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Reviewed, UniProtKB/Swiss-Prot Q05902 (ECM38_YEAST)

Last modified November 3, 2009. Version 70. 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-glutamyltransferase
    EC=2.3.2.2
Alternative name(s):
    Gamma-glutamyltranspeptidase
      Short name=Gamma-GT
    Extracellular mutant protein 38
    CIK1 suppressor protein 2
Cleaved into the following 2 chains:
    1- Recommended name:
            Gamma-glutamyltransferase heavy chain
    2- Recommended name:
            Gamma-glutamyltransferase light chain
Gene names
Name: ECM38
Synonyms: CIS2
Ordered Locus Names: YLR299W
OrganismSaccharomyces cerevisiae (Baker's yeast) [Complete proteome]
Taxonomic identifier4932 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

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Protein attributes

Sequence length660 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Function

Plays a role in the turnover of the vacuolar glutathione and in the supply of growth requirements during nitrogen starvation. Ref.8

Catalytic activity

(5-L-glutamyl)-peptide + an amino acid = peptide + 5-L-glutamyl amino acid. Ref.2 Ref.3

Enzyme regulation

Activity is decreased by glutathione and ammonium ion. Ref.5

Pathway

Sulfur metabolism; glutathione metabolism.

Subunit structure

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

Subcellular location

Vacuole membrane; Single-pass type II membrane protein. Ref.8 Ref.3 Ref.4

Induction

Induced upon nitrogen starvation. Repressed by ammonium ions. 6-diazo-5-oxo-L-norleucine and L-azaserine are irreversible inhibitors whereas serine-borate is a reversible inhibitor. Ref.2 Ref.3 Ref.7 Ref.9

Post-translational modification

The precursor protein is cleaved into two polypeptide chains, a heavy and a light chain.

Miscellaneous

Present with 672 molecules/cell in log phase SD medium. Ref.10

Sequence similarities

Belongs to the gamma-glutamyltransferase family.

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 469469Gamma-glutamyltransferase heavy chain By similarity
PRO_0000011078
Chain470 – 660191Gamma-glutamyltransferase light chain By similarity
PRO_0000011079

Regions

Topological domain1 – 1313Cytoplasmic Potential
Transmembrane14 – 3421Signal-anchor for type II membrane protein Potential
Topological domain35 – 660626Lumenal Potential

Amino acid modifications

Glycosylation1191N-linked (GlcNAc...) Potential
Glycosylation1911N-linked (GlcNAc...) Potential
Glycosylation2701N-linked (GlcNAc...) Potential
Glycosylation2981N-linked (GlcNAc...) Potential
Glycosylation4541N-linked (GlcNAc...) Potential
Glycosylation5171N-linked (GlcNAc...) Potential

Natural variations

Natural variant1711H → R in strain: YPH499. Ref.11
Natural variant4941G → D in strain: YPH499; lack of gamma-glutamyl transferase activity. Ref.11

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Sequences

Sequence LengthMass (Da)Tools
Q05902-1 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 9896E9EBFF822F55

FASTA66073,180
        10         20         30         40         50         60 
MLLCNRKVPK TLNTCFILHI FTLLTLGVLV SGMPSKMVSF ASQETLQRIN NLLRGSANRD 

        70         80         90        100        110        120 
VDIIAEYLKK DDDDDGGDKD HHNIDIDPLP RRPSLTPDRQ LLKVGLHGAI SSDLEVCSNL 

       130        140        150        160        170        180 
TINEVLLKFP GSNAADAAVT QALCKGMVNF FNSGIGGGGY VVFSGKDDED HLSIDFREKA 

       190        200        210        220        230        240 
PMDSHKFMFE NCSLCSKIGG LAVGVPGELM GLYRLFKERG SGQVDWRDLI EPVAKLGSVG 

       250        260        270        280        290        300 
WQIGEALGAT LELYEDVFLT LKEDWSFVLN STHDGVLKEG DWIKRPALSN MLMELAKNGS 

       310        320        330        340        350        360 
VAPFYDPDHW IAKSMIDTVA KYNGIMNLQD VSSYDVHVTK PLSMKIRKGA NFIPDNDMTV 

       370        380        390        400        410        420 
LTSSGSSSGA ALLAALRIMD NFQNQEGGDY EKETTYHLLE SMKWMASARS RLGDFEGEAL 

       430        440        450        460        470        480 
PKHIEEVLDP EWALKAVKSI KRNSQDGNFK TLENWTLYDP AYDINNPHGT AHFSIVDSHG 

       490        500        510        520        530        540 
NAVSLTTTIN LLFGSLVHDP KTGVIFNNEM DDFAQFNKSN SFELAPSIYN FPEPGKRPLS 

       550        560        570        580        590        600 
STAPTIVLSE LGIPDLVVGA SGGSRITTSV LQTIVRTYWY NMPILETIAY PRIHHQLLPD 

       610        620        630        640        650        660 
RIELESFPMI GKAVLSTLKE MGYTMKEVFP KSVVNAIRNV RGEWHAVSDY WRKRGISSVY

« Hide

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References

« Hide 'large scale' references
[1]"The nucleotide sequence of Saccharomyces cerevisiae chromosome XII."
Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W., Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A., Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K., Heuss-Neitzel D., Hilbert H. expand/collapse author list , Hilger F., Kleine K., Koetter P., Louis E.J., Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S., Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D., Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M., Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P., Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M., Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K., Zollner A., Hani J., Hoheisel J.D.
Nature 387:87-90(1997) [PubMed: 9169871] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204511 / S288c / AB972.
[2]"Glutathione metabolism in relation to the amino-acid permeation systems of the yeast Saccharomyces cerevisiae. Occurrence of gamma-glutamyltranspeptidase: its regulation and the effects of permeation mutations on the enzyme cellular level."
Penninckx M., Jaspers C., Wiame J.M.
Eur. J. Biochem. 104:119-123(1980) [PubMed: 6102906] [Abstract]
Cited for: CATALYTIC ACTIVITY, INDUCTION.
[3]"Gamma-glutamyltransferase is not involved in the bulk uptake of amino acids, peptides or gamma-glutamyl-amino acids in yeast (Saccharomyces cerevisiae)."
Payne G.M., Payne J.W.
Biochem. J. 218:147-155(1984) [PubMed: 6143552] [Abstract]
Cited for: CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, INDUCTION.
[4]"Glutathione metabolism in yeast Saccharomyces cerevisiae. Evidence that gamma-glutamyltranspeptidase is a vacuolar enzyme."
Jaspers C.J., Penninckx M.J.
Biochimie 66:71-74(1984) [PubMed: 6143574] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[5]"Glutathione as an endogenous sulphur source in the yeast Saccharomyces cerevisiae."
Elskens M.T., Jaspers C.J., Penninckx M.J.
J. Gen. Microbiol. 137:637-644(1991) [PubMed: 1674526] [Abstract]
Cited for: ENZYME REGULATION.
[6]"Large scale identification of genes involved in cell surface biosynthesis and architecture in Saccharomyces cerevisiae."
Lussier M., White A.-M., Sheraton J., di Paolo T., Treadwell J., Southard S.B., Horenstein C.I., Chen-Weiner J., Ram A.F.J., Kapteyn J.C., Roemer T.W., Vo D.H., Bondoc D.C., Hall J., Zhong W.-W., Sdicu A.-M., Davies J., Klis F.M., Robbins P.W., Bussey H.
Genetics 147:435-450(1997) [PubMed: 9335584] [Abstract]
Cited for: IDENTIFICATION.
[7]"An important role for glutathione and gamma-glutamyltranspeptidase in the supply of growth requirements during nitrogen starvation of the yeast Saccharomyces cerevisiae."
Mehdi K., Penninckx M.J.
Microbiology 143:1885-1889(1997) [PubMed: 9202464] [Abstract]
Cited for: INDUCTION.
[8]"Gamma-glutamyl transpeptidase in the yeast Saccharomyces cerevisiae and its role in the vacuolar transport and metabolism of glutathione."
Mehdi K., Thierie J., Penninckx M.J.
Biochem. J. 359:631-637(2001) [PubMed: 11672438] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
[9]"Nitrogen-source regulation of yeast gamma-glutamyl transpeptidase synthesis involves the regulatory network including the GATA zinc-finger factors Gln3, Nil1/Gat1 and Gzf3."
Springael J.-Y., Penninckx M.J.
Biochem. J. 371:589-595(2003) [PubMed: 12529169] [Abstract]
Cited for: INDUCTION.
[10]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed: 14562106] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[11]"Investigations into the polymorphisms at the ECM38 locus of two widely used Saccharomyces cerevisiae S288C strains, YPH499 and BY4742."
Kumar C., Sharma R., Bachhawat A.K.
Yeast 20:857-863(2003) [PubMed: 12868055] [Abstract]
Cited for: VARIANTS ARG-171 AND ASP-494.
Strain: ATCC 76625 / YPH499.
+Additional computationally mapped references.

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Cross-references

Sequence databases

U17243 Genomic DNA. Translation: AAB67344.1.
PIRS50383.
RefSeqNP_013402.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

DIPDIP:4682N.
IntActQ05902. 1 interaction.
STRINGQ05902.

Protein family/group databases

MEROPST03.012.

Genome annotation databases

EnsemblYLR299W; YLR299W; YLR299W; Saccharomyces cerevisiae. [Genome view]
GeneID851006.
GenomeReviewsGene locus YLR299W in contig Y13138_GR.
KEGGsce:YLR299W.
NMPDRfig|4932.3.peg.4419.

Organism-specific databases

CYGDYLR299w.
SGDS000004290. ECM38.

Phylogenomic databases

HOGENOMQ05902.
OMALELIANN.

Enzyme and pathway databases

BRENDA2.3.2.2. 250.

Gene expression databases

ArrayExpressQ05902.
GenevestigatorQ05902.
GermOnlineYLR299W. Saccharomyces cerevisiae.

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. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio967555.

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Entry information

Entry nameECM38_YEAST
AccessionPrimary (citable) accession number: Q05902
Entry history
Integrated into UniProtKB/Swiss-Prot: March 1, 2005
Last sequence update: November 1, 1996
Last modified: November 3, 2009
This is version 70 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

SIMILARITY comments

Index of protein domains and families

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

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