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Protein

Glutathionylspermidine synthase

Gene

GSP

Organism
Crithidia fasciculata
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

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 activityi

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

Cofactori

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei350 – 3501GlutathioneBy similarity
Sitei350 – 3501Transition state stabilizerBy similarity
Metal bindingi352 – 3521Magnesium 1By similarity
Metal bindingi364 – 3641Magnesium 1By similarity
Metal bindingi364 – 3641Magnesium 2By similarity
Metal bindingi366 – 3661Magnesium 2By similarity
Binding sitei369 – 3691GlutathioneBy similarity
Binding sitei432 – 4321SpermidineBy similarity
Binding sitei433 – 4331GlutathioneBy similarity
Binding sitei501 – 5011GlutathioneBy similarity
Binding sitei544 – 5441ATPBy similarity
Binding sitei579 – 5791ATPBy similarity
Binding sitei586 – 5861ATP; via amide nitrogenBy similarity
Binding sitei653 – 6531ATPBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi350 – 3523ATPBy similarity
Nucleotide bindingi689 – 6913ATPBy similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. glutathionylspermidine synthase activity Source: UniProtKB-EC
  3. metal ion binding Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Ligandi

ATP-binding, Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi6.3.1.8. 1365.
SABIO-RKP90518.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutathionylspermidine synthase (EC:6.3.1.8)
Gene namesi
Name:GSP
OrganismiCrithidia fasciculata
Taxonomic identifieri5656 [NCBI]
Taxonomic lineageiEukaryotaEuglenozoaKinetoplastidaTrypanosomatidaeLeishmaniinaeCrithidia

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 719719Glutathionylspermidine synthasePRO_0000070442Add
BLAST

Post-translational modificationi

The N-terminus is blocked.

Interactioni

Structurei

3D structure databases

ProteinModelPortaliP90518.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini54 – 200147Peptidase C51PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

In the C-terminal section; belongs to the glutathionylspermidine synthase preATP-grasp family.Curated
Contains 1 peptidase C51 domain.PROSITE-ProRule annotation

Family and domain databases

InterProiIPR007921. CHAP_dom.
IPR005494. GSPS_pre-ATP-grasp-like_dom.
IPR016185. PreATP-grasp_dom.
[Graphical view]
PfamiPF05257. CHAP. 1 hit.
PF03738. GSP_synth. 1 hit.
[Graphical view]
SUPFAMiSSF52440. SSF52440. 1 hit.
PROSITEiPS50911. CHAP. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P90518-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSSLPHNHHY ETHHRGTAEV PFDELIGVTP DGVPVISNGN EAHFSNLESI
60 70 80 90 100
TAACLPLSSF ERKAPCKQPY RKMGVKWQCV EFVRRYLASR KAVWMTSLCT
110 120 130 140 150
AEEVWREENL FVDVRDGRPV EVVRTPNKST GPAPAVADIV VWGEGPETPF
160 170 180 190 200
GHVAIVTEVC ASCVRVAEQN QGFEKWPEDV PFSREIAMRT TESGEVELLD
210 220 230 240 250
EDPLLGWVTV QAPFYNFDDG DLADSFRLVV GQGQILRQPF PKHVDVPWLN
260 270 280 290 300
TGEECDTILK HSLVVDGNMG EGAHAEEGDV PGAFYFLDYD MFCRLGRAAS
310 320 330 340 350
SLHRIAMAAT AKVLEDPEST HLLEHYFGVP PEIQPLLRRS WEMTPPMGGR
360 370 380 390 400
FDFGYDGKNV VMLEYNCDSS GALLECCNTQ EKMARFYGVS QGTSTGSFLG
410 420 430 440 450
AKCVTYFQRL LTNEKVCPQH RLIHFMIDED DEERYTARCM MGFAEQAGFR
460 470 480 490 500
TKLCVKLVNF RYRDGPPSNA APLATPCDHP TIVDGEDEEV LMVWKTWSWD
510 520 530 540 550
TVLHQYHSQR SSSDAVNTPT LSDILLNNNI RVLEPLWKAV TGSKAILPFM
560 570 580 590 600
HALAPDHEHM LAASFLPTRE IISRHYISKP VNGRAGQNIM MYDPVTSPTE
610 620 630 640 650
LEGAPQQDIC EALSQNASAR SLLNGSPLPL SQSVDQTNEC SPGKFFDSVL
660 670 680 690 700
VYQQRLFLKK FDGKYFPIFC GWMVGDEFGG VVVREDTSKI TKLSSMVVPA
710
RVVRDNVPLG VSYSDEGET
Length:719
Mass (Da):80,322
Last modified:March 1, 2001 - v2
Checksum:i46069BE9C40EEEFC
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U66520 Genomic DNA. Translation: AAC48361.2.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U66520 Genomic DNA. Translation: AAC48361.2.

3D structure databases

ProteinModelPortaliP90518.
ModBaseiSearch...
MobiDBiSearch...

Chemistry

BindingDBiP90518.
ChEMBLiCHEMBL3354.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

BRENDAi6.3.1.8. 1365.
SABIO-RKP90518.

Family and domain databases

InterProiIPR007921. CHAP_dom.
IPR005494. GSPS_pre-ATP-grasp-like_dom.
IPR016185. PreATP-grasp_dom.
[Graphical view]
PfamiPF05257. CHAP. 1 hit.
PF03738. GSP_synth. 1 hit.
[Graphical view]
SUPFAMiSSF52440. SSF52440. 1 hit.
PROSITEiPS50911. CHAP. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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.

Entry informationi

Entry nameiGSP_CRIFA
AccessioniPrimary (citable) accession number: P90518
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 6, 2002
Last sequence update: March 1, 2001
Last modified: November 26, 2014
This is version 61 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

Keywords - Technical termi

Direct protein sequencing

Documents

  1. Peptidase families
    Classification of peptidase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.