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Q8ZFV7 (ASSY_YERPE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 97. 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:YPO1570, y2595, YP_1458
OrganismYersinia pestis [Reference proteome] [HAMAP]
Taxonomic identifier632 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Yersinia

Protein attributes

Sequence length455 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

ATP + L-citrulline + L-aspartate = AMP + diphosphate + N(omega)-(L-arginino)succinate. HAMAP-Rule MF_00005

Pathway

Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine from L-ornithine and carbamoyl phosphate: step 2/3. HAMAP-Rule MF_00005

Subunit structure

Homotetramer By similarity. HAMAP-Rule MF_00005

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00005.

Sequence similarities

Belongs to the argininosuccinate synthase family. Type 2 subfamily.

Sequence caution

The sequence AAM86150.1 differs from that shown. Reason: Erroneous initiation.

The sequence AAS61697.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Biological processAmino-acid biosynthesis
Arginine biosynthesis
   Cellular componentCytoplasm
   LigandATP-binding
Nucleotide-binding
   Molecular functionLigase
   Technical termComplete proteome
Reference 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

Initiator methionine11Removed By similarity
Chain2 – 455454Argininosuccinate synthase HAMAP-Rule MF_00005
PRO_0000148710

Regions

Nucleotide binding17 – 259ATP By similarity

Sites

Binding site431ATP; via amide nitrogen and carbonyl oxygen 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
Q8ZFV7 [UniParc].

Last modified January 23, 2007. Version 3.
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 Yersinia pestis, the causative agent of plague."
Parkhill J., Wren B.W., Thomson N.R., Titball R.W., Holden M.T.G., Prentice M.B., Sebaihia M., James K.D., Churcher C.M., Mungall K.L., Baker S., Basham D., Bentley S.D., Brooks K., Cerdeno-Tarraga A.-M., Chillingworth T., Cronin A., Davies R.M. expand/collapse author list , Davis P., Dougan G., Feltwell T., Hamlin N., Holroyd S., Jagels K., Karlyshev A.V., Leather S., Moule S., Oyston P.C.F., Quail M.A., Rutherford K.M., Simmonds M., Skelton J., Stevens K., Whitehead S., Barrell B.G.
Nature 413:523-527(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: CO-92 / Biovar Orientalis.
[2]"Genome sequence of Yersinia pestis KIM."
Deng W., Burland V., Plunkett G. III, Boutin A., Mayhew G.F., Liss P., Perna N.T., Rose D.J., Mau B., Zhou S., Schwartz D.C., Fetherston J.D., Lindler L.E., Brubaker R.R., Plano G.V., Straley S.C., McDonough K.A., Nilles M.L. expand/collapse author list , Matson J.S., Blattner F.R., Perry R.D.
J. Bacteriol. 184:4601-4611(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: KIM10+ / Biovar Mediaevalis.
[3]"Complete genome sequence of Yersinia pestis strain 91001, an isolate avirulent to humans."
Song Y., Tong Z., Wang J., Wang L., Guo Z., Han Y., Zhang J., Pei D., Zhou D., Qin H., Pang X., Han Y., Zhai J., Li M., Cui B., Qi Z., Jin L., Dai R. expand/collapse author list , Chen F., Li S., Ye C., Du Z., Lin W., Wang J., Yu J., Yang H., Wang J., Huang P., Yang R.
DNA Res. 11:179-197(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 91001 / Biovar Mediaevalis.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AL590842 Genomic DNA. Translation: CAL20215.1.
AE009952 Genomic DNA. Translation: AAM86150.1. Different initiation.
AE017042 Genomic DNA. Translation: AAS61697.1. Different initiation.
PIRAE0191.
RefSeqNP_669899.1. NC_004088.1.
NP_992820.1. NC_005810.1.
YP_002346583.1. NC_003143.1.

3D structure databases

ProteinModelPortalQ8ZFV7.
SMRQ8ZFV7. Positions 2-441.
ModBaseSearch...

Protein-protein interaction databases

IntActQ8ZFV7. 1 interaction.
STRING214092.YPO1570.

Proteomic databases

PRIDEQ8ZFV7.

Protocols and materials databases

DNASU1147542.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAM86150; AAM86150; y2595.
AAS61697; AAS61697; YP_1458.
GeneID1147542.
1174408.
2765614.
KEGGype:YPO1570.
ypk:y2595.
ypm:YP_1458.

Phylogenomic databases

eggNOGCOG0137.
HOGENOMHOG000230094.
KOK01940.
OMAGGRKEMS.
ProtClustDBPRK05370.

Enzyme and pathway databases

BioCycYPES214092:GKDD-1550-MONOMER.
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_YERPE
AccessionPrimary (citable) accession number: Q8ZFV7
Secondary accession number(s): Q0WGK5
Entry history
Integrated into UniProtKB/Swiss-Prot: October 19, 2002
Last sequence update: January 23, 2007
Last modified: May 29, 2013
This is version 97 of the entry and version 3 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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