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Protein

Glutathione synthetase

Gene

gshB

Organism
Bordetella parapertussis (strain 12822 / ATCC BAA-587 / NCTC 13253)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Catalytic activityi

ATP + gamma-L-glutamyl-L-cysteine + glycine = ADP + phosphate + glutathione.UniRule annotation

Cofactori

Mg2+By similarity, Mn2+By similarityNote: Binds 1 Mg(2+) or Mn2+ ion per subunit.By similarity

Pathway:iglutathione biosynthesis

This protein is involved in step 2 of the subpathway that synthesizes glutathione from L-cysteine and L-glutamate.UniRule annotation
Proteins known to be involved in the 2 steps of the subpathway in this organism are:
  1. Glutamate--cysteine ligase (gshA)
  2. Glutathione synthetase (gshB)
This subpathway is part of the pathway glutathione biosynthesis, which is itself part of Sulfur metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes glutathione from L-cysteine and L-glutamate, the pathway glutathione biosynthesis and in Sulfur metabolism.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi285 – 2851Magnesium or manganeseUniRule annotation
Metal bindingi287 – 2871Magnesium or manganeseUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi155 – 21157ATPUniRule annotationAdd
BLAST

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Glutathione biosynthesis

Keywords - Ligandi

ATP-binding, Magnesium, Manganese, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciBPAR257311:BPP1965-MONOMER.
UniPathwayiUPA00142; UER00210.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutathione synthetaseUniRule annotation (EC:6.3.2.3UniRule annotation)
Alternative name(s):
GSH synthetaseUniRule annotation
Short name:
GSH-SUniRule annotation
Short name:
GSHaseUniRule annotation
Glutathione synthaseUniRule annotation
Gene namesi
Name:gshBUniRule annotation
Synonyms:gsh-II
Ordered Locus Names:BPP1965
OrganismiBordetella parapertussis (strain 12822 / ATCC BAA-587 / NCTC 13253)
Taxonomic identifieri257311 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesAlcaligenaceaeBordetella
ProteomesiUP000001421 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 318318Glutathione synthetasePRO_0000197454Add
BLAST

Structurei

3D structure databases

ProteinModelPortaliQ7W910.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini129 – 314186ATP-graspUniRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the prokaryotic GSH synthase family.UniRule annotation
Contains 1 ATP-grasp domain.UniRule annotation

Phylogenomic databases

eggNOGiCOG0189.
HOGENOMiHOG000265022.
KOiK01920.
OMAiMKPLHGH.
OrthoDBiEOG6WMHWB.

Family and domain databases

Gene3Di3.30.1490.20. 1 hit.
3.30.470.20. 1 hit.
3.40.50.20. 1 hit.
HAMAPiMF_00162. GSH_S.
InterProiIPR011761. 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]
PfamiPF02955. GSH-S_ATP. 1 hit.
PF02951. GSH-S_N. 1 hit.
[Graphical view]
SUPFAMiSSF52440. SSF52440. 1 hit.
TIGRFAMsiTIGR01380. glut_syn. 1 hit.
PROSITEiPS50975. ATP_GRASP. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q7W910-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MHVLFIIDPL PLLKAYKDSS VAMMQALQAR GHTLSVALQG DLYIDAGEVR
60 70 80 90 100
TRFAPIALRD GADLHGHDWW RETGAADEAP LARFDAVVMR KDPPFDMEYV
110 120 130 140 150
YSTHLLEYAQ QQGARVFNSG AAIRNHPEKL AITEFPDLTT PTLVTRDMGR
160 170 180 190 200
IRAFHAAQGD VIVKPLDGMG GTGIFRLQRS EPNLNAILET LTDNGTRTIM
210 220 230 240 250
AQRYIPEIVK GDKRILLIGG EPVPYSLARI PLAGETRGNL AAGGRGVAQP
260 270 280 290 300
LSERDLHLAR TVADRLAGRG LLLVGLDVIG DYITEVNVTS PTCFVEITEQ
310
TGFNVPEMFA VALESAAG
Length:318
Mass (Da):34,652
Last modified:October 1, 2003 - v1
Checksum:i5902082AD5DC4F97
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BX640429 Genomic DNA. Translation: CAE37264.1.
RefSeqiWP_003812603.1. NC_002928.3.

Genome annotation databases

EnsemblBacteriaiCAE37264; CAE37264; BPP1965.
KEGGibpa:BPP1965.
PATRICi21147744. VBIBorPar43418_2070.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BX640429 Genomic DNA. Translation: CAE37264.1.
RefSeqiWP_003812603.1. NC_002928.3.

3D structure databases

ProteinModelPortaliQ7W910.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAE37264; CAE37264; BPP1965.
KEGGibpa:BPP1965.
PATRICi21147744. VBIBorPar43418_2070.

Phylogenomic databases

eggNOGiCOG0189.
HOGENOMiHOG000265022.
KOiK01920.
OMAiMKPLHGH.
OrthoDBiEOG6WMHWB.

Enzyme and pathway databases

UniPathwayiUPA00142; UER00210.
BioCyciBPAR257311:BPP1965-MONOMER.

Family and domain databases

Gene3Di3.30.1490.20. 1 hit.
3.30.470.20. 1 hit.
3.40.50.20. 1 hit.
HAMAPiMF_00162. GSH_S.
InterProiIPR011761. 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]
PfamiPF02955. GSH-S_ATP. 1 hit.
PF02951. GSH-S_N. 1 hit.
[Graphical view]
SUPFAMiSSF52440. SSF52440. 1 hit.
TIGRFAMsiTIGR01380. glut_syn. 1 hit.
PROSITEiPS50975. ATP_GRASP. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Comparative analysis of the genome sequences of Bordetella pertussis, Bordetella parapertussis and Bordetella bronchiseptica."
    Parkhill J., Sebaihia M., Preston A., Murphy L.D., Thomson N.R., Harris D.E., Holden M.T.G., Churcher C.M., Bentley S.D., Mungall K.L., Cerdeno-Tarraga A.-M., Temple L., James K.D., Harris B., Quail M.A., Achtman M., Atkin R., Baker S.
    , Basham D., Bason N., Cherevach I., Chillingworth T., Collins M., Cronin A., Davis P., Doggett J., Feltwell T., Goble A., Hamlin N., Hauser H., Holroyd S., Jagels K., Leather S., Moule S., Norberczak H., O'Neil S., Ormond D., Price C., Rabbinowitsch E., Rutter S., Sanders M., Saunders D., Seeger K., Sharp S., Simmonds M., Skelton J., Squares R., Squares S., Stevens K., Unwin L., Whitehead S., Barrell B.G., Maskell D.J.
    Nat. Genet. 35:32-40(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 12822 / ATCC BAA-587 / NCTC 13253.

Entry informationi

Entry nameiGSHB_BORPA
AccessioniPrimary (citable) accession number: Q7W910
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 2003
Last sequence update: October 1, 2003
Last modified: July 22, 2015
This is version 75 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.