GSHB_PROMP
ID GSHB_PROMP Reviewed; 307 AA.
AC Q7TUG9;
DT 15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 104.
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=PMM0178;
OS Prochlorococcus marinus subsp. pastoris (strain CCMP1986 / NIES-2087 /
OS MED4).
OC Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC Prochlorococcus.
OX NCBI_TaxID=59919;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCMP1986 / NIES-2087 / MED4;
RX PubMed=12917642; DOI=10.1038/nature01947;
RA Rocap G., Larimer F.W., Lamerdin J.E., Malfatti S., Chain P., Ahlgren N.A.,
RA Arellano A., Coleman M., Hauser L., Hess W.R., Johnson Z.I., Land M.L.,
RA Lindell D., Post A.F., Regala W., Shah M., Shaw S.L., Steglich C.,
RA Sullivan M.B., Ting C.S., Tolonen A., Webb E.A., Zinser E.R.,
RA Chisholm S.W.;
RT "Genome divergence in two Prochlorococcus ecotypes reflects oceanic niche
RT differentiation.";
RL Nature 424:1042-1047(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}.
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DR EMBL; BX548174; CAE18637.1; -; Genomic_DNA.
DR RefSeq; WP_011131817.1; NC_005072.1.
DR AlphaFoldDB; Q7TUG9; -.
DR SMR; Q7TUG9; -.
DR STRING; 59919.PMM0178; -.
DR EnsemblBacteria; CAE18637; CAE18637; PMM0178.
DR KEGG; pmm:PMM0178; -.
DR eggNOG; COG0189; Bacteria.
DR HOGENOM; CLU_068239_0_0_3; -.
DR OMA; WMRKDPP; -.
DR OrthoDB; 878336at2; -.
DR UniPathway; UPA00142; UER00210.
DR Proteomes; UP000001026; 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.
FT CHAIN 1..307
FT /note="Glutathione synthetase"
FT /id="PRO_0000197475"
FT DOMAIN 120..304
FT /note="ATP-grasp"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00162"
FT BINDING 146..202
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00162"
FT BINDING 275
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00162"
FT BINDING 277
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00162"
SQ SEQUENCE 307 AA; 34254 MW; 76EC5F13BDE80B24 CRC64;
MKFLFVVDPI KNINPLKDSS AALMQASSKK KIEVWICTPQ DLEARGDEVW ASSWRAEVCP
WVSFKENKCI PLAEFNCIWM RKDPPVNEGY LYATHLLEVA ERKGVKVINK PSSLRAWNEK
LGALRYSHLM APTIVASKVK DLINFAQINH DVVVKPLGGK GGQGVIRLTK DSPGIKAMIE
LITSQEQLPV MMQKFIPEVK EGDKRIIIVN GEPIGSINRI PQGGDFRSNL AMGGKAEKTN
LTAKEKKICT ELSQHFKDEG LFFVGIDVIN EMLSEINVTS PTGLREIETL SNKSVSDKVI
EKLLEII
