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D5TYR7 (D5TYR7_BACT1) Unreviewed, UniProtKB/TrEMBL

Last modified May 1, 2013. Version 25. Feed History...

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

Protein namesRecommended name:
Glutathione biosynthesis bifunctional protein GshAB HAMAP-Rule MF_00782
Alternative name(s):
Gamma-GCS-GS HAMAP-Rule MF_00782
Gene names
Name:gshAB HAMAP-Rule MF_00782
Synonyms:gshF HAMAP-Rule MF_00782
Ordered Locus Names:BMB171_P0005 EMBL ADH09901.1
Encoded onPlasmid pBMB171 EMBL ADH09901.1
OrganismBacillus thuringiensis (strain BMB171) [Complete proteome] [HAMAP] EMBL ADH09901.1
Taxonomic identifier714359 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacilli › Bacillales › Bacillaceae › Bacillus › Bacillus cereus group ›

Protein attributes

Sequence length755 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Synthesizes glutathione from L-glutamate and L-cysteine via gamma-L-glutamyl-L-cysteine By similarity. HAMAP-Rule MF_00782

Catalytic activity

ATP + L-glutamate + L-cysteine = ADP + phosphate + gamma-L-glutamyl-L-cysteine. HAMAP-Rule MF_00782

ATP + gamma-L-glutamyl-L-cysteine + glycine = ADP + phosphate + glutathione. HAMAP-Rule MF_00782

Pathway

Sulfur metabolism; glutathione biosynthesis; glutathione from L-cysteine and L-glutamate: step 1/2. HAMAP-Rule MF_00782

Sulfur metabolism; glutathione biosynthesis; glutathione from L-cysteine and L-glutamate: step 2/2. HAMAP-Rule MF_00782

Subunit structure

Monomer By similarity. HAMAP-Rule MF_00782

Sequence similarities

Contains 1 ATP-grasp domain. HAMAP-Rule MF_00782

In the N-terminal section; belongs to the glutamate--cysteine ligase type 1 family. Type 2 subfamily. HAMAP-Rule MF_00782

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Regions

Domain491 – 749259ATP-grasp By similarity HAMAP-Rule MF_00782
Nucleotide binding518 – 57760ATP By similarity HAMAP-Rule MF_00782
Region1 – 336336Glutamate--cysteine ligase By similarity HAMAP-Rule MF_00782

Sites

Metal binding6991Magnesium or manganese 1 By similarity HAMAP-Rule MF_00782
Metal binding7191Magnesium or manganese 1 By similarity HAMAP-Rule MF_00782
Metal binding7191Magnesium or manganese 2 By similarity HAMAP-Rule MF_00782
Metal binding7211Magnesium or manganese 2 By similarity HAMAP-Rule MF_00782

Sequences

Sequence LengthMass (Da)Tools
D5TYR7 [UniParc].

Last modified July 13, 2010. Version 1.
Checksum: FB903CC352EDA507

FASTA75586,801
        10         20         30         40         50         60 
MEMKKMLNND RIKPYLLKAR FGVEKESQRV DLSGSLAKTE HPKSISVRDE HPYIQRDFSE 

        70         80         90        100        110        120 
TQMELITPVT ETLGDLFNYL AAIHDVAYRS MGNNEMLWPL SMPPQLPEKE EDIVIAKLNN 

       130        140        150        160        170        180 
HENVLYRRYL SNSYGRRKQM ISGIHYNFEF SDNLIQALFE LQSEIKDYHQ FKTEIYLKVT 

       190        200        210        220        230        240 
RNYLHYRWLI TYFFGASPSS EKNFFEINPL NDAVRSIRNS KYGYSNENDV QVSYSSLQNY 

       250        260        270        280        290        300 
ISDLSSLVSK GVLLEEKEFY ASVRLRGGPQ VSDLKNHGIR YIELRNLDLN PFETYGISHE 

       310        320        330        340        350        360 
QAEFLHLFLI YLLWIDQDDN NDEWVKIGDF QNNLVALEHP LEHTQFKTDA ERIIDEMEHL 

       370        380        390        400        410        420 
TGLLDITVSN TLFVNLREML TDPSKTLAGR LYKEIIKSSQ SQVASRIAKE NYKKAWDKPY 

       430        440        450        460        470        480 
QLSGFTDMEL STQILMFDAI QQGLQVDVLD RQDQFLKLQL GNHVEYVKNG NMTSKDSYIS 

       490        500        510        520        530        540 
PLIMENKTVT KKILQQHGFR VPIGEEFSDI EKALRSYDIF AGKPFVVKPK TTNYGLGISI 

       550        560        570        580        590        600 
FKENGASYED YQKALTIAFK EDSSVLIEEF INGTEYRFFV LDGKVSAVLL RIPANVIGDG 

       610        620        630        640        650        660 
SHTIEELVAQ KNLNSLRGMD HRTPLENIQL GELEVLMLKA QGYRKDSIPT SDEIVFLREN 

       670        680        690        700        710        720 
SNVSTGGDSI DMTDQIPDDY KKIAVDAVSA LGANISGIDL IIENTEVPAA NKNAYGIIEA 

       730        740        750 
NFNPSMYMHI YPYKGKSRRL TICILHYLFP ELPKK

« Hide

References

[1]"Complete genome sequence of Bacillus thuringiensis mutant strain BMB171."
He J., Shao X., Zheng H., Li M., Wang J., Zhang Q., Li L., Liu Z., Sun M., Wang S., Yu Z.
J. Bacteriol. 192:4074-4075(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: BMB171.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP001904 Genomic DNA. Translation: ADH09901.1.
RefSeqYP_003667621.1. NC_014172.1.

3D structure databases

ProteinModelPortalD5TYR7.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaADH09901; ADH09901; BMB171_P0005.
GeneID9196135.
KEGGbtb:BMB171_P0005.
PATRIC38137382. VBIBacThu148000_5440.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHOG000156471.
KOK01919.

Enzyme and pathway databases

BioCycBTHU714359:GJBQ-5242-MONOMER.
UniPathwayUPA00142; UER00209.
UPA00142; UER00210.

Family and domain databases

Gene3D3.30.1490.20. 1 hit.
3.30.470.20. 3 hits.
HAMAPMF_00782. Glut_biosynth.
InterProIPR011761. ATP-grasp.
IPR013815. ATP_grasp_subdomain_1.
IPR013816. ATP_grasp_subdomain_2.
IPR007370. Glu_cys_ligase.
IPR006335. Glut_cys-rel.
[Graphical view]
PfamPF04262. Glu_cys_ligase. 1 hit.
[Graphical view]
TIGRFAMsTIGR01435. glu_cys_lig_rel. 1 hit.
PROSITEPS50975. ATP_GRASP. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameD5TYR7_BACT1
AccessionPrimary (citable) accession number: D5TYR7
Entry history
Integrated into UniProtKB/TrEMBL: July 13, 2010
Last sequence update: July 13, 2010
Last modified: May 1, 2013
This is version 25 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info