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Database: UniProt
Entry: F6CUK3_MARPP
LinkDB: F6CUK3_MARPP
Original site: F6CUK3_MARPP 
ID   F6CUK3_MARPP            Unreviewed;       315 AA.
AC   F6CUK3;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   27-JUL-2011, sequence version 1.
DT   24-JAN-2024, entry version 62.
DE   RecName: Full=Glutathione synthetase {ECO:0000256|HAMAP-Rule:MF_00162};
DE            EC=6.3.2.3 {ECO:0000256|HAMAP-Rule:MF_00162};
DE   AltName: Full=GSH synthetase {ECO:0000256|HAMAP-Rule:MF_00162};
DE            Short=GSH-S {ECO:0000256|HAMAP-Rule:MF_00162};
DE            Short=GSHase {ECO:0000256|HAMAP-Rule:MF_00162};
DE   AltName: Full=Glutathione synthase {ECO:0000256|HAMAP-Rule:MF_00162};
GN   Name=gshB {ECO:0000256|HAMAP-Rule:MF_00162};
GN   OrderedLocusNames=Mar181_3407 {ECO:0000313|EMBL:AEF56423.1};
OS   Marinomonas posidonica (strain CECT 7376 / NCIMB 14433 / IVIA-Po-181).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC   Oceanospirillaceae; Marinomonas.
OX   NCBI_TaxID=491952 {ECO:0000313|EMBL:AEF56423.1, ECO:0000313|Proteomes:UP000009230};
RN   [1] {ECO:0000313|EMBL:AEF56423.1, ECO:0000313|Proteomes:UP000009230}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CECT 7376 / NCIMB 14433 / IVIA-Po-181
RC   {ECO:0000313|Proteomes:UP000009230};
RX   PubMed=23458837; DOI=10.4056/sigs.2976373;
RA   Lucas-Elio P., Goodwin L., Woyke T., Pitluck S., Nolan M., Kyrpides N.C.,
RA   Detter J.C., Copeland A., Lu M., Bruce D., Detter C., Tapia R., Han S.,
RA   Land M.L., Ivanova N., Mikhailova N., Johnston A.W., Sanchez-Amat A.;
RT   "Complete genome sequence of Marinomonas posidonica type strain (IVIA-Po-
RT   181(T)).";
RL   Stand. Genomic Sci. 7:31-43(2012).
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:0000256|HAMAP-
CC         Rule:MF_00162};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|ARBA:ARBA00001936};
CC   -!- PATHWAY: Sulfur metabolism; glutathione biosynthesis; glutathione from
CC       L-cysteine and L-glutamate: step 2/2. {ECO:0000256|HAMAP-
CC       Rule:MF_00162}.
CC   -!- SIMILARITY: Belongs to the prokaryotic GSH synthase family.
CC       {ECO:0000256|HAMAP-Rule:MF_00162}.
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DR   EMBL; CP002771; AEF56423.1; -; Genomic_DNA.
DR   RefSeq; WP_013797889.1; NC_015559.1.
DR   AlphaFoldDB; F6CUK3; -.
DR   STRING; 491952.Mar181_3407; -.
DR   KEGG; mpc:Mar181_3407; -.
DR   eggNOG; COG0189; Bacteria.
DR   HOGENOM; CLU_068239_0_0_6; -.
DR   OrthoDB; 9785415at2; -.
DR   UniPathway; UPA00142; UER00210.
DR   Proteomes; UP000009230; 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; 3.40.50.20; -; 1.
DR   Gene3D; 3.30.1490.20; ATP-grasp fold, A domain; 1.
DR   Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 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   NCBIfam; TIGR01380; glut_syn; 1.
DR   PANTHER; PTHR21621:SF4; GLUTATHIONE SYNTHETASE; 1.
DR   PANTHER; PTHR21621; RIBOSOMAL PROTEIN S6 MODIFICATION PROTEIN; 1.
DR   Pfam; PF02955; GSH-S_ATP; 1.
DR   Pfam; PF02951; GSH-S_N; 1.
DR   SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR   SUPFAM; SSF52440; PreATP-grasp domain; 1.
DR   PROSITE; PS50975; ATP_GRASP; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_00162};
KW   Glutathione biosynthesis {ECO:0000256|ARBA:ARBA00022684, ECO:0000256|HAMAP-
KW   Rule:MF_00162};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_00162};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Manganese {ECO:0000256|ARBA:ARBA00023211};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_00162}.
FT   DOMAIN          125..311
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
SQ   SEQUENCE   315 AA;  35407 MW;  E55E3D506E4743A2 CRC64;
     MTIKLGMVMD PISSINYKKD TSLAMLWAAA EKGWELIYME QKDLFLDNGK AYAMARSLSV
     YKDPKHFYDL GEEERIALGD LDIILMRKDP PFDGEFVYST MILEQAERDG CMVVNDPKSL
     RDCNEKLFAT QFPQCCPPVL VTRRADLLKT FHKEHGDVIF KPLDGMGGTS IFRLKPDDSN
     VSVIIETLTN MGQEQIMAQK FIPEIKQGDK RILVVDGEPV PYALARIPAS GETRGNLAAG
     GRGEGRPLTE RDHWICQQVI PSLKEKGLLF VGLDVIGDYL TEINVTSPTC VRELDNQFDL
     NIAMTLIEAI EKRLT
//
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