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P0AE37 (ASTA_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 74. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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

Names and origin

Protein namesRecommended name:
Arginine N-succinyltransferase

Short name=AST
EC=2.3.1.109
Alternative name(s):
AOST
Gene names
Name:astA
Synonyms:ydjV
Ordered Locus Names:b1747, JW1736
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length344 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Catalyzes the transfer of succinyl-CoA to arginine to produce N(2)-succinylarginine. Ref.3

Catalytic activity

Succinyl-CoA + L-arginine = CoA + N(2)-succinyl-L-arginine. HAMAP-Rule MF_01171

Pathway

Amino-acid degradation; L-arginine degradation via AST pathway; L-glutamate and succinate from L-arginine: step 1/5. HAMAP-Rule MF_01171

Induction

By nitrogen starvation, and arginine. Induced at stationary phase by sigma S. Ref.4

Sequence similarities

Belongs to the arginine N-succinyltransferase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 344344Arginine N-succinyltransferase HAMAP-Rule MF_01171
PRO_0000064712

Sites

Active site2291Proton donor Potential
Binding site1251Succinyl-CoA; via amide nitrogen Potential

Sequences

Sequence LengthMass (Da)Tools
P0AE37 [UniParc].

Last modified December 6, 2005. Version 1.
Checksum: 89C7BB412A880BEF

FASTA34438,456
        10         20         30         40         50         60 
MMVIRPVERS DVSALMQLAS KTGGGLTSLP ANEATLSARI ERAIKTWQGE LPKSEQGYVF 

        70         80         90        100        110        120 
VLEDSETGTV AGICAIEVAV GLNDPWYNYR VGTLVHASKE LNVYNALPTL FLSNDHTGSS 

       130        140        150        160        170        180 
ELCTLFLDPD WRKEGNGYLL SKSRFMFMAA FRDKFNDKVV AEMRGVIDEH GYSPFWQSLG 

       190        200        210        220        230        240 
KRFFSMDFSR ADFLCGTGQK AFIAELMPKH PIYTHFLSQE AQDVIGQVHP QTAPARAVLE 

       250        260        270        280        290        300 
KEGFRYRNYI DIFDGGPTLE CDIDRVRAIR KSRLVEVAEG QPAQGDFPAC LVANENYHHF 

       310        320        330        340 
RVVLVRTDPA TERLILTAAQ LDALKCHAGD RVRLVRLCAE EKTA 

« Hide

References

« Hide 'large scale' references
[1]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1462(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[2]"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[3]"Arginine catabolism and the arginine succinyltransferase pathway in Escherichia coli."
Schneider B.L., Kiupakis A.K., Reitzer L.J.
J. Bacteriol. 180:4278-4286(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[4]"ArgR-independent induction and ArgR-dependent superinduction of the astCADBE operon in Escherichia coli."
Kiupakis A.K., Reitzer L.
J. Bacteriol. 184:2940-2950(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION.
[5]"Prediction of the structure and function of AstA and AstB, the first two enzymes of the arginine succinyltransferase pathway of arginine catabolism."
Shirai H., Mizuguchi K.
FEBS Lett. 555:505-510(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: 3D-STRUCTURE MODELING, REACTION MECHANISM.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U00096 Genomic DNA. Translation: AAC74817.1.
AP009048 Genomic DNA. Translation: BAE76517.1.
PIRC64934.
RefSeqNP_416261.1. NC_000913.3.
YP_490008.1. NC_007779.1.

3D structure databases

ProteinModelPortalP0AE37.
SMRP0AE37. Positions 1-335.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP0AE37. 6 interactions.
STRING511145.b1747.

Proteomic databases

PRIDEP0AE37.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC74817; AAC74817; b1747.
BAE76517; BAE76517; BAE76517.
GeneID12933241.
946261.
KEGGecj:Y75_p1722.
eco:b1747.
PATRIC32118803. VBIEscCol129921_1819.

Organism-specific databases

EchoBASEEB3754.
EcoGeneEG13998. astA.

Phylogenomic databases

eggNOGCOG3138.
HOGENOMHOG000258231.
KOK00673.
OMARFFSMEF.
OrthoDBEOG6XQ3H4.
PhylomeDBP0AE37.
ProtClustDBPRK10456.

Enzyme and pathway databases

BioCycEcoCyc:ARGSUCCTRAN-MONOMER.
ECOL316407:JW1736-MONOMER.
MetaCyc:ARGSUCCTRAN-MONOMER.
UniPathwayUPA00185; UER00279.

Gene expression databases

GenevestigatorP0AE37.

Family and domain databases

Gene3D3.40.630.30. 2 hits.
HAMAPMF_01171. AstA.
InterProIPR016181. Acyl_CoA_acyltransferase.
IPR007041. Arg_N-succinylTrfase_Ast/AOST.
IPR017650. Arginine_N-succinylTrfase_AstA.
[Graphical view]
PfamPF04958. AstA. 1 hit.
[Graphical view]
SUPFAMSSF55729. SSF55729. 1 hit.
TIGRFAMsTIGR03243. arg_catab_AOST. 1 hit.
TIGR03244. arg_catab_AstA. 1 hit.
ProtoNetSearch...

Other

PROP0AE37.

Entry information

Entry nameASTA_ECOLI
AccessionPrimary (citable) accession number: P0AE37
Secondary accession number(s): P76218, Q2MB39
Entry history
Integrated into UniProtKB/Swiss-Prot: December 6, 2005
Last sequence update: December 6, 2005
Last modified: April 16, 2014
This is version 74 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene