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Reviewed, UniProtKB/Swiss-Prot Q9US04 (GGT1_SCHPO)

Last modified February 9, 2010. Version 52. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Gamma-glutamyltranspeptidase 1
    EC=2.3.2.2
Alternative name(s):
    Gamma-glutamyltransferase 1
Cleaved into the following 2 chains:
    1- Recommended name:
            Gamma-glutamyltranspeptidase 1 heavy chain
    2- Recommended name:
            Gamma-glutamyltranspeptidase 1 light chain
Gene names
Name: ggt1
ORF Names: SPAC664.09
OrganismSchizosaccharomyces pombe (Fission yeast) [Complete proteome]
Taxonomic identifier4896 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces

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Protein attributes

Sequence length630 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level.

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General annotation (Comments)

Function

Initiates extracellular glutathione (GSH) breakdown, provides cells with a local cysteine supply and contributes to maintain intracelular GSH level. It is part of the cell antioxidant defense mechanism. Catalyzes the transfer of the glutamyl moiety of glutathione to amino acids and dipeptide acceptors. Alternatively, glutathione can be hydrolyzed to give Cys-Gly and gamma glutamate. Ref.1

Catalytic activity

(5-L-glutamyl)-peptide + an amino acid = peptide + 5-L-glutamyl amino acid.

Pathway

Sulfur metabolism; glutathione metabolism.

Subunit structure

Heterodimer composed of the light and heavy chains. The active site is located in the light chain By similarity.

Subcellular location

Membrane; Single-pass type II membrane protein Potential.

Induction

Induced upon nitrogen starvation. Also induced by non-fermentable carbon sources such as glycerol, acetate and ethanol in a pap1-independent manner. Ref.3

Sequence similarities

Belongs to the gamma-glutamyltransferase family.

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Ontologies

Keywords
   Biological processGlutathione biosynthesis
   Cellular componentMembrane
   DomainSignal-anchor
Transmembrane
   Molecular functionAcyltransferase
Transferase
   PTMGlycoprotein
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processcell redox homeostasis Ref.3

Traceable author statement. Source: GeneDB_SPombe

cellular response to nitrogen starvation Ref.3

Inferred from direct assay. Source: GeneDB_SPombe

glutathione biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

glutathione catabolic process Ref.1

Inferred by curator. Source: GeneDB_SPombe

   Cellular componentendoplasmic reticulum

Inferred from direct assay. Source: GeneDB_SPombe

integral to membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionacyltransferase activity

Inferred from electronic annotation. Source: UniProtKB-KW

gamma-glutamyltransferase activity Ref.1

Inferred from direct assay. Source: GeneDB_SPombe

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 440440Gamma-glutamyltranspeptidase 1 heavy chain By similarity
PRO_0000247898
Chain441 – 630190Gamma-glutamyltranspeptidase 1 light chain By similarity
PRO_0000247899

Regions

Topological domain1 – 4949Cytoplasmic Potential
Transmembrane50 – 7021Signal-anchor for type II membrane protein Potential
Topological domain71 – 630560Extracellular Potential

Amino acid modifications

Glycosylation1561N-linked (GlcNAc...) Potential
Glycosylation1801N-linked (GlcNAc...) Potential
Glycosylation3151N-linked (GlcNAc...) Potential
Glycosylation3971N-linked (GlcNAc...) Potential
Glycosylation4171N-linked (GlcNAc...) Potential
Glycosylation6121N-linked (GlcNAc...) Potential

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Sequences

Sequence LengthMass (Da)Tools
Q9US04-1 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: E85E83D21AC24B20

FASTA63068,722
        10         20         30         40         50         60 
MGINTSSAQS SGAASIARSS VNVKSGNRHL SSNKKSATSA LEERASRPSI LVTFLVLAGT 

        70         80         90        100        110        120 
ILSLYIWPIL SPDLFFANQR CSFKYKNKGS QRVVVEGKNG VVATEEETCS QIGVGILKAG 

       130        140        150        160        170        180 
GNAVDAAIAS GICIGAVNSF SSGIGGGGFM LIRHPNGTAH SLNFRETAPA GASKNMFHGN 

