Skip Header

Contribute Send feedback
Read comments (?) or add your own

Q0B4C4 (ASSY_BURCM) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 40. 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
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:Bamb_5452
OrganismBurkholderia ambifaria (strain ATCC BAA-244 / AMMD) (Burkholderia cepacia (strain AMMD)) [Complete proteome] [HAMAP]
Taxonomic identifier339670 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Burkholderiaceae › Burkholderia › Burkholderia cepacia complex

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 MF_00581

Pathway

Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine from L-ornithine and carbamoyl phosphate: step 2/3. HAMAP MF_00581

Subunit structure

Homotetramer By similarity. HAMAP MF_00581

Subcellular location

Cytoplasm By similarity HAMAP 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-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

protein homodimerization activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 445445Argininosuccinate synthase HAMAP MF_00581
PRO_1000129741

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
Q0B4C4 [UniParc].

Last modified October 17, 2006. Version 1.
Checksum: 421324120E81576F

FASTA44549,238
        10         20         30         40         50         60 
MSTILESLPT GQKVGIAFSG GLDTSAALHW MKLKGAVPYA YTANLGQPDE DDYDAIPKRA 

        70         80         90        100        110        120 
IEYGAAGARL IDCRAQLVAE GIAALQSGAF HITTAGVTYF NTTPIGRAVT GTMLVAAMKE 

       130        140        150        160        170        180 
DGVNIWGDGS TYKGNDIERF YRYGLLVNPD LKIYKPWLDQ TFIDELGGRA EMSEFMNQAG 

       190        200        210        220        230        240 
FAYKMSAEKA YSTDSNLLGA THEAKDLESL ESGIKIVNPI MGVAFWRDDV KIAAEEVTVR 

       250        260        270        280        290        300 
FEAGQPVALN GVEYKDPVEL LLEANRIGGR HGLGMSDQIE NRIIEAKSRG IYEAPGLALL 

       310        320        330        340        350        360 
YIAYERLVTG IHNEDTIEQY RENGRRLGRL LYQGRWFDPQ AIMLRETAQR WVARAITGEV 

       370        380        390        400        410        420 
KIELRRGNDY SILSTKSPNL TYQPERLSME KVASTFSPRD RIGQLTMRNL DITDTRDKLR 

       430        440 
VYSQVGLLTP GESSALPQIK GDSDK

« Hide

References

[1]"Complete sequence of chromosome 2 of Burkholderia cepacia AMMD."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Pitluck S., Bruce D., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M., Hauser L. expand/collapse author list , Kyrpides N., Kim E., Parke J., Coenye T., Konstantinidis K., Ramette A., Tiedje J., Richardson P.
Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-244 / AMMD.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000441 Genomic DNA. Translation: ABI90999.1.
RefSeqYP_777333.1. NC_008391.1.

3D structure databases

ProteinModelPortalQ0B4C4.
SMRQ0B4C4. Positions 2-445.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ0B4C4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4314341.
GenomeReviewsGene locus Bamb_5452 in contig CP000441_GR.
KEGGbam:Bamb_5452.
NMPDRfig|339670.3.peg.1277.
PATRIC19026895. VBIBurAmb61564_5697.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0137.
HOGENOMHBG289560.
OMAGGRKEMS.
PhylomeDBQ0B4C4.
ProtClustDBPRK05370.

Enzyme and pathway databases

BioCycBAMB339670:BAMB_5452-MONOMER.

Family and domain databases

HAMAPMF_00581. Arg_succ_synth_type2.
[Tree]
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]
Gene3DG3DSA:1.10.287.400. G3DSA:1.10.287.400. 1 hit.
G3DSA: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_BURCM
AccessionPrimary (citable) accession number: Q0B4C4
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: October 17, 2006
Last modified: January 25, 2012
This is version 40 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

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents