UniProt: N1MRD5

Database: UniProt
Entry: N1MRD5_9SPHN

LinkDB:  N1MRD5_9SPHN 
Original site:  N1MRD5_9SPHN

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Ontology (3)   
   GO (3)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (9)   
   InterPro (6)   
   Pfam (2)   
   PROSITE (1)   
All databases (15)   

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ID   N1MRD5_9SPHN            Unreviewed;       324 AA.
AC   N1MRD5;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   24-JAN-2024, entry version 48.
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=EBBID32_36600 {ECO:0000313|EMBL:CCW19294.1};
OS   Sphingobium indicum BiD32.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingobium.
OX   NCBI_TaxID=1301087 {ECO:0000313|EMBL:CCW19294.1, ECO:0000313|Proteomes:UP000013201};
RN   [1] {ECO:0000313|EMBL:CCW19294.1, ECO:0000313|Proteomes:UP000013201}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BiD32 {ECO:0000313|EMBL:CCW19294.1,
RC   ECO:0000313|Proteomes:UP000013201};
RA   Le V.;
RL   Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:CCW19294.1, ECO:0000313|Proteomes:UP000013201}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BiD32 {ECO:0000313|EMBL:CCW19294.1,
RC   ECO:0000313|Proteomes:UP000013201};
RA   Nielsen J.L., Zhou N.A., Kjeldal H.;
RT   "Bisphenol A degrading Sphingobium sp. strain BiD32.";
RL   Submitted (APR-2013) 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}.
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:CCW19294.1}.
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DR   EMBL; CAVK010000185; CCW19294.1; -; Genomic_DNA.
DR   RefSeq; WP_006962648.1; NZ_CAVK010000185.1.
DR   AlphaFoldDB; N1MRD5; -.
DR   OrthoDB; 9785415at2; -.
DR   UniPathway; UPA00142; UER00210.
DR   Proteomes; UP000013201; 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:UP000013201}.
FT   DOMAIN          130..315
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
SQ   SEQUENCE   324 AA;  35042 MW;  FDA919559E29CC95 CRC64;
     MTQLNPLTVA VQMDPMEGIK IAGDSTFHIM LAGQARGHRL YHYLAPDLTY RDGRVLAKAR
     PVNVQKVEGD HFAFGEAEML DLGRDVDVVL MRQDPPFDLS YITATHLLER VQEETLVVND
     PASVRNAPEK LFVLDYARFM PPTMITRDLA EVRSFLAQHG EIVVKPLYGN AGNAVFHVGP
     KGSNLSALVE IFNASWVEPF MVQAFIPGVA QGDKRIVLID GEVAGAINRI PGVGEIRSNL
     AVGGSAAKTV LTDKEREICA AMGPELKARG LLFVGIDVIG GEWLTEINVT SPTGIVSIDA
     FDGTDTGGLI WDAIDARLAA RAAD
//

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