ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!
Search for

UniProtKB/Swiss-Prot entry Q8K931


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

Note: most headings are clickable, even if they don't appear as links. They link to the user manual or other documents.
Entry information
Entry name GSHB_BUCAP
Primary accession number Q8K931
Secondary accession numbers None
Integrated into Swiss-Prot on November 8, 2002
Sequence was last modified on October 1, 2002 (Sequence version 1)
Annotations were last modified on    November 4, 2008 (Entry version 39)
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: BUsg_529
From
Buchnera aphidicola subsp. Schizaphis graminum [TaxID: 98794] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; Enterobacteriaceae; Buchnera.
Protein existence 3: Inferred from homology;
References
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1126/science.1071278; PubMed=12089438 [NCBI, ExPASy, EBI, Israel, Japan]
Tamas I., Klasson L., Canbaeck B., Naeslund A.K., Eriksson A.-S., Wernegreen J.J., Sandstroem J.P., Moran N.A., Andersson S.G.E.;
"50 million years of genomic stasis in endosymbiotic bacteria.";
Science 296:2376-2379(2002).
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
AE013218; AAM68070.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_660859.1; -.
3D structure databases
HSSP P04425; 1GSH. [HSSP ENTRY / PDB]
ModBase Q8K931.
Enzyme and pathway databases
BioCyc BAPH198804:BUSG529-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).
ProtoNet Q8K931.
Genome annotation databases
GeneID 1005649; -.
GenomeReviews AE013218_GR; BUsg_529.
KEGG bas:BUsg529; -.
Phylogenomic databases
HOGENOM Q8K931; -.
Genome annotation databases
CMR Q8K931; BUsg_529.
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   320  320     Glutathione synthetase. PRO_0000197460
DOMAIN   130   315  186     ATP-grasp. 
NP_BIND   156   212  57     ATP (By similarity). 
METAL   286   286        Magnesium or manganese (By similarity). 
METAL   288   288        Magnesium or manganese (By similarity). 
Sequence information
Length: 320 AA [This is the length of the unprocessed precursor] Molecular weight: 37166 Da [This is the MW of the unprocessed precursor] CRC64: 20D4A253EEBBD83E [This is a checksum on the sequence]
        10         20         30         40         50         60 
MRKKKNLKIG IVMDSITLIN IKKDSSFAIL LEAQKRQHEI YYMEMNDLYL RKGQSYATTK 

        70         80         90        100        110        120 
SIEIQKNQNN YFKFIQKKDI SLNELDAILM RKDPPFNTEF IYATYILERA EEKGVLVINK 

       130        140        150        160        170        180 
PKSLRDCNEK IFISWFSRFT TDTLVTRKLS KIHNFWKEKN DIILKPLDAM GGKGVFRIKK 

       190        200        210        220        230        240 
DDPNFSVIVE TLTNYEKKYC MIQTYLPEVQ FGDKRILIVN GKPIPWSLTR IPKHGETRAN 

       250        260        270        280        290        300 
LAVGGEGRVQ KLNDKDWEIA NYLAPILKKR GLILVGLDVI GDKLTEINVT SPTCICEIEE 

       310        320 
KKNISITGIL IDYIEDKIYK 

Q8K931 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

BLAST logo BLAST submission on ExPASy/SIB
or at NCBI (USA)
Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
PROSITE logo ScanProsite, MotifScan SWISS-MODEL Submit a homology modeling request to SWISS-MODEL
NPSA logo NPSA Sequence analysis tools

ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
 Hosted by ch flag SIB Switzerland Mirror sites: Australia  Brazil  Canada  China  Korea
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!