ID GSHB_SYNY3 Reviewed; 320 AA.
AC P73493;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 01-MAY-2013, entry version 88.
DE RecName: Full=Glutathione synthetase;
DE EC=6.3.2.3;
DE AltName: Full=GSH synthetase;
DE Short=GSH-S;
DE Short=GSHase;
DE AltName: Full=Glutathione synthase;
GN Name=gshB; OrderedLocusNames=slr1238;
OS Synechocystis sp. (strain PCC 6803 / Kazusa).
OC Bacteria; Cyanobacteria; Oscillatoriophycideae; Chroococcales;
OC Synechocystis.
OX NCBI_TaxID=1111708;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 6803 / Kazusa;
RX PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T.,
RA Hosouchi T., Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S.,
RA Shimpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M.,
RA Tabata S.;
RT "Sequence analysis of the genome of the unicellular cyanobacterium
RT Synechocystis sp. strain PCC6803. II. Sequence determination of the
RT entire genome and assignment of potential protein-coding regions.";
RL DNA Res. 3:109-136(1996).
CC -!- CATALYTIC ACTIVITY: ATP + gamma-L-glutamyl-L-cysteine + glycine =
CC ADP + phosphate + glutathione.
CC -!- COFACTOR: Binds 1 magnesium or manganese ion per subunit (By
CC similarity).
CC -!- PATHWAY: Sulfur metabolism; glutathione biosynthesis; glutathione
CC from L-cysteine and L-glutamate: step 2/2.
CC -!- SIMILARITY: Belongs to the prokaryotic GSH synthase family.
CC -!- SIMILARITY: Contains 1 ATP-grasp domain.
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DR EMBL; BA000022; BAA17533.1; -; Genomic_DNA.
DR PIR; S77430; S77430.
DR RefSeq; NP_440853.1; NC_000911.1.
DR RefSeq; YP_005650912.1; NC_017277.1.
DR RefSeq; YP_007450736.1; NC_020286.1.
DR ProteinModelPortal; P73493; -.
DR IntAct; P73493; 1.
DR STRING; 1148.slr1238; -.
DR PaxDb; P73493; -.
DR EnsemblBacteria; BAA17533; BAA17533; BAA17533.
DR GeneID; 12254916; -.
DR GeneID; 14616388; -.
DR GeneID; 954156; -.
DR KEGG; syn:slr1238; -.
DR KEGG; syy:SYNGTS_0959; -.
DR PATRIC; 23838946; VBISynSp132158_1038.
DR eggNOG; COG0189; -.
DR HOGENOM; HOG000265022; -.
DR KO; K01920; -.
DR OMA; WMRKDPP; -.
DR ProtClustDB; PRK05246; -.
DR UniPathway; UPA00142; UER00210.
DR GO; GO:0005829; C:cytosol; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:HAMAP.
DR GO; GO:0004363; F:glutathione synthase activity; IEA:HAMAP.
DR GO; GO:0000287; F:magnesium ion binding; IEA:HAMAP.
DR GO; GO:0030145; F:manganese ion binding; IEA:HAMAP.
DR Gene3D; 3.30.1490.20; -; 1.
DR Gene3D; 3.30.470.20; -; 1.
DR Gene3D; 3.40.50.20; -; 1.
DR HAMAP; MF_00162; GSH-S; 1; -.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
DR InterPro; IPR013816; ATP_grasp_subdomain_2.
DR InterPro; IPR006284; Glut_synth_pro.
DR InterPro; IPR004218; GSHS_ATP-bd.
DR InterPro; IPR004215; GSHS_N.
DR InterPro; IPR016185; PreATP-grasp_dom.
DR Pfam; PF02955; GSH-S_ATP; 1.
DR Pfam; PF02951; GSH-S_N; 1.
DR SUPFAM; SSF52440; PreATP-grasp-like; 1.
DR TIGRFAMs; TIGR01380; glut_syn; 1.
DR PROSITE; PS50975; ATP_GRASP; 1.
PE 3: Inferred from homology;
KW ATP-binding; Complete proteome; Glutathione biosynthesis; Ligase;
KW Magnesium; Manganese; Metal-binding; Nucleotide-binding;
KW Reference proteome.
FT CHAIN 1 320 Glutathione synthetase.
FT /FTId=PRO_0000197490.
FT DOMAIN 133 317 ATP-grasp.
FT NP_BIND 159 215 ATP (By similarity).
FT METAL 288 288 Magnesium or manganese (By similarity).
FT METAL 290 290 Magnesium or manganese (By similarity).
SQ SEQUENCE 320 AA; 35069 MW; 6C7BD439A23D185A CRC64;
MKLAFIIDPL EKLDPGHDST VAIMEAAQKL GHEVFVTSVG DLAVINGQAW AKLAAVRLQP
VILVDGHWQV SQPWSELSKS QWMALTECQA VFMRKDPPVT VQYLYATFIL ELLAPTKTMV
INSPQGLREA NEKMYTLQFA AVMPPTVVSL DKGLIRQFLE EHGAAVLKPL GGKAGEGILF
LDPGDRNFNS LVEISTQHGK EPVMVQRFLP EAKEGDKRII LLDGDPIGAV NRIPSGAEFR
GNMAVGGQVA PTTITSREIE ICALLKPKLQ ADGLYFVGID VIGGYLTEVN VTSPTGIREI
DRLEGVRLGE KVICWLEKQF
//
