ID Q0C5G2_HYPNA Unreviewed; 316 AA.
AC Q0C5G2;
DT 17-OCT-2006, integrated into UniProtKB/TrEMBL.
DT 17-OCT-2006, sequence version 1.
DT 27-MAR-2024, entry version 124.
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:ABI75773.1};
GN OrderedLocusNames=HNE_0301 {ECO:0000313|EMBL:ABI75773.1};
OS Hyphomonas neptunium (strain ATCC 15444).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomonadales;
OC Hyphomonadaceae; Hyphomonas.
OX NCBI_TaxID=228405 {ECO:0000313|EMBL:ABI75773.1, ECO:0000313|Proteomes:UP000001959};
RN [1] {ECO:0000313|EMBL:ABI75773.1, ECO:0000313|Proteomes:UP000001959}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15444 {ECO:0000313|EMBL:ABI75773.1,
RC ECO:0000313|Proteomes:UP000001959};
RX PubMed=16980487; DOI=10.1128/JB.00111-06;
RA Badger J.H., Hoover T.R., Brun Y.V., Weiner R.M., Laub M.T., Alexandre G.,
RA Mrazek J., Ren Q., Paulsen I.T., Nelson K.E., Khouri H.M., Radune D.,
RA Sosa J., Dodson R.J., Sullivan S.A., Rosovitz M.J., Madupu R.,
RA Brinkac L.M., Durkin A.S., Daugherty S.C., Kothari S.P., Giglio M.G.,
RA Zhou L., Haft D.H., Selengut J.D., Davidsen T.M., Yang Q., Zafar N.,
RA Ward N.L.;
RT "Comparative genomic evidence for a close relationship between the
RT dimorphic prosthecate bacteria Hyphomonas neptunium and Caulobacter
RT crescentus.";
RL J. Bacteriol. 188:6841-6850(2006).
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; CP000158; ABI75773.1; -; Genomic_DNA.
DR RefSeq; WP_011645331.1; NC_008358.1.
DR AlphaFoldDB; Q0C5G2; -.
DR STRING; 228405.HNE_0301; -.
DR KEGG; hne:HNE_0301; -.
DR eggNOG; COG0189; Bacteria.
DR HOGENOM; CLU_068239_0_0_5; -.
DR UniPathway; UPA00142; UER00210.
DR Proteomes; UP000001959; 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:UP000001959}.
FT DOMAIN 125..310
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 316 AA; 34476 MW; D65BC52EDE6C1969 CRC64;
MTLRIAIQMD PLERVNIDGD TSFALAEVAQ ARGADIFVYG PGDLSFREGR VTAWARPAKV
QRVRETPGIF GPHQRLDIAR DVDVVLMRQD PPFDMAYITA CHLLESVTNQ TLVVNDPAGV
RSSPEKIFPL MFPEIMPPTL VTRDRQVIDA FREEYRDIIV KPLHGHGGAG VFRLKHDDSN
LDSLLELFFA RSPEPLMVQA FLPAVSEGDK RIILIDGEPV GAINRRPKAG QVRSNLVVGG
TAEATELSGA DKNICEAIGP ELRRRGLTLT GIDVIGGRLT EVNVTSPTGV QALKRLSGID
AAAKFWDVVQ AKLAAA
//
