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Q8Y3R3

- GSHAB_LISMO

UniProt

Q8Y3R3 - GSHAB_LISMO

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Protein

Glutathione biosynthesis bifunctional protein GshAB

Gene
gshAB, gshF, lmo2770
Organism
Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e)
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at protein leveli

Functioni

Synthesizes glutathione from L-glutamate and L-cysteine via gamma-L-glutamyl-L-cysteine.UniRule annotation

Catalytic activityi

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

Cofactori

Binds 2 magnesium or manganese ions per subunit By similarity.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi721 – 7211Magnesium or manganese 1 By similarity
Metal bindingi738 – 7381Magnesium or manganese 1 By similarity
Metal bindingi738 – 7381Magnesium or manganese 2 By similarity
Metal bindingi740 – 7401Magnesium or manganese 2 By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi541 – 59959ATP By similarityAdd
BLAST

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-HAMAP
  2. glutamate-cysteine ligase activity Source: UniProtKB-HAMAP
  3. glutathione synthase activity Source: UniProtKB-HAMAP
  4. magnesium ion binding Source: UniProtKB-HAMAP
  5. manganese ion binding Source: UniProtKB-HAMAP
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

BioCyciLMON169963:LMO2770-MONOMER.
UniPathwayiUPA00142; UER00209.
UPA00142; UER00210.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutathione biosynthesis bifunctional protein GshAB
Alternative name(s):
Gamma-GCS-GS
Short name:
GCS-GS
Including the following 2 domains:
Glutamate--cysteine ligase (EC:6.3.2.2)
Alternative name(s):
Gamma-ECS
Short name:
GCS
Gamma-glutamylcysteine synthetase
Glutathione synthetase (EC:6.3.2.3)
Alternative name(s):
GSH synthetase
Short name:
GS
Short name:
GSH-S
Short name:
GSHase
Glutathione synthase
Gene namesi
Name:gshAB
Synonyms:gshF
Ordered Locus Names:lmo2770
OrganismiListeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e)
Taxonomic identifieri169963 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesListeriaceaeListeria
ProteomesiUP000000817: Chromosome

Organism-specific databases

GenoListiLMO2770.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 769769Glutathione biosynthesis bifunctional protein GshABUniRule annotationPRO_0000192555Add
BLAST

Interactioni

Subunit structurei

Monomer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi169963.lmo2770.

Structurei

3D structure databases

ProteinModelPortaliQ8Y3R3.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini514 – 768255ATP-graspAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 347347Glutamate--cysteine ligaseUniRule annotationAdd
BLAST

Sequence similaritiesi

In the N-terminal section; belongs to the glutamate--cysteine ligase type 1 family. Type 2 subfamily.
Contains 1 ATP-grasp domain.

Phylogenomic databases

eggNOGiCOG1181.
HOGENOMiHOG000156471.
KOiK01919.
OrthoDBiEOG6BKJ7H.

Family and domain databases

Gene3Di3.30.1490.20. 1 hit.
3.30.470.20. 3 hits.
HAMAPiMF_00782. Glut_biosynth.
InterProiIPR011761. ATP-grasp.
IPR013815. ATP_grasp_subdomain_1.
IPR013816. ATP_grasp_subdomain_2.
IPR007370. Glu_cys_ligase.
IPR006335. Glut_biosynth.
IPR020561. PRibGlycinamid_synth_ATP-grasp.
[Graphical view]
PfamiPF01071. GARS_A. 1 hit.
PF04262. Glu_cys_ligase. 1 hit.
[Graphical view]
TIGRFAMsiTIGR01435. glu_cys_lig_rel. 1 hit.
PROSITEiPS50975. ATP_GRASP. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q8Y3R3-1 [UniParc]FASTAAdd to Basket

