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Database: UniProt
Entry: A0A0G3XMI3_9SPHN
LinkDB: A0A0G3XMI3_9SPHN
Original site: A0A0G3XMI3_9SPHN 
ID   A0A0G3XMI3_9SPHN        Unreviewed;       322 AA.
AC   A0A0G3XMI3;
DT   16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT   16-SEP-2015, sequence version 1.
DT   24-JAN-2024, entry version 32.
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   ORFNames=AB433_08485 {ECO:0000313|EMBL:AKM11673.1};
OS   Croceicoccus naphthovorans.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Erythrobacteraceae; Croceicoccus.
OX   NCBI_TaxID=1348774 {ECO:0000313|EMBL:AKM11673.1, ECO:0000313|Proteomes:UP000035287};
RN   [1] {ECO:0000313|EMBL:AKM11673.1, ECO:0000313|Proteomes:UP000035287}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PQ-2 {ECO:0000313|EMBL:AKM11673.1,
RC   ECO:0000313|Proteomes:UP000035287};
RA   Zeng Y., Huang Y.;
RL   Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
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; CP011770; AKM11673.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G3XMI3; -.
DR   STRING; 1348774.AB433_08485; -.
DR   KEGG; cna:AB433_08485; -.
DR   PATRIC; fig|1348774.3.peg.1779; -.
DR   OrthoDB; 9785415at2; -.
DR   UniPathway; UPA00142; UER00210.
DR   Proteomes; UP000035287; 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}; Reference proteome {ECO:0000313|Proteomes:UP000035287}.
FT   DOMAIN          123..313
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
SQ   SEQUENCE   322 AA;  35385 MW;  1718395BFE89E1CC CRC64;
     MDPMESIGIA GDSSFALMLS AQARGYELFH YDVRTLAWKS DGQGGGRVTA WAAPVTVQRV
     EGDHFTMGEH RTIDLGRDVD VVLMRQDPPF DIGYLTGTWL LERIKGETLV INDPVSVRDA
     PEKVYVLDFA RFMPPTLITR RIEDVREFQR EHRDWSGGAI VMKPLHGNGG KAVFKVDAEG
     SNLSALVEIF NQTWPEPFMV QPFLPDVSLG DKRIVLVDGE VAGAINRLPG EGEFRSNLAQ
     GGSAEATELT ETEQEICAAM GPELKKLGLV FVGIDVIGGR WLTEINVTSP TGIVAIDRFN
     GTDTSGMIWN AIERRIAERA AT
//
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