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UniProtKB/Swiss-Prot entry Q7TUG9

[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name GSHB_PROMP
Primary accession number Q7TUG9
Secondary accession numbers None
Integrated into Swiss-Prot on December 15, 2003
Sequence was last modified on October 1, 2003 (Sequence version 1)
Annotations were last modified on    November 4, 2008 (Entry version 32)
Name and origin of the protein
Protein name Glutathione synthetase
Synonyms EC 6.3.2.3
Glutathione synthase
GSH synthetase
GSH-S
GSHase
Gene name
Name: gshB
OrderedLocusNames: PMM0178
From
Prochlorococcus marinus subsp. pastoris (strain CCMP1378 / MED4) [TaxID: 59919] [HAMAP proteome]
Taxonomy Bacteria; Cyanobacteria; Prochlorales; Prochlorococcaceae; Prochlorococcus.
Protein existence 3: Inferred from homology;
References
[1]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1038/nature01947; PubMed=12917642 [NCBI, ExPASy, EBI, Israel, Japan]
Rocap G., Larimer F.W., Lamerdin J.E., Malfatti S., Chain P., Ahlgren N.A., Arellano A., Coleman M., Hauser L., Hess W.R., Johnson Z.I., Land M.L., Lindell D., Post A.F., Regala W., Shah M., Shaw S.L., Steglich C., Sullivan M.B., Ting C.S., Tolonen A., Webb E.A., Zinser E.R., Chisholm S.W.;
"Genome divergence in two Prochlorococcus ecotypes reflects oceanic niche differentiation.";
Nature 424:1042-1047(2003).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
BX548174; CAE18637.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_892299.1; -.
3D structure databases
ModBase Q7TUG9.
Enzyme and pathway databases
BioCyc PMAR167540:PMM0178-MON; -.
Ontologies
GO
GO:0005524; Molecular function: ATP binding (inferred from electronic annotation from HAMAP).
GO:0004363; Molecular function: glutathione synthase activity (inferred from electronic annotation from HAMAP).
GO:0000287; Molecular function: magnesium ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0030145; Molecular function: manganese ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0006750; Biological process: glutathione biosynthetic process (inferred from electronic annotation from HAMAP).
QuickGo view.
Family and domain databases
HAMAP MF_00162; -; 1.
PBIL [Tree]
InterPro IPR011761; ATP-grasp.
IPR013816; ATP_grasp_subdomain_2.
IPR006284; Glut_synth_pro.
IPR004218; GSHS_ATP_bd.
IPR004215; GSHS_N.
IPR013817; Pre-ATP_grasp.
Graphical view of domain structure.
Gene3D G3DSA:3.30.470.20; ATP_grasp_subdomain_2; 1.
G3DSA:3.40.50.20; Pre-ATP_grasp; 1.
Pfam PF02955; GSH-S_ATP; 1.
PF02951; GSH-S_N; 1.
Pfam graphical view of domain structure.
TIGRFAMs TIGR01380; glut_syn; 1.
PROSITE PS50975; ATP_GRASP; 1.
PROSITE graphical view of domain structure (profiles).
BLOCKS Q7TUG9.
ProtoNet Q7TUG9.
Genome annotation databases
GeneID 1727216; -.
GenomeReviews BX548174_GR; PMM0178.
KEGG pmm:PMM0178; -.
NMPDR fig|59919.1.peg.178; -.
Phylogenomic databases
HOGENOM Q7TUG9; -.
Genome annotation databases
CMR Q7TUG9; PMM0178.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
ATP-binding; Complete proteome; Glutathione biosynthesis; Ligase; Magnesium; Manganese; Metal-binding; Nucleotide-binding.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   307  307     Glutathione synthetase. PRO_0000197475
DOMAIN   120   304  185     ATP-grasp. 
NP_BIND   146   202  57     ATP (By similarity). 
METAL   275   275        Magnesium or manganese (By similarity). 
METAL   277   277        Magnesium or manganese (By similarity). 
Sequence information
Length: 307 AA [This is the length of the unprocessed precursor] Molecular weight: 34254 Da [This is the MW of the unprocessed precursor] CRC64: 76EC5F13BDE80B24 [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MKFLFVVDPI KNINPLKDSS AALMQASSKK KIEVWICTPQ DLEARGDEVW ASSWRAEVCP 

        70         80         90        100        110        120 
WVSFKENKCI PLAEFNCIWM RKDPPVNEGY LYATHLLEVA ERKGVKVINK PSSLRAWNEK 

       130        140        150        160        170        180 
LGALRYSHLM APTIVASKVK DLINFAQINH DVVVKPLGGK GGQGVIRLTK DSPGIKAMIE 

       190        200        210        220        230        240 
LITSQEQLPV MMQKFIPEVK EGDKRIIIVN GEPIGSINRI PQGGDFRSNL AMGGKAEKTN 

       250        260        270        280        290        300 
LTAKEKKICT ELSQHFKDEG LFFVGIDVIN EMLSEINVTS PTGLREIETL SNKSVSDKVI 


EKLLEII
Q7TUG9 in FASTA format

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