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UniProtKB/Swiss-Prot entry Q7TUK9

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

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Entry information
Entry name GSHB_PROMM
Primary accession number Q7TUK9
Secondary accession numbers None
Integrated into Swiss-Prot on December 15, 2003
Sequence was last modified on December 15, 2003 (Sequence version 2)
Annotations were last modified on    November 4, 2008 (Entry version 30)
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: PMT2061
From
Prochlorococcus marinus (strain MIT 9313) [TaxID: 74547] [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
BX572101; CAE22235.1; ALT_INIT; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_895886.1; -.
3D structure databases
ModBase Q7TUK9.
Enzyme and pathway databases
BioCyc PMAR74547:PMT2061-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 Q7TUK9.
ProtoNet Q7TUK9.
Genome annotation databases
GeneID 1729231; -.
GenomeReviews BX548175_GR; PMT2061.
KEGG pmt:PMT2061; -.
NMPDR fig|74547.1.peg.2053; -.
Phylogenomic databases
HOGENOM Q7TUK9; -.
Genome annotation databases
CMR Q7TUK9; PMT2061.
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   308  308     Glutathione synthetase. PRO_0000197474
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: 308 AA [This is the length of the unprocessed precursor] Molecular weight: 33316 Da [This is the MW of the unprocessed precursor] CRC64: C5D44F7E79D83F49 [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MRQLFVLDPL QCIQPAKDSS AALMQAAQRA SIEVWACTPA DLQARGDQLS AIAVPVVAEP 

        70         80         90        100        110        120 
WISTGEPRSL PLTDFACIWM RKDPPVDEGY LYATHLLELA ERAGVCVLNR PAALRAWNEK 

       130        140        150        160        170        180 
LGALRFNNLM APTLVASRVS ELAAFAREQE EVVLKPLGGR AGQGLVRVAG AAPGLEALLE 

       190        200        210        220        230        240 
LVTDQEQLPV MVQRFLPAVI EGDKRILLVD GEPLGAVNRR PKAGDFRSNL AMGGRPEPTE 

       250        260        270        280        290        300 
LDSRELQICA ELAPVLREQG LFFVGIDVID GLLSEINVTS PTGIREVERL KGVPLADQVI 


ARLLVSLG
Q7TUK9 in FASTA format

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