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Reviewed, UniProtKB/Swiss-Prot A9IL50 (ASSY_BART1)

Last modified November 3, 2009. Version 12. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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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: BT_0022
OrganismBartonella tribocorum (strain CIP 105476 / IBS 506) [Complete proteome] [HAMAP]
Taxonomic identifier382640 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Bartonellaceae › Bartonella

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Protein attributes

Sequence length411 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

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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.

Subcellular location

Cytoplasm Probable.

Sequence similarities

Belongs to the argininosuccinate synthase family. Type 1 subfamily.

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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: HAMAP

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionATP binding

Inferred from electronic annotation. Source: HAMAP

argininosuccinate synthase activity

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 411411Argininosuccinate synthase HAMAP MF_00005
PRO_1000073812

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

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Sequences

Sequence LengthMass (Da)Tools
A9IL50-1 [UniParc].

Last modified February 5, 2008. Version 1.
Checksum: 4283A55BE98C3686

FASTA41146,247
        10         20         30         40         50         60 
MKKWQNIRKV VLAYSGGLDT SIILKWLQST LDAEVVTFTA DLGQGEELEL ARRKAEMLGV 

        70         80         90        100        110        120 
KEIYIEDLRE EFVRDFVFPM FRANTVYEGA YLLGTSIARP LISKRLIEIA KETGADAIAH 

       130        140        150        160        170        180 
GATGKGNDQV RFELSAYALN PDIKIIAPWR DWDFKSRTDL FEFARMHQIP VEKDQQGEAP 

       190        200        210        220        230        240 
FSVDANLLHS SSEGKILENP ALPAPEYVHI RTLSPEDAPD QATRITLGFK KGDAVSINGK 

       250        260        270        280        290        300 
NLSPATLLAE LNRYGRDNGI GRLDLVENRF VGMKSRGFYE TPGGTILLAA HRAIESLTLD 

       310        320        330        340        350        360 
RGAAHLKDEL MPRYAELIYY GFWFSPERKM LQAAIDLSQE HVEGEVTLKL YKGNVIVEGR 

       370        380        390        400        410 
QSKKSLYSSE LVTFEDDQGA YDQRDATGFI KLNALRLRTL ARRCQGNQEK K

« Hide

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References

[1]"Genomic analysis of Bartonella identifies type IV secretion systems as host adaptability factors."
Saenz H.L., Engel P., Stoeckli M.C., Lanz C., Raddatz G., Vayssier-Taussat M., Birtles R., Schuster S.C., Dehio C.
Nat. Genet. 39:1469-1476(2007) [PubMed: 18037886] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

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Cross-references

Sequence databases

AM260525 Genomic DNA. Translation: CAK00526.1.
RefSeqYP_001608521.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID5829894.
GenomeReviewsGene locus BT_0022 in contig AM260525_GR.

Organism-specific databases

CMRSearch...

Phylogenomic databases

OMAYVFPMFR.

Family and domain databases

HAMAPMF_00005.
[Tree]
InterProIPR001518. Arginosuc_synth.
IPR018223. Arginosuc_synth_CS.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view]
Gene3DG3DSA:3.40.50.620. Rossmann-like_a/b/a_fold. 1 hit.
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...

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Entry information

Entry nameASSY_BART1
AccessionPrimary (citable) accession number: A9IL50
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: February 5, 2008
Last modified: November 3, 2009
This is version 12 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents