Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q9PC29 (GSHB_XYLFA) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 77. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Glutathione synthetase

EC=6.3.2.3
Alternative name(s):
GSH synthetase
Short name=GSH-S
Short name=GSHase
Glutathione synthase
Gene names
Name:gshB
Ordered Locus Names:XF_1956
OrganismXylella fastidiosa (strain 9a5c) [Complete proteome] [HAMAP]
Taxonomic identifier160492 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaXanthomonadalesXanthomonadaceaeXylella

Protein attributes

Sequence length314 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

ATP + gamma-L-glutamyl-L-cysteine + glycine = ADP + phosphate + glutathione. HAMAP-Rule MF_00162

Cofactor

Binds 1 magnesium or manganese ion per subunit By similarity.

Pathway

Sulfur metabolism; glutathione biosynthesis; glutathione from L-cysteine and L-glutamate: step 2/2. HAMAP-Rule MF_00162

Sequence similarities

Belongs to the prokaryotic GSH synthase family.

Contains 1 ATP-grasp domain.

Ontologies

Keywords
   Biological processGlutathione biosynthesis
   LigandATP-binding
Magnesium
Manganese
Metal-binding
Nucleotide-binding
   Molecular functionLigase
   Technical termComplete proteome
Gene Ontology (GO)
   Cellular_componentcytosol

Inferred from electronic annotation. Source: InterPro

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

glutathione synthase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

magnesium ion binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

manganese ion binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 314314Glutathione synthetase HAMAP-Rule MF_00162
PRO_0000197498

Regions

Domain125 – 311187ATP-grasp
Nucleotide binding151 – 20858ATP By similarity

Sites

Metal binding2821Magnesium or manganese By similarity
Metal binding2841Magnesium or manganese By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9PC29 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: D05F3E281E50F8D9

FASTA31434,714
        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 

« Hide

References

[1]"The genome sequence of the plant pathogen Xylella fastidiosa."
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. expand/collapse author list , 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.
Nature 406:151-159(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 9a5c.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE003849 Genomic DNA. Translation: AAF84758.1.
PIRF82616.
RefSeqNP_299238.1. NC_002488.3.

3D structure databases

ProteinModelPortalQ9PC29.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING160492.XF1956.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAF84758; AAF84758; XF_1956.
GeneID1127507.
KEGGxfa:XF1956.
PATRIC24134125. VBIXylFas578_2085.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0189.
KOK01920.
OMADWKIARA.
OrthoDBEOG6WMHWB.

Enzyme and pathway databases

UniPathwayUPA00142; UER00210.

Family and domain databases

Gene3D3.30.1490.20. 1 hit.
3.30.470.20. 1 hit.
3.40.50.20. 1 hit.
HAMAPMF_00162. GSH_S.
InterProIPR011761. ATP-grasp.
IPR013815. ATP_grasp_subdomain_1.
IPR013816. ATP_grasp_subdomain_2.
IPR006284. Glut_synth_pro.
IPR004218. GSHS_ATP-bd.
IPR004215. GSHS_N.
IPR016185. PreATP-grasp_dom.
[Graphical view]
PfamPF02955. GSH-S_ATP. 1 hit.
PF02951. GSH-S_N. 1 hit.
[Graphical view]
SUPFAMSSF52440. SSF52440. 1 hit.
TIGRFAMsTIGR01380. glut_syn. 1 hit.
PROSITEPS50975. ATP_GRASP. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGSHB_XYLFA
AccessionPrimary (citable) accession number: Q9PC29
Entry history
Integrated into UniProtKB/Swiss-Prot: January 23, 2002
Last sequence update: October 1, 2000
Last modified: May 14, 2014
This is version 77 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways