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P90518 (GSP_CRIFA) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 59. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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:
Glutathionylspermidine synthase

EC=6.3.1.8
Gene names
Name:GSP
OrganismCrithidia fasciculata
Taxonomic identifier5656 [NCBI]
Taxonomic lineageEukaryotaEuglenozoaKinetoplastidaTrypanosomatidaeLeishmaniinaeCrithidia

Protein attributes

Sequence length719 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Conjugates glutathione (gamma-Glu-Cys-Gly) and spermidine to form glutathionylspermidine in the biosynthesis trypanothione (N1,N(8)-bis(glutathionyl)spermidine), which is involved in maintaining intracellular thiol redox and in defense against oxidants.

Catalytic activity

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

Cofactor

Magnesium.

Post-translational modification

The N-terminus is blocked.

Sequence similarities

In the C-terminal section; belongs to the glutathionylspermidine synthase preATP-grasp family.

Contains 1 peptidase C51 domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 719719Glutathionylspermidine synthase
PRO_0000070442

Regions

Domain54 – 200147Peptidase C51
Nucleotide binding350 – 3523ATP By similarity
Nucleotide binding689 – 6913ATP By similarity

Sites

Metal binding3521Magnesium 1 By similarity
Metal binding3641Magnesium 1 By similarity
Metal binding3641Magnesium 2 By similarity
Metal binding3661Magnesium 2 By similarity
Binding site3501Glutathione By similarity
Binding site3691Glutathione By similarity
Binding site4321Spermidine By similarity
Binding site4331Glutathione By similarity
Binding site5011Glutathione By similarity
Binding site5441ATP By similarity
Binding site5791ATP By similarity
Binding site5861ATP; via amide nitrogen By similarity
Binding site6531ATP By similarity
Site3501Transition state stabilizer By similarity

Sequences

Sequence LengthMass (Da)Tools
P90518 [UniParc].

Last modified March 1, 2001. Version 2.
Checksum: 46069BE9C40EEEFC

FASTA71980,322
        10         20         30         40         50         60 
MSSLPHNHHY ETHHRGTAEV PFDELIGVTP DGVPVISNGN EAHFSNLESI TAACLPLSSF 

        70         80         90        100        110        120 
ERKAPCKQPY RKMGVKWQCV EFVRRYLASR KAVWMTSLCT AEEVWREENL FVDVRDGRPV 

       130        140        150        160        170        180 
EVVRTPNKST GPAPAVADIV VWGEGPETPF GHVAIVTEVC ASCVRVAEQN QGFEKWPEDV 

       190        200        210        220        230        240 
PFSREIAMRT TESGEVELLD EDPLLGWVTV QAPFYNFDDG DLADSFRLVV GQGQILRQPF 

       250        260        270        280        290        300 
PKHVDVPWLN TGEECDTILK HSLVVDGNMG EGAHAEEGDV PGAFYFLDYD MFCRLGRAAS 

       310        320        330        340        350        360 
SLHRIAMAAT AKVLEDPEST HLLEHYFGVP PEIQPLLRRS WEMTPPMGGR FDFGYDGKNV 

       370        380        390        400        410        420 
VMLEYNCDSS GALLECCNTQ EKMARFYGVS QGTSTGSFLG AKCVTYFQRL LTNEKVCPQH 

       430        440        450        460        470        480 
RLIHFMIDED DEERYTARCM MGFAEQAGFR TKLCVKLVNF RYRDGPPSNA APLATPCDHP 

       490        500        510        520        530        540 
TIVDGEDEEV LMVWKTWSWD TVLHQYHSQR SSSDAVNTPT LSDILLNNNI RVLEPLWKAV 

       550        560        570        580        590        600 
TGSKAILPFM HALAPDHEHM LAASFLPTRE IISRHYISKP VNGRAGQNIM MYDPVTSPTE 

       610        620        630        640        650        660 
LEGAPQQDIC EALSQNASAR SLLNGSPLPL SQSVDQTNEC SPGKFFDSVL VYQQRLFLKK 

       670        680        690        700        710 
FDGKYFPIFC GWMVGDEFGG VVVREDTSKI TKLSSMVVPA RVVRDNVPLG VSYSDEGET 

« Hide

References

[1]"Cloning and characterization of the two enzymes responsible for trypanothione biosynthesis in Crithidia fasciculata."
Tetaud E., Manai F., Barrett M.P., Nadeau K., Walsh C.T., Fairlamb A.H.
J. Biol. Chem. 273:19383-19390(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE.
Strain: HS6.
[2]"Purification of glutathionylspermidine and trypanothione synthetases from Crithidia fasciculata."
Smith K., Nadeau K., Bradley M., Walsh C., Fairlamb A.H.
Protein Sci. 1:874-883(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 191-209; 351-358; 512-530; 532-538 AND 695-710, CHARACTERIZATION.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U66520 Genomic DNA. Translation: AAC48361.2.

3D structure databases

ProteinModelPortalP90518.
ModBaseSearch...
MobiDBSearch...

Chemistry

BindingDBP90518.
ChEMBLCHEMBL3354.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

BRENDA6.3.1.8. 1365.
SABIO-RKP90518.

Family and domain databases

InterProIPR007921. CHAP_dom.
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. SSF52440. 1 hit.
PROSITEPS50911. CHAP. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGSP_CRIFA
AccessionPrimary (citable) accession number: P90518
Entry history
Integrated into UniProtKB/Swiss-Prot: December 6, 2002
Last sequence update: March 1, 2001
Last modified: July 9, 2014
This is version 59 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries