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Database: UniProt
Entry: H5TDI4_9ALTE
LinkDB: H5TDI4_9ALTE
Original site: H5TDI4_9ALTE 
ID   H5TDI4_9ALTE            Unreviewed;       315 AA.
AC   H5TDI4;
DT   18-APR-2012, integrated into UniProtKB/TrEMBL.
DT   18-APR-2012, sequence version 1.
DT   24-JAN-2024, entry version 52.
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   ECO:0000313|EMBL:GAB56361.1};
GN   ORFNames=GPUN_2246 {ECO:0000313|EMBL:GAB56361.1};
OS   Glaciecola punicea ACAM 611.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Alteromonadaceae; Glaciecola.
OX   NCBI_TaxID=1121923 {ECO:0000313|EMBL:GAB56361.1, ECO:0000313|Proteomes:UP000053586};
RN   [1] {ECO:0000313|EMBL:GAB56361.1, ECO:0000313|Proteomes:UP000053586}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ACAM 611 {ECO:0000313|EMBL:GAB56361.1,
RC   ECO:0000313|Proteomes:UP000053586};
RX   PubMed=22628500; DOI=10.1128/JB.00463-12;
RA   Qin Q.-L., Xie B.-B., Shu Y.-L., Rong J.-C., Zhao D.-L., Zhang X.-Y.,
RA   Chen X.-L., Zhou B.-C., Zhanga Y.-Z.;
RT   "Genome sequence of proteorhodopsin-containing sea ice bacterium Glaciecola
RT   punicea ACAM 611T.";
RL   J. Bacteriol. 194:3267-3267(2012).
RN   [2] {ECO:0000313|EMBL:GAB56361.1, ECO:0000313|Proteomes:UP000053586}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ACAM 611 {ECO:0000313|EMBL:GAB56361.1,
RC   ECO:0000313|Proteomes:UP000053586};
RX   PubMed=25009843;
RA   Qin Q.-L., Xie B.-B., Yu Y., Shu Y.-L., Rong J.-C., Zhang Y.-J.,
RA   Zhao D.-L., Chen X.-L., Zhang X.-Y., Chen B., Zhou B.-C., Zhang Y.-Z.;
RT   "Comparative genomics of the marine bacterial genus Glaciecola reveals the
RT   high degree of genomic diversity and genomic characteristic for cold
RT   adaptation.";
RL   Environ. Microbiol. 16:1642-1653(2014).
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:GAB56361.1}.
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DR   EMBL; BAET01000028; GAB56361.1; -; Genomic_DNA.
DR   RefSeq; WP_006006433.1; NZ_BAET01000028.1.
DR   AlphaFoldDB; H5TDI4; -.
DR   STRING; 56804.BAE46_05080; -.
DR   eggNOG; COG0189; Bacteria.
DR   OrthoDB; 9785415at2; -.
DR   UniPathway; UPA00142; UER00210.
DR   Proteomes; UP000053586; Unassembled WGS sequence.
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}; Reference proteome {ECO:0000313|Proteomes:UP000053586}.
FT   DOMAIN          126..311
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
SQ   SEQUENCE   315 AA;  34965 MW;  EAC8A67DECD45192 CRC64;
     MTIKLGIVMD PIESINIKKD TTFAMMLEAQ KRGYEIYYMQ IGDLYITNGQ PRATVTRISV
     QEKASDYYSI LAQDDICLGD LTVLLMRKDP PVDSQFIYAT HIFSLAKDLG TLVVNDPQAL
     RDFNEKLFTS LYSDFIPPTL VTSNKERIKA FHAAHKDIIV KPLDGMGGTS IFRVKEDGVN
     LGVICEIITS NESVHAMVQA YMPEIKLGDK RILLVDGEVI PYCLARLPSG NETRGNLAAG
     GIGQSQQVNQ QDMQVAQAIA KDMPDRGILF VGLDMIGNKV TEINITSPTC VREIEAAYDI
     NICAKLFDAI EKRLH
//
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