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P90518

- GSP_CRIFA

UniProt

P90518 - GSP_CRIFA

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Protein

Glutathionylspermidine synthase

Gene
GSP
Organism
Crithidia fasciculata
Status
Reviewed - 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

Magnesium.

Sites

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

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi350 – 3523ATP By similarity
Nucleotide bindingi689 – 6913ATP By 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.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini54 – 200147Peptidase C51Add
BLAST

Sequence similaritiesi

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

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

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MSSLPHNHHY ETHHRGTAEV PFDELIGVTP DGVPVISNGN EAHFSNLESI    50
TAACLPLSSF ERKAPCKQPY RKMGVKWQCV EFVRRYLASR KAVWMTSLCT 100
AEEVWREENL FVDVRDGRPV EVVRTPNKST GPAPAVADIV VWGEGPETPF 150
GHVAIVTEVC ASCVRVAEQN QGFEKWPEDV PFSREIAMRT TESGEVELLD 200
EDPLLGWVTV QAPFYNFDDG DLADSFRLVV GQGQILRQPF PKHVDVPWLN 250
TGEECDTILK HSLVVDGNMG EGAHAEEGDV PGAFYFLDYD MFCRLGRAAS 300
SLHRIAMAAT AKVLEDPEST HLLEHYFGVP PEIQPLLRRS WEMTPPMGGR 350
FDFGYDGKNV VMLEYNCDSS GALLECCNTQ EKMARFYGVS QGTSTGSFLG 400
AKCVTYFQRL LTNEKVCPQH RLIHFMIDED DEERYTARCM MGFAEQAGFR 450
TKLCVKLVNF RYRDGPPSNA APLATPCDHP TIVDGEDEEV LMVWKTWSWD 500
TVLHQYHSQR SSSDAVNTPT LSDILLNNNI RVLEPLWKAV TGSKAILPFM 550
HALAPDHEHM LAASFLPTRE IISRHYISKP VNGRAGQNIM MYDPVTSPTE 600
LEGAPQQDIC EALSQNASAR SLLNGSPLPL SQSVDQTNEC SPGKFFDSVL 650
VYQQRLFLKK FDGKYFPIFC GWMVGDEFGG VVVREDTSKI TKLSSMVVPA 700
RVVRDNVPLG VSYSDEGET 719
Length:719
Mass (Da):80,322
Last modified:March 1, 2001 - v2
Checksum:i46069BE9C40EEEFC
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U66520 Genomic DNA. Translation: AAC48361.2.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U66520 Genomic DNA. Translation: AAC48361.2 .

3D structure databases

ProteinModelPortali P90518.
ModBasei Search...
MobiDBi Search...

Chemistry

BindingDBi P90518.
ChEMBLi CHEMBL3354.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

BRENDAi 6.3.1.8. 1365.
SABIO-RK P90518.

Family and domain databases

InterProi IPR007921. CHAP_dom.
IPR005494. GSPS_pre-ATP-grasp-like_dom.
IPR016185. PreATP-grasp_dom.
[Graphical view ]
Pfami PF05257. CHAP. 1 hit.
PF03738. GSP_synth. 1 hit.
[Graphical view ]
SUPFAMi SSF52440. SSF52440. 1 hit.
PROSITEi PS50911. CHAP. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: July 9, 2014
This is version 59 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

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