GSHB_GLOVI
ID GSHB_GLOVI Reviewed; 324 AA.
AC Q7NF44;
DT 15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Glutathione synthetase {ECO:0000255|HAMAP-Rule:MF_00162};
DE EC=6.3.2.3 {ECO:0000255|HAMAP-Rule:MF_00162};
DE AltName: Full=GSH synthetase {ECO:0000255|HAMAP-Rule:MF_00162};
DE Short=GSH-S {ECO:0000255|HAMAP-Rule:MF_00162};
DE Short=GSHase {ECO:0000255|HAMAP-Rule:MF_00162};
DE AltName: Full=Glutathione synthase {ECO:0000255|HAMAP-Rule:MF_00162};
GN Name=gshB {ECO:0000255|HAMAP-Rule:MF_00162}; OrderedLocusNames=gll3682;
OS Gloeobacter violaceus (strain ATCC 29082 / PCC 7421).
OC Bacteria; Cyanobacteria; Gloeobacteria; Gloeobacterales; Gloeobacteraceae;
OC Gloeobacter.
OX NCBI_TaxID=251221;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29082 / PCC 7421;
RX PubMed=14621292; DOI=10.1093/dnares/10.4.137;
RA Nakamura Y., Kaneko T., Sato S., Mimuro M., Miyashita H., Tsuchiya T.,
RA Sasamoto S., Watanabe A., Kawashima K., Kishida Y., Kiyokawa C., Kohara M.,
RA Matsumoto M., Matsuno A., Nakazaki N., Shimpo S., Takeuchi C., Yamada M.,
RA Tabata S.;
RT "Complete genome structure of Gloeobacter violaceus PCC 7421, a
RT cyanobacterium that lacks thylakoids.";
RL DNA Res. 10:137-145(2003).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + gamma-L-glutamyl-L-cysteine + glycine = ADP +
CC glutathione + H(+) + phosphate; Xref=Rhea:RHEA:13557,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:57305, ChEBI:CHEBI:57925, ChEBI:CHEBI:58173,
CC ChEBI:CHEBI:456216; EC=6.3.2.3; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_00162};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC Note=Binds 1 Mg(2+) or Mn(2+) ion per subunit. {ECO:0000250};
CC -!- PATHWAY: Sulfur metabolism; glutathione biosynthesis; glutathione from
CC L-cysteine and L-glutamate: step 2/2. {ECO:0000255|HAMAP-
CC Rule:MF_00162}.
CC -!- SIMILARITY: Belongs to the prokaryotic GSH synthase family.
CC {ECO:0000255|HAMAP-Rule:MF_00162}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BA000045; BAC91623.1; -; Genomic_DNA.
DR RefSeq; NP_926628.1; NC_005125.1.
DR RefSeq; WP_011143671.1; NC_005125.1.
DR AlphaFoldDB; Q7NF44; -.
DR SMR; Q7NF44; -.
DR STRING; 251221.35214254; -.
DR EnsemblBacteria; BAC91623; BAC91623; BAC91623.
DR KEGG; gvi:gll3682; -.
DR PATRIC; fig|251221.4.peg.3716; -.
DR eggNOG; COG0189; Bacteria.
DR HOGENOM; CLU_068239_0_0_3; -.
DR InParanoid; Q7NF44; -.
DR OMA; WMRKDPP; -.
DR OrthoDB; 878336at2; -.
DR PhylomeDB; Q7NF44; -.
DR UniPathway; UPA00142; UER00210.
DR Proteomes; UP000000557; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004363; F:glutathione synthase activity; IBA:GO_Central.
DR GO; GO:0016879; F:ligase activity, forming carbon-nitrogen bonds; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 3.30.1490.20; -; 1.
DR HAMAP; MF_00162; GSH_S; 1.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
DR InterPro; IPR006284; Glut_synth_pro.
DR InterPro; IPR004218; GSHS_ATP-bd.
DR InterPro; IPR004215; GSHS_N.
DR InterPro; IPR016185; PreATP-grasp_dom_sf.
DR PANTHER; PTHR21621:SF4; PTHR21621:SF4; 1.
DR Pfam; PF02955; GSH-S_ATP; 1.
DR Pfam; PF02951; GSH-S_N; 1.
DR SUPFAM; SSF52440; SSF52440; 1.
DR TIGRFAMs; TIGR01380; glut_syn; 1.
DR PROSITE; PS50975; ATP_GRASP; 1.
PE 3: Inferred from homology;
KW ATP-binding; Glutathione biosynthesis; Ligase; Magnesium; Manganese;
KW Metal-binding; Nucleotide-binding; Reference proteome.
FT CHAIN 1..324
FT /note="Glutathione synthetase"
FT /id="PRO_0000197468"
FT DOMAIN 129..313
FT /note="ATP-grasp"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00162"
FT BINDING 155..211
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00162"
FT BINDING 284
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00162"
FT BINDING 286
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00162"
SQ SEQUENCE 324 AA; 35906 MW; 7D3277C55E838EAF CRC64;
MKILFIVDPL ETLKPGHDTS VALMQAAARR GHSVWAAEVG DLQVHHHRAA AQVRTLTIHP
GRTPFYTVEA VGFYPLSEAD VIWMRKDPPV TSAYLWATQV LDLVNAGRGD GRTTFVLNRP
SGLRNDNEKL YALHFPDLVP ETRVCTHRQD ILDFVDIHGR AVIKPLDGKG GEGIFLLARA
DRNLNAIIEA STAYGTRHVM VQRYLEESRQ GDKRIVLLAG EPIGALLRVP REDDVRGNMA
AGGRVVKTTL TERDREICRV VGPRLVADGH YFVGIDVIGA YLTEINVTSP TGICEIDVLD
GVVLEDEIVD WLVEYTRPAL ARNL