       190        200        210        220        230        240 
STLSQVGGLS VAVPGEIAGY ERAWKMYGSL PWHKLFEPTI RLMRDGMPMP KELASRIRRP 

       250        260        270        280        290        300 
EFSYFKTHPD WSKIFAPEGV FLHVGEKFYR PALASTLEEI AKFGPEVFYT GKIAERLVKF 

       310        320        330        340        350        360 
VQQQGGILTM EDMANFSVVV EEPIYGNFYD REVITCGSPC SGEALILGLN VLSKVDLSEG 

       370        380        390        400        410        420 
TSILGCEMTD IGVHHLIETM KWMSAGRTVL ADPTFYNNTD HVEQLLSLEY ADEIRNNISN 

       430        440        450        460        470        480 
ERTFDFTHYK AEYDFPNDHG TTHLSVIDKD NMAVGLTASI NLMFGSQLLE PETGIILNDH 

       490        500        510        520        530        540 
MDDFASPGIV NAFGLSPSPY NFIAPGKRPQ SSAVPTILVY NGEVEMVLGG SGGSRIVTAV 

       550        560        570        580        590        600 
LDTIIKKYKW GKSLLESVES PRFHHQLMPN IVYIDETVEI EVLRALEKFG HIVDLIPVQY 

       610        620        630 
PFSEIQAVFR TNGTLYGLSD SRKQAVAAAY

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References

« Hide 'large scale' references
[1]"Characterization and regulation of the gamma-glutamyl transpeptidase gene from the fission yeast Schizosaccharomyces pombe."
Park H.-J., Lim H.-W., Kim K., Kim I.-H., Park E.-H., Lim C.-J.
Can. J. Microbiol. 50:61-66(2004) [PubMed: 15052323] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION.
[2]"The genome sequence of Schizosaccharomyces pombe."
Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M. expand/collapse author list , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.
Nature 415:871-880(2002) [PubMed: 11859360] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 38366 / 972.
[3]"The Schizosaccharomyces pombe gene encoding gamma-glutamyl transpeptidase I is regulated by non-fermentable carbon sources and nitrogen starvation."
Kim H.-G., Park H.-J., Kang H.-J., Lim H.-W., Kim K., Park E.-H., Ahn K., Lim C.-J.
J. Microbiol. 43:44-48(2005) [PubMed: 15765057] [Abstract]
Cited for: INDUCTION.

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AF535133 Genomic DNA. Translation: AAN01227.1.
CU329670 Genomic DNA. Translation: CAB65810.1.
PIRT50239.
RefSeqNP_593457.1.

3D structure databases

SMRQ9US04. Positions 89-630.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ9US04.

Protein family/group databases

MEROPST03.011.

Genome annotation databases

GeneID2543536.
GenomeReviewsGene locus ggt1 in contig CU329670_GR.
KEGGspo:SPAC664.09.
NMPDRfig|4896.1.peg.3427.

Organism-specific databases

GeneDB_SpombeSPAC664.09.

Phylogenomic databases

eggNOGfuNOG04439.
HOGENOMHBG738311.
OMAAYAKRSN.
OrthoDBEOG9ZW6T5.
PhylomeDBQ9US04.

Enzyme and pathway databases

BRENDA2.3.2.2. 653.

Gene expression databases

ArrayExpressQ9US04.

Family and domain databases

InterProIPR000101. GGT_peptidase.
[Graphical view]
PANTHERPTHR11686. GGT_peptidase. 1 hit.
PfamPF01019. G_glu_transpept. 1 hit.
[Graphical view]
PRINTSPR01210. GGTRANSPTASE.
TIGRFAMsTIGR00066. g_glut_trans. 1 hit.
PROSITEPS00462. G_GLU_TRANSPEPTIDASE. False negative.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry nameGGT1_SCHPO
AccessionPrimary (citable) accession number: Q9US04
Entry history
Integrated into UniProtKB/Swiss-Prot: July 25, 2006
Last sequence update: May 1, 2000
Last modified: February 9, 2010
This is version 52 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectFPAP (Fungal Proteome Annotation Project)

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Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

Schizosaccharomyces pombe

Schizosaccharomyces pombe: entries and gene names

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents