Skip Header

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

A9IQ90 (ASSY_BORPD) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 31. 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:Bpet2689
OrganismBordetella petrii (strain ATCC BAA-461 / DSM 12804 / CCUG 43448) [Complete proteome] [HAMAP]
Taxonomic identifier340100 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Alcaligenaceae › Bordetella

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_1000129733

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
A9IQ90 [UniParc].

Last modified February 5, 2008. Version 1.
Checksum: D4BE6B7A865372AE

FASTA44549,347
        10         20         30         40         50         60 
MTTILPNLPV GQKVGIAFSG GLDTSAALLW MRNKGAIPYA YTANLGQPDE DDYDAIPRRA 

        70         80         90        100        110        120 
MEYGAENARL IDCRAQLVAE GIAALQAGAF HVSTAGITYF NTTPIGRAVT GTMLVAAMKE 

       130        140        150        160        170        180 
DGVNIWGDGS TYKGNDIERF YRYGLLTNPD LKIYKPWLDQ LFIDELGGRA EMSEYMRQAG 

       190        200        210        220        230        240 
FDYKMSAEKA YSTDSNMLGA THEAKDLEQL NSGIRIVKPI MGVAFWRDDV AVKAEEVSVR 

       250        260        270        280        290        300 
FEEGQPVALN GVEYADPVEL MLEANRIGGR HGLGMSDQIE NRIIEAKSRG IYEAPGLALL 

       310        320        330        340        350        360 
FIAYERLVTG IHNEDTIEQY RESGRKLGRL LYQGRWFDPQ AIMLRETAQR WVARAVTGEV 

       370        380        390        400        410        420 
TLELRRGNDY SLLNTESPNL TYAPERLSME KVENAPFTPA DRIGQLTMRN LDITDTRDKL 

       430        440 
FTYVKTGLLA SSGGAALPQL KDAKK

« Hide

References

[1]"The missing link: Bordetella petrii is endowed with both the metabolic versatility of environmental bacteria and virulence traits of pathogenic Bordetellae."
Gross R., Guzman C.A., Sebaihia M., Martin dos Santos V.A.P., Pieper D.H., Koebnik R., Lechner M., Bartels D., Buhrmester J., Choudhuri J.V., Ebensen T., Gaigalat L., Herrmann S., Khachane A.N., Larisch C., Link S., Linke B., Meyer F. expand/collapse author list , Mormann S., Nakunst D., Rueckert C., Schneiker-Bekel S., Schulze K., Voerholter F.-J., Yevsa T., Engle J.T., Goldman W.E., Puehler A., Goebel U.B., Goesmann A., Bloecker H., Kaiser O., Martinez-Arias R.
BMC Genomics 9:449-449(2008) [PubMed: 18826580] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-461 / DSM 12804 / CCUG 43448.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AM902716 Genomic DNA. Translation: CAP43031.1.
RefSeqYP_001631299.1. NC_010170.1.

3D structure databases

ProteinModelPortalA9IQ90.
SMRA9IQ90. Positions 2-442.
ModBaseSearch...

Protein-protein interaction databases

STRINGA9IQ90.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5817562.
GenomeReviewsGene locus Bpet2689 in contig AM902716_GR.
KEGGbpt:Bpet2689.
PATRIC21166874. VBIBorPet31633_2698.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG289560.
OMAGGRKEMS.
ProtClustDBPRK05370.

Enzyme and pathway databases

BioCycBPET94624:BPET2689-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_BORPD
AccessionPrimary (citable) accession number: A9IQ90
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: February 5, 2008
Last modified: January 25, 2012
This is version 31 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