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Protein

Glutathione biosynthesis bifunctional protein GshAB

Gene

gshAB

Organism
Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e)
Status
Reviewed-Annotation score: 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.

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

Mg2+By similarity, Mn2+By similarityNote: Binds 2 magnesium or manganese ions per subunit.By similarity

Pathwayi

Sites

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

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi541 – 59959ATPUniRule 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

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

Names & Taxonomyi

Protein namesi
Recommended name:
Glutathione biosynthesis bifunctional protein GshABUniRule annotation
Alternative name(s):
Gamma-GCS-GSUniRule annotation
Short name:
GCS-GSUniRule annotation
Including the following 2 domains:
Glutamate--cysteine ligaseUniRule annotation (EC:6.3.2.2UniRule annotation)
Alternative name(s):
Gamma-ECSUniRule annotation
Short name:
GCSUniRule annotation
Gamma-glutamylcysteine synthetaseUniRule annotation
Glutathione synthetaseUniRule annotation (EC:6.3.2.3UniRule annotation)
Alternative name(s):
GSH synthetaseUniRule annotation
Short name:
GSUniRule annotation
Short name:
GSH-SUniRule annotation
Short name:
GSHaseUniRule annotation
Glutathione synthaseUniRule annotation
Gene namesi
Name:gshABUniRule annotation
Synonyms:gshFUniRule annotation
Ordered Locus Names:lmo2770
OrganismiListeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e)
Taxonomic identifieri169963 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesListeriaceaeListeria
ProteomesiUP000000817 Componenti: Chromosome

Organism-specific databases

GenoListiLMO2770.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 769769Glutathione biosynthesis bifunctional protein GshABPRO_0000192555Add
BLAST

Interactioni

Subunit structurei

Monomer.UniRule annotation

Protein-protein interaction databases

STRINGi169963.lmo2770.

Structurei

3D structure databases

ProteinModelPortaliQ8Y3R3.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

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

Region

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

Sequence similaritiesi

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

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

        10         20         30         40         50
MLDSFKEDPN LRKLLFSGHF GLEKENIRVT SDGKLALTPH PAIFGPKEDN
60 70 80 90 100
PYIKTDFSES QIEMITPVTD SIDSVYEWLE NLHNIVSLRS ENELLWPSSN
110 120 130 140 150
PPILPAEEDI PIAEYKTPDS PDRKYREHLA KGYGKKIQLL SGIHYNFSFP
160 170 180 190 200
EALIDGLYAN ISLPEESKQD FKNRLYLKVA KYFMKNRWLL IYLTGASPVY
210 220 230 240 250
LADFSKTKHE ESLPDGSSAL RDGISLRNSN AGYKNKEALF VDYNSFDAYI
260 270 280 290 300
SSISNYIEAG KIESMREFYN PIRLKNAHTD QTVESLAEHG VEYLEIRSID
310 320 330 340 350
LNPLEPNGIS KDELDFIHLF LIKGLLSEDR ELCANNQQLA DENENNIALN
360 370 380 390 400
GLAQPSIKNC DNEDIPLADA GLLELDKMSD FIKSLRPEDT KLRAIIEKQK
410 420 430 440 450
ERLLHPEKTI AAQVKQQVTK EGYVDFHLNQ AKTYMEETEA LAYKLIGAED
460 470 480 490 500
MELSTQIIWK DAIARGIKVD VLDRAENFLR FQKGDHIEYV KQASKTSKDN
510 520 530 540 550
YVSVLMMENK VVTKLVLAEH DIRVPFGDSF SDQALALEAF SLFEDKQIVV
560 570 580 590 600
KPKSTNYGWG ISIFKNKFTL EDYQEALNIA FSYDSSVIIE EFIPGDEFRF
610 620 630 640 650
LVINDKVEAV LKRVPANVTG DGIHTVRELV EEKNTDPLRG TDHLKPLEKI
660 670 680 690 700
RTGPEETLML SMQNLSWDSI PKAEEIIYLR ENSNVSTGGD SIDYTEEMDD
710 720 730 740 750
YFKEIAIRAT QVLDAKICGV DIIVPRETID RDKHAIIELN FNPAMHMHCF
760
PYQGEQKKIG DKILDFLFD
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. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
Links Updated
AL591984 Genomic DNA. Translation: CAD00983.1. Different initiation.
PIRiAI1420.
RefSeqiNP_466292.1. NC_003210.1.

3D structure databases

ProteinModelPortaliQ8Y3R3.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi169963.lmo2770.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

GenoListiLMO2770.

Phylogenomic databases

eggNOGiCOG1181.
HOGENOMiHOG000156471.
KOiK01919.
OrthoDBiEOG6BKJ7H.

Enzyme and pathway databases

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

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]
ProtoNetiSearch...

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 27, 2015
This is version 81 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

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.