GSHB_NOSS1
ID GSHB_NOSS1 Reviewed; 324 AA.
AC P45480; Q43879;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2002, sequence version 2.
DT 03-AUG-2022, entry version 121.
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}; Synonyms=gsh-II;
GN OrderedLocusNames=all3859;
OS Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576).
OC Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Nostoc.
OX NCBI_TaxID=103690;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7557485; DOI=10.1016/0378-1119(95)00416-4;
RA Doherty H.M., Adams D.G.;
RT "Cloning and sequence of ftsZ and flanking regions from the cyanobacterium
RT Anabaena PCC 7120.";
RL Gene 163:93-96(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7120 / SAG 25.82 / UTEX 2576;
RX PubMed=11759840; DOI=10.1093/dnares/8.5.205;
RA Kaneko T., Nakamura Y., Wolk C.P., Kuritz T., Sasamoto S., Watanabe A.,
RA Iriguchi M., Ishikawa A., Kawashima K., Kimura T., Kishida Y., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakazaki N., Shimpo S., Sugimoto M.,
RA Takazawa M., Yamada M., Yasuda M., Tabata S.;
RT "Complete genomic sequence of the filamentous nitrogen-fixing
RT cyanobacterium Anabaena sp. strain PCC 7120.";
RL DNA Res. 8:205-213(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 24-324.
RX PubMed=8525061; DOI=10.1016/0923-2508(96)80290-7;
RA Zhang C.C., Huguenin S., Friry A.;
RT "Analysis of genes encoding the cell division protein FtsZ and a
RT glutathione synthetase homologue in the cyanobacterium Anabaena sp. PCC
RT 7120.";
RL Res. Microbiol. 146:445-455(1995).
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}.
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DR EMBL; U14408; AAA85527.1; -; Genomic_DNA.
DR EMBL; BA000019; BAB75558.1; -; Genomic_DNA.
DR EMBL; Z31371; CAA83242.1; -; Genomic_DNA.
DR PIR; AD2288; AD2288.
DR PIR; JC4291; JC4291.
DR RefSeq; WP_010998000.1; NZ_RSCN01000011.1.
DR AlphaFoldDB; P45480; -.
DR SMR; P45480; -.
DR STRING; 103690.17132993; -.
DR EnsemblBacteria; BAB75558; BAB75558; BAB75558.
DR KEGG; ana:all3859; -.
DR eggNOG; COG0189; Bacteria.
DR OMA; WMRKDPP; -.
DR OrthoDB; 878336at2; -.
DR UniPathway; UPA00142; UER00210.
DR Proteomes; UP000002483; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004363; F:glutathione synthase activity; IEA:UniProtKB-UniRule.
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_0000197452"
FT DOMAIN 133..317
FT /note="ATP-grasp"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00162"
FT BINDING 159..215
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00162"
FT BINDING 288
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00162"
FT BINDING 290
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00162"
FT CONFLICT 50
FT /note="W -> C (in Ref. 1; AAA85527)"
FT /evidence="ECO:0000305"
FT CONFLICT 243
FT /note="M -> V (in Ref. 3; CAA83242)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 324 AA; 35953 MW; 03C6E7E8481DD8D1 CRC64;
MKLAFIIDPI HQLDPCHDTS VALMEAAQIL GHEVWVTQAN WLSVVDSKAW AILQQVELVP
VQLIDGRWVA ASPWYTLNTR SFSSLETMDA VFMRTDPPVN DAYLYATYVL DYVDQRKTLV
INNPNGIRGA NEKMYALQFT KAIPETIVSA DKDFIRQFVE AKGATVLKPL GNKAGEGILF
LQAGDRNFNS IVELSTQQGR LPVMVQTYLP EAKEGDKRII LLNGEPIGAL NRLASGSDFR
NNMATGGTVA KTEITPREEE ICSQIAANLR QDGLIFVGID VIGGYLTEVN VTSPTGIREI
DRLDGTRLAH QVIQWVEKNL QIQN
