRE EFVRDFVFPM FRANAVYEGV YLLGTSIARP LISKHLIDIA KKTGADAIAH 

       130        140        150        160        170        180 
GATGKGNDQV RFELSAYALN PDIKIIAPWR DWSFKSRTQL LEFAEQHQIP VAKDKKGEAP 

       190        200        210        220        230        240 
FSVDANLLHS SSEGKVLEDP SQEAPEYVHM RTISPETAPD KATIIKIGFE KGDAVSINGE 

       250        260        270        280        290        300 
RLSPATLLAK LNDYGRDNGI GRLDLVENRF VGMKSRGVYE TPGGTILLAA HRAIESITLD 

       310        320        330        340        350        360 
RGAAHLKDEL MPRYAELIYY GFWFSPEREM LQAAIDHSQR HVEGEVTLKL YKGNVMVIGR 

       370        380        390        400 
ESAKSLYSDK LVTFEDDQGA YDQKDAAGFI KLNALRLRTL AARDRK

« Hide

References

[1]"Whole-genome analyses of speciation events in pathogenic Brucellae."
Chain P.S., Comerci D.J., Tolmasky M.E., Larimer F.W., Malfatti S.A., Vergez L.M., Aguero F., Land M.L., Ugalde R.A., Garcia E.
Infect. Immun. 73:8353-8361(2005) [PubMed: 16299333] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 2308.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AM040264 Genomic DNA. Translation: CAJ10027.1.
RefSeqYP_413571.1. NC_007618.1.

3D structure databases

HSSPHSSP built from PDB template 1VL2 based on UniProtKB Q9X2A1.
ProteinModelPortalQ2YPQ8.
SMRQ2YPQ8. Positions 9-405.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ2YPQ8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3786883.
GenomeReviewsGene locus BAB1_0071 in contig AM040264_GR.
KEGGbmf:BAB1_0071.
PATRIC17842965. VBIBruMel86222_0075.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0137.
HOGENOMHBG335267.
OMARANAIYE.
ProtClustDBPRK00509.

Enzyme and pathway databases

BioCycBMEL359391:BAB1_0071-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_BRUA2
AccessionPrimary (citable) accession number: Q2YPQ8
Entry history
Integrated into UniProtKB/Swiss-Prot: December 12, 2006
Last sequence update: February 7, 2006
Last modified: January 25, 2012
This is version 37 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Brucella abortus strain 2308

Brucella abortus (strain 2308): entries and gene names

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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