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P63186 (GGT_BACNA) Reviewed, UniProtKB/Swiss-Prot

Last modified October 19, 2011. Version 35. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Gamma-glutamyltranspeptidase
EC=2.3.2.2

Cleaved into the following 2 chains:

  1. Gamma-glutamyltranspeptidase large chain
  2. Gamma-glutamyltranspeptidase small chain
Gene names
Name:ggt
OrganismBacillus subtilis subsp. natto
Taxonomic identifier86029 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length587 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

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

Glutathione + H2O = L-cysteinylglycine + L-glutamate.

Enzyme regulation

Inhibited by glucose.

Pathway

Sulfur metabolism; glutathione metabolism.

Subunit structure

This enzyme consists of two polypeptide chains, which are synthesized in precursor form from a single polypeptide By similarity.

Subcellular location

Secreted.

Sequence similarities

Belongs to the gamma-glutamyltransferase family.

Ontologies

Keywords
   Biological processGlutathione biosynthesis
   Cellular componentSecreted
   DomainSignal
   Molecular functionAcyltransferase
Transferase
   PTMZymogen
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological processglutathione biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functiongamma-glutamyltransferase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2828 Potential
Propeptide29 – 357 Potential
PRO_0000011046
Chain36 – 402367Gamma-glutamyltranspeptidase large chain
PRO_0000011047
Chain403 – 587185Gamma-glutamyltranspeptidase small chain
PRO_0000011048

Experimental info

Sequence conflict461D → V AA sequence Ref.2

Sequences

Sequence LengthMass (Da)Tools
P63186 [UniParc].

Last modified September 27, 2004. Version 1.
Checksum: 4025FB5FC9A33C58

FASTA58764,070
        10         20         30         40         50         60 
MKRTWNVCLT ALLSVLLVAG SVPFHAEAKK PPKSYDEYKQ VDVGKDGMVA TAHALASEIG 

        70         80         90        100        110        120 
ADVLKKGGNA IDAAVAIQFA LNVTEPMMSG IGGGGFMMVY DGKTKDTTII DSRERAPAGA 

       130        140        150        160        170        180 
TPDMFLDENG KAIPFSERVT KGTAVGVPGT LKGLEEALDK WGTRSMKLLI TLTIKLAEKG 

       190        200        210        220        230        240 
FPIDSVLADA ISDYQEKLSR TAAKDVFLPN GEPLKEGDTL IQKDLAKTFK LIRSKGTDAF 

       250        260        270        280        290        300 
YKGKFAKTLS DTVQDFGGSM TEKDLENYDI TIDEPIWGDY QGYQIATTPP PSSGGIFLLQ 

       310        320        330        340        350        360 
MLKILDDFNL SQYDVRSWEK YQLLAETMHL SYADRASYAG DPEFVNVPLK GLLHPDYIKE 

       370        380        390        400        410        420 
RQQLINLDQV NKKPKAGDPW KYQEGSANYK QVEQPKDKVE GQTTHFTVAD RWGNVVSYTT 

       430        440        450        460        470        480 
TIEQLFGTGI MVPDYGVILN NELTDFDAIP GGANEVQPNK RPLSSMTPTI LFKDDKPVLT 

       490        500        510        520        530        540 
VGSPGGATII SSVLQTILYH IEYGMGLKAA VEEPRIYTTS MSSYRYEDGV PKDVLSKLNG 

       550        560        570        580 
MGHRFGTSPV DIGNVQSISI DHENGTFKGV VISGSNDAAI GINLKRK

« Hide

References

[1]"DNA sequence of Bacillus subtilis (natto) NR-1 gamma-glutamyltranspeptidase gene, ggt."
Ogawa Y., Sugiura D., Motai H., Yuasa K., Tahara Y.
Biosci. Biotechnol. Biochem. 61:1596-1600(1997) [PubMed: 9339568] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: NR-1.
[2]"Purification and properties of gamma-glutamyltranspeptidase from Bacillus subtilis (natto)."
Ogawa Y., Hosoyama H., Hamano M., Motai H.
Agric. Biol. Chem. 55:2971-2977(1991) [PubMed: 1371053] [Abstract]
Cited for: PROTEIN SEQUENCE OF 36-52 AND 403-442, CHARACTERIZATION.
Strain: NR-1.

Cross-references

Sequence databases

PIRF69631.

3D structure databases

ProteinModelPortalP63186.
SMRP63186. Positions 38-395, 403-585.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

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...

Entry information

Entry nameGGT_BACNA
AccessionPrimary (citable) accession number: P63186
Entry history
Integrated into UniProtKB/Swiss-Prot: September 27, 2004
Last sequence update: September 27, 2004
Last modified: October 19, 2011
This is version 35 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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