« Hide

MLDSFKEDPN LRKLLFSGHF GLEKENIRVT SDGKLALTPH PAIFGPKEDN    50
PYIKTDFSES QIEMITPVTD SIDSVYEWLE NLHNIVSLRS ENELLWPSSN 100
PPILPAEEDI PIAEYKTPDS PDRKYREHLA KGYGKKIQLL SGIHYNFSFP 150
EALIDGLYAN ISLPEESKQD FKNRLYLKVA KYFMKNRWLL IYLTGASPVY 200
LADFSKTKHE ESLPDGSSAL RDGISLRNSN AGYKNKEALF VDYNSFDAYI 250
SSISNYIEAG KIESMREFYN PIRLKNAHTD QTVESLAEHG VEYLEIRSID 300
LNPLEPNGIS KDELDFIHLF LIKGLLSEDR ELCANNQQLA DENENNIALN 350
GLAQPSIKNC DNEDIPLADA GLLELDKMSD FIKSLRPEDT KLRAIIEKQK 400
ERLLHPEKTI AAQVKQQVTK EGYVDFHLNQ AKTYMEETEA LAYKLIGAED 450
MELSTQIIWK DAIARGIKVD VLDRAENFLR FQKGDHIEYV KQASKTSKDN 500
YVSVLMMENK VVTKLVLAEH DIRVPFGDSF SDQALALEAF SLFEDKQIVV 550
KPKSTNYGWG ISIFKNKFTL EDYQEALNIA FSYDSSVIIE EFIPGDEFRF 600
LVINDKVEAV LKRVPANVTG DGIHTVRELV EEKNTDPLRG TDHLKPLEKI 650
RTGPEETLML SMQNLSWDSI PKAEEIIYLR ENSNVSTGGD SIDYTEEMDD 700
YFKEIAIRAT QVLDAKICGV DIIVPRETID RDKHAIIELN FNPAMHMHCF 750
PYQGEQKKIG DKILDFLFD 769
Length:769
Mass (Da):87,728
Last modified:July 5, 2005 - v2
Checksum:iB60DA05A3D8B43FD
GO

Sequence cautioni

The sequence CAD00983.1 differs from that shown. Reason: Erroneous initiation.

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AL591984 Genomic DNA. Translation: CAD00983.1. Different initiation.
PIRiAI1420.
RefSeqiNP_466292.1. NC_003210.1.

Genome annotation databases

EnsemblBacteriaiCAD00983; CAD00983; CAD00983.
GeneIDi986798.
KEGGilmo:lmo2770.
PATRICi20314847. VBILisMon69206_2839.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AL591984 Genomic DNA. Translation: CAD00983.1 . Different initiation.
PIRi AI1420.
RefSeqi NP_466292.1. NC_003210.1.

3D structure databases

ProteinModelPortali Q8Y3R3.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 169963.lmo2770.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CAD00983 ; CAD00983 ; CAD00983 .
GeneIDi 986798.
KEGGi lmo:lmo2770.
PATRICi 20314847. VBILisMon69206_2839.

Organism-specific databases

GenoListi LMO2770.

Phylogenomic databases

eggNOGi COG1181.
HOGENOMi HOG000156471.
KOi K01919.
OrthoDBi EOG6BKJ7H.

Enzyme and pathway databases

UniPathwayi UPA00142 ; UER00209 .
UPA00142 ; UER00210 .
BioCyci LMON169963:LMO2770-MONOMER.

Family and domain databases

Gene3Di 3.30.1490.20. 1 hit.
3.30.470.20. 3 hits.
HAMAPi MF_00782. Glut_biosynth.
InterProi IPR011761. ATP-grasp.
IPR013815. ATP_grasp_subdomain_1.
IPR013816. ATP_grasp_subdomain_2.
IPR007370. Glu_cys_ligase.
IPR006335. Glut_biosynth.
IPR020561. PRibGlycinamid_synth_ATP-grasp.
[Graphical view ]
Pfami PF01071. GARS_A. 1 hit.
PF04262. Glu_cys_ligase. 1 hit.
[Graphical view ]
TIGRFAMsi TIGR01435. glu_cys_lig_rel. 1 hit.
PROSITEi PS50975. ATP_GRASP. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC BAA-679 / EGD-e.
  2. "A multidomain fusion protein in Listeria monocytogenes catalyzes the two primary activities for glutathione biosynthesis."
    Gopal S., Borovok I., Ofer A., Yanku M., Cohen G., Goebel W., Kreft J., Aharonowitz Y.
    J. Bacteriol. 187:3839-3847(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
    Strain: ATCC BAA-679 / EGD-e.

Entry informationi

Entry nameiGSHAB_LISMO
AccessioniPrimary (citable) accession number: Q8Y3R3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 30, 2002
Last sequence update: July 5, 2005
Last modified: May 14, 2014
This is version 76 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Multifunctional enzyme, Reference proteome

Documents

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

External Data

Dasty 3

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