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P0AES0 (GSP_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 67. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Bifunctional glutathionylspermidine synthetase/amidase

Including the following 2 domains:

  1. Glutathionylspermidine synthase
    EC=6.3.1.8
    Alternative name(s):
    GSP synthetase
    Glutathione:spermidine ligase [ADP-forming]
  2. Glutathionylspermidine amidase
    EC=3.5.1.78
    Alternative name(s):
    Glutathionylspermidine amidohydrolase [spermidine-forming]
    Short name=GSP amidase
Gene names
Name:gsp
Ordered Locus Names:b2988, JW2956
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia ›

Protein attributes

Sequence length619 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the formation of an amide bond between glutathione and spermidine coupled with hydrolysis of ATP; also catalyzes the hydrolysis of glutathionylspermidine to glutathione and spermidine.

Catalytic activity

Glutathione + spermidine + ATP = glutathionylspermidine + ADP + phosphate.

Glutathionylspermidine + H2O = glutathione + spermidine.

Pathway

Sulfur metabolism; glutathione metabolism.

Amine and polyamine metabolism; spermidine metabolism.

Domain

The two activities reside in distinct domains (N-terminal amidase and C-terminal synthetase).

Sequence similarities

Contains 1 peptidase C51 domain.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

dkgBP308631EBI-557080,EBI-1114788

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 619619Bifunctional glutathionylspermidine synthetase/amidase
PRO_0000070443

Regions

Domain34 – 176143Peptidase C51

Secondary structure

1 ............................................................................................................................ 619
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P0AES0 [UniParc].

Last modified December 20, 2005. Version 1.
Checksum: 07FB43D8A0B2933C

FASTA61970,532
        10         20         30         40         50         60 
MSKGTTSQDA PFGTLLGYAP GGVAIYSSDY SSLDPQEYED DAVFRSYIDD EYMGHKWQCV 

        70         80         90        100        110        120 
EFARRFLFLN YGVVFTDVGM AWEIFSLRFL REVVNDNILP LQAFPNGSPR APVAGALLIW 

       130        140        150        160        170        180 
DKGGEFKDTG HVAIITQLHG NKVRIAEQNV IHSPLPQGQQ WTRELEMVVE NGCYTLKDTF 

       190        200        210        220        230        240 
DDTTILGWMI QTEDTEYSLP QPEIAGELLK ISGARLENKG QFDGKWLDEK DPLQNAYVQA 

       250        260        270        280        290        300 
NGQVINQDPY HYYTITESAE QELIKATNEL HLMYLHATDK VLKDDNLLAL FDIPKILWPR 

       310        320        330        340        350        360 
LRLSWQRRRH HMITGRMDFC MDERGLKVYE YNADSASCHT EAGLILERWA EQGYKGNGFN 

       370        380        390        400        410        420 
PAEGLINELA GAWKHSRARP FVHIMQDKDI EENYHAQFME QALHQAGFET RILRGLDELG 

       430        440        450        460        470        480 
WDAAGQLIDG EGRLVNCVWK TWAWETAFDQ IREVSDREFA AVPIRTGHPQ NEVRLIDVLL 

       490        500        510        520        530        540 
RPEVLVFEPL WTVIPGNKAI LPILWSLFPH HRYLLDTDFT VNDELVKTGY AVKPIAGRCG 

       550        560        570        580        590        600 
SNIDLVSHHE EVLDKTSGKF AEQKNIYQQL WCLPKVDGKY IQVCTFTVGG NYGGTCLRGD 

       610 
ESLVIKKESD IEPLIVVKK

« Hide

References

« Hide 'large scale' references
[1]"Glutathionylspermidine metabolism in Escherichia coli. Purification, cloning, overproduction, and characterization of a bifunctional glutathionylspermidine synthetase/amidase."
Bollinger J.M. Jr., Kwon D.S., Huisman G.W., Kolter R., Walsh C.T.
J. Biol. Chem. 270:14031-14041(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], CHARACTERIZATION.
Strain: K12.
[2]"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 277:1453-1474(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[3]"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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		U23148 Genomic DNA. Translation: AAC43339.1.
U28377 Genomic DNA. Translation: AAA69155.1.
U00096 Genomic DNA. Translation: AAC76024.1.
AP009048 Genomic DNA. Translation: BAE77049.1.
PIRA57538.
RefSeqNP_417462.1. NC_000913.2.
YP_491185.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2IO7X-ray2.70A/B1-619[»]
2IO8X-ray2.10A/B1-619[»]
2IO9X-ray2.20A/B1-619[»]
2IOAX-ray2.80A/B1-619[»]
2IOBX-ray2.20A/B1-619[»]
3A2YX-ray1.95A1-197[»]
3A2ZX-ray1.50A1-197[»]
3A30X-ray2.20A1-197[»]
3O98X-ray2.80A/B1-619[»]
ProteinModelPortalP0AES0.
SMRP0AES0. Positions 8-618.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-36018N.
IntActP0AES0. 11 interactions.
MINTMINT-1234290.
STRING511145.b2988.

Protein family/group databases

MEROPSC51.A01.

Proteomic databases

PaxDbP0AES0.
PRIDEP0AES0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC76024; AAC76024; b2988.
BAE77049; BAE77049; BAE77049.
GeneID12932186.
947474.
KEGGecj:Y75_p2917.
eco:b2988.
PATRIC32121392. VBIEscCol129921_3083.

Organism-specific databases

EchoBASEEB2720.
EcoGeneEG12882. gsp.

Phylogenomic databases

eggNOGCOG0754.
HOGENOMHOG000124980.
KOK01460.
OMAYMGYKWQ.
ProtClustDBPRK10507.

Enzyme and pathway databases

BioCycEcoCyc:GSP-MONOMER.
ECOL316407:JW2956-MONOMER.
MetaCyc:GSP-MONOMER.
UniPathwayUPA00204.
UPA00819.

Gene expression databases

GenevestigatorP0AES0.

Family and domain databases

InterProIPR007921. CHAP.
IPR005494. GSPS_pre-ATP-grasp-like_dom.
IPR016185. PreATP-grasp_dom.
[Graphical view]
PfamPF05257. CHAP. 1 hit.
PF03738. GSP_synth. 1 hit.
[Graphical view]
SUPFAMSSF52440. PreATP-grasp-like. 1 hit.
PROSITEPS50911. CHAP. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP0AES0.

Entry information

Entry nameGSP_ECOLI
AccessionPrimary (citable) accession number: P0AES0
Secondary accession number(s): P43675, Q2M9K7
Entry history
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: December 20, 2005
Last modified: May 1, 2013
This is version 67 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Peptidase families

Classification of peptidase families and list of entries

Escherichia coli

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

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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