SPOT_SYNY3
ID SPOT_SYNY3 Reviewed; 760 AA.
AC P74007;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 25-MAY-2022, entry version 142.
DE RecName: Full=Probable guanosine-3',5'-bis(diphosphate) 3'-pyrophosphohydrolase;
DE EC=3.1.7.2;
DE AltName: Full=Penta-phosphate guanosine-3'-pyrophosphohydrolase;
DE Short=(ppGpp)ase;
GN Name=spoT; OrderedLocusNames=slr1325;
OS Synechocystis sp. (strain PCC 6803 / Kazusa).
OC Bacteria; Cyanobacteria; Synechococcales; Merismopediaceae; Synechocystis;
OC unclassified 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., Hosouchi T.,
RA Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence analysis of the genome of the unicellular cyanobacterium
RT Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT genome and assignment of potential protein-coding regions.";
RL DNA Res. 3:109-136(1996).
CC -!- FUNCTION: In eubacteria ppGpp (guanosine 3'-diphosphate 5'-diphosphate)
CC is a mediator of the stringent response that coordinates a variety of
CC cellular activities in response to changes in nutritional abundance.
CC This enzyme catalyzes the degradation of ppGpp into GDP. It may also be
CC capable of catalyzing the synthesis of ppGpp (By similarity).
CC {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=guanosine 3',5'-bis(diphosphate) + H2O = diphosphate + GDP +
CC H(+); Xref=Rhea:RHEA:14253, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:58189, ChEBI:CHEBI:77828; EC=3.1.7.2;
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC -!- PATHWAY: Purine metabolism; ppGpp biosynthesis; ppGpp from GDP: step
CC 1/1.
CC -!- SIMILARITY: Belongs to the RelA/SpoT family. {ECO:0000305}.
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DR EMBL; BA000022; BAA18078.1; -; Genomic_DNA.
DR PIR; S75517; S75517.
DR AlphaFoldDB; P74007; -.
DR SMR; P74007; -.
DR IntAct; P74007; 3.
DR STRING; 1148.1653162; -.
DR PaxDb; P74007; -.
DR EnsemblBacteria; BAA18078; BAA18078; BAA18078.
DR KEGG; syn:slr1325; -.
DR eggNOG; COG0317; Bacteria.
DR InParanoid; P74007; -.
DR OMA; DWISSPK; -.
DR PhylomeDB; P74007; -.
DR UniPathway; UPA00908; UER00886.
DR Proteomes; UP000001425; Chromosome.
DR GO; GO:0008893; F:guanosine-3',5'-bis(diphosphate) 3'-diphosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0015970; P:guanosine tetraphosphate biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd00077; HDc; 1.
DR CDD; cd05399; NT_Rel-Spo_like; 1.
DR CDD; cd01668; TGS_RSH; 1.
DR Gene3D; 3.10.20.30; -; 1.
DR Gene3D; 3.30.460.10; -; 1.
DR InterPro; IPR045865; ACT-like_dom_sf.
DR InterPro; IPR002912; ACT_dom.
DR InterPro; IPR012675; Beta-grasp_dom_sf.
DR InterPro; IPR003607; HD/PDEase_dom.
DR InterPro; IPR006674; HD_domain.
DR InterPro; IPR043519; NT_sf.
DR InterPro; IPR004811; RelA/Spo_fam.
DR InterPro; IPR045600; RelA/SpoT_AH_RIS.
DR InterPro; IPR007685; RelA_SpoT.
DR InterPro; IPR004095; TGS.
DR InterPro; IPR012676; TGS-like.
DR InterPro; IPR033655; TGS_RelA/SpoT.
DR Pfam; PF13291; ACT_4; 1.
DR Pfam; PF19296; DUF5913; 1.
DR Pfam; PF04607; RelA_SpoT; 1.
DR Pfam; PF02824; TGS; 1.
DR SMART; SM00471; HDc; 1.
DR SMART; SM00954; RelA_SpoT; 1.
DR SUPFAM; SSF55021; SSF55021; 1.
DR SUPFAM; SSF81271; SSF81271; 1.
DR SUPFAM; SSF81301; SSF81301; 1.
DR TIGRFAMs; TIGR00691; spoT_relA; 1.
DR PROSITE; PS51671; ACT; 1.
DR PROSITE; PS51831; HD; 1.
DR PROSITE; PS51880; TGS; 1.
PE 3: Inferred from homology;
KW Hydrolase; Manganