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UniProtKB/Swiss-Prot entry Q9PC29


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

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Entry information
Entry name GSHB_XYLFA
Primary accession number Q9PC29
Secondary accession numbers None
Integrated into Swiss-Prot on January 23, 2002
Sequence was last modified on October 1, 2000 (Sequence version 1)
Annotations were last modified on    November 4, 2008 (Entry version 42)
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: XF_1956
From
Xylella fastidiosa [TaxID: 2371] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales; Xanthomonadaceae; Xylella.
Protein existence 3: Inferred from homology;
References
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=9a5c;
DOI=10.1038/35018003; PubMed=10910347 [NCBI, ExPASy, EBI, Israel, Japan]
Simpson A.J.G., Reinach F.C., Arruda P., Abreu F.A., Acencio M., Alvarenga R., Alves L.M.C., Araya J.E., Baia G.S., Baptista C.S., Barros M.H., Bonaccorsi E.D., Bordin S., Bove J.M., Briones M.R.S., Bueno M.R.P., Camargo A.A., Camargo L.E.A., Carraro D.M., Carrer H., Colauto N.B., Colombo C., Costa F.F., Costa M.C.R., Costa-Neto C.M., Coutinho L.L., Cristofani M., Dias-Neto E., Docena C., El-Dorry H., Facincani A.P., Ferreira A.J.S., Ferreira V.C.A., Ferro J.A., Fraga J.S., Franca S.C., Franco M.C., Frohme M., Furlan L.R., Garnier M., Goldman G.H., Goldman M.H.S., Gomes S.L., Gruber A., Ho P.L., Hoheisel J.D., Junqueira M.L., Kemper E.L., Kitajima J.P., Krieger J.E., Kuramae E.E., Laigret F., Lambais M.R., Leite L.C.C., Lemos E.G.M., Lemos M.V.F., Lopes S.A., Lopes C.R., Machado J.A., Machado M.A., Madeira A.M.B.N., Madeira H.M.F., Marino C.L., Marques M.V., Martins E.A.L., Martins E.M.F., Matsukuma A.Y., Menck C.F.M., Miracca E.C., Miyaki C.Y., Monteiro-Vitorello C.B., Moon D.H., Nagai M.A., Nascimento A.L.T.O., Netto L.E.S., Nhani A. Jr., Nobrega F.G., Nunes L.R., Oliveira M.A., de Oliveira M.C., de Oliveira R.C., Palmieri D.A., Paris A., Peixoto B.R., Pereira G.A.G., Pereira H.A. Jr., Pesquero J.B., Quaggio R.B., Roberto P.G., Rodrigues V., de Rosa A.J.M., de Rosa V.E. Jr., de Sa R.G., Santelli R.V., Sawasaki H.E., da Silva A.C.R., da Silva A.M., da Silva F.R., Silva W.A. Jr., da Silveira J.F., Silvestri M.L.Z., Siqueira W.J., de Souza A.A., de Souza A.P., Terenzi M.F., Truffi D., Tsai S.M., Tsuhako M.H., Vallada H., Van Sluys M.A., Verjovski-Almeida S., Vettore A.L., Zago M.A., Zatz M., Meidanis J., Setubal J.C.;
"The genome sequence of the plant pathogen Xylella fastidiosa.";
Nature 406:151-159(2000).
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
AE003849; AAF84758.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR F82616; F82616.
RefSeq NP_299238.1; -.
3D structure databases
HSSP P04425; 1GLV. [HSSP ENTRY / PDB]
ModBase Q9PC29.
Enzyme and pathway databases
BioCyc XFAS160492:XF1956-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 Q9PC29.
Genome annotation databases
GeneID 1127507; -.
GenomeReviews AE003849_GR; XF_1956.
KEGG xfa:XF1956; -.
NMPDR fig|160492.1.peg.1945; -.
Phylogenomic databases
HOGENOM Q9PC29; -.
Genome annotation databases
CMR Q9PC29; XF_1956.
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   314  314     Glutathione synthetase. PRO_0000197498
DOMAIN   125   311  187     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: 314 AA [This is the length of the unprocessed precursor] Molecular weight: 34714 Da [This is the MW of the unprocessed precursor] CRC64: D05F3E281E50F8D9 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MPLDVVVVMD PITGIKIAKD TTFALLLEGQ RRSHRLHYVH PGSLSLNEGR TFAQIAPLQV 

        70         80         90        100        110        120 
RDNKTDWYTL GEFSETQLGQ GQIILMRKDP PVNAEFIYDT QLLSIAQAAG AQVINHPQGL 

       130        140        150        160        170        180 
RDLNEKLAAQ LFPQCCPPTL ISRDMRALKM FVQKQEQAIL KPLDGMGGHS IFRSSNGDPN 

       190        200        210        220        230        240 
LNVILETLTD GGRTLAIAQR YLQQIIEGDK RILLIDGVPI DHCLARIPQG DEFRGNMAAG 

       250        260        270        280        290        300 
GRGESRPLNE HDRWIAAQVG PEMRRRGMRF VGIDVIGDYL TEINVTSPTC LRELDAQCGL 

       310 
NIAGQLFDAI ETGG 

Q9PC29 in FASTA format

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