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UniProtKB/Swiss-Prot entry Q8PHZ5


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

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Entry information
Entry name GSHB_XANAC
Primary accession number Q8PHZ5
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: XAC3103
From
Xanthomonas axonopodis pv. citri (Citrus canker) [TaxID: 92829] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales; Xanthomonadaceae; Xanthomonas.
Protein existence 3: Inferred from homology;
References
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=306;
DOI=10.1038/417459a; PubMed=12024217 [NCBI, ExPASy, EBI, Israel, Japan]
da Silva A.C.R., Ferro J.A., Reinach F.C., Farah C.S., Furlan L.R., Quaggio R.B., Monteiro-Vitorello C.B., Van Sluys M.A., Almeida N.F. Jr., Alves L.M.C., do Amaral A.M., Bertolini M.C., Camargo L.E.A., Camarotte G., Cannavan F., Cardozo J., Chambergo F., Ciapina L.P., Cicarelli R.M.B., Coutinho L.L., Cursino-Santos J.R., El-Dorry H., Faria J.B., Ferreira A.J.S., Ferreira R.C.C., Ferro M.I.T., Formighieri E.F., Franco M.C., Greggio C.C., Gruber A., Katsuyama A.M., Kishi L.T., Leite R.P., Lemos E.G.M., Lemos M.V.F., Locali E.C., Machado M.A., Madeira A.M.B.N., Martinez-Rossi N.M., Martins E.C., Meidanis J., Menck C.F.M., Miyaki C.Y., Moon D.H., Moreira L.M., Novo M.T.M., Okura V.K., Oliveira M.C., Oliveira V.R., Pereira H.A., Rossi A., Sena J.A.D., Silva C., de Souza R.F., Spinola L.A.F., Takita M.A., Tamura R.E., Teixeira E.C., Tezza R.I.D., Trindade dos Santos M., Truffi D., Tsai S.M., White F.F., Setubal J.C., Kitajima J.P.;
"Comparison of the genomes of two Xanthomonas pathogens with differing host specificities.";
Nature 417:459-463(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
AE011954; AAM37948.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_643412.1; -.
3D structure databases
HSSP P04425; 1GLV. [HSSP ENTRY / PDB]
ModBase Q8PHZ5.
Enzyme and pathway databases
BioCyc XAXO190486:XAC3103-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.
IPR002035; VWF_A.
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.
PRINTS PR00453; VWFADOMAIN.
TIGRFAMs TIGR01380; glut_syn; 1.
PROSITE PS50975; ATP_GRASP; 1.
PROSITE graphical view of domain structure (profiles).
ProtoNet Q8PHZ5.
Genome annotation databases
GeneID 1157174; -.
GenomeReviews AE008923_GR; XAC3103.
KEGG xac:XAC3103; -.
NMPDR fig|190486.1.peg.3056; -.
Phylogenomic databases
HOGENOM Q8PHZ5; -.
Genome annotation databases
CMR Q8PHZ5; XAC3103.
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   316  316     Glutathione synthetase. PRO_0000197496
DOMAIN   124   311  188     ATP-grasp. 
NP_BIND   151   208  58     ATP (By similarity). 
METAL   282   282        Magnesium or manganese (By similarity). 
METAL   284   284        Magnesium or manganese (By similarity). 
Sequence information
Length: 316 AA [This is the length of the unprocessed precursor] Molecular weight: 34321 Da [This is the MW of the unprocessed precursor] CRC64: BAEABE5F8A0FF268 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MSLDVVVVMD PIASIKIAKD TTFAMLLEAQ RRGHRLHYVR PGGLSLREGR AVAQVAPLSV 

        70         80         90        100        110        120 
REDKTSWFTL GEFAELAFGP GQVVLMRKDP PVDAEFVYDT QVLSVAQRAG AQIVNDPQGL 

       130        140        150        160        170        180 
RDYNEKLAAL LFPQCCPPTL VSRDAAALKA FVLEHGQAVL KPLDGMGGRS IFRSGSGDPN 

       190        200        210        220        230        240 
LNVILETLTD GNRKLTLAQR FIPDITAGDK RILLVDGLPV DYCLARIPQG DEFRGNLAAG 

       250        260        270        280        290        300 
GRGEGRPLSE RDRWIAAQVG PEMRRRGMRF VGLDVIGDYL TEVNVTSPTC VRELDAQFGL 

       310 
NIAGLLFDAI EAGAAQ 

Q8PHZ5 in FASTA format

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Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
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