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A9R622 (ASSY_YERPG) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 44. 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:YpAngola_A1695
OrganismYersinia pestis bv. Antiqua (strain Angola) [Complete proteome] [HAMAP]
Taxonomic identifier349746 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Yersinia ›

Protein attributes

Sequence length455 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-Rule MF_00581

Pathway

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

Subunit structure

Homotetramer By similarity.

Subcellular location

Cytoplasm By similarity.

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: 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...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 455455Argininosuccinate synthase HAMAP-Rule MF_00581
PRO_1000129772

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
A9R622 [UniParc].

Last modified February 5, 2008. Version 1.
Checksum: 7B1A2B828CDAE057

FASTA45551,009
        10         20         30         40         50         60 
MTTILKHLPI NQRVGIAFSG GLDTSAALLW MQKKGAIPYA YTANLGQPDE EDYEAIPRKA 

        70         80         90        100        110        120 
MEYGAEKARL IDCRKQLVAE GIAAIQCGAF HNTTAGVTYF NTTPLGRAVT GTMLVAAMKE 

       130        140        150        160        170        180 
DDVNIWGDGS TYKGNDIERF YRYGLLTNAE LKIYKPWLDT DFIDELGGRH EMSEFMIQSG 

       190        200        210        220        230        240 
FDYKMSTEKA YSTDSNMLGA THEAKDLEFL NSSVKIVNPI MGVKFWDENV VVKAEEVTVR 

       250        260        270        280        290        300 
FERGYPVALN GVVFDDSVEL MMEANRIGGR HGLGMSDQIE NRIIEAKSRG IYEAPGMALL 

       310        320        330        340        350        360 
HIAYERLLTG IHNEDTIEQY HANGRVLGRL LYQGRWFDPQ ALMLRDSIQR WVASEITGEV 

       370        380        390        400        410        420 
TLELRRGNDY SILNTVSDNL TYKPERLTME KGDSVFSPDD RIGQLTMRNL DITDTREKLF 

       430        440        450 
NYVETGLLTS SAATGLPQVD NNNLSSGRGL QDKRQ

« Hide

References

[1]"Genome sequence of the deep-rooted Yersinia pestis strain Angola reveals new insights into the evolution and pangenome of the plague bacterium."
Eppinger M., Worsham P.L., Nikolich M.P., Riley D.R., Sebastian Y., Mou S., Achtman M., Lindler L.E., Ravel J.
J. Bacteriol. 192:1685-1699(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Angola.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000901 Genomic DNA. Translation: ABX88291.1.
RefSeqYP_001606190.1. NC_010159.1.

3D structure databases

ProteinModelPortalA9R622.
SMRA9R622. Positions 2-441.
ModBaseSearch...

Protein-protein interaction databases

STRING349746.YpAngola_A1695.

Proteomic databases

PRIDEA9R622.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABX88291; ABX88291; YpAngola_A1695.
GeneID5800166.
KEGGypg:YpAngola_A1695.
PATRIC18572572. VBIYerPes97331_2070.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0137.
HOGENOMHOG000230094.
KOK01940.
OMAGGRKEMS.
ProtClustDBPRK05370.

Enzyme and pathway databases

UniPathwayUPA00068; UER00113.

Family and domain databases

Gene3D1.10.287.400. 1 hit.
3.40.50.620. 1 hit.
3.90.1260.10. 1 hit.
HAMAPMF_00581. Arg_succ_synth_type2.
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]
PANTHERPTHR11587. PTHR11587. 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_YERPG
AccessionPrimary (citable) accession number: A9R622
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: February 5, 2008
Last modified: May 1, 2013
This is version 44 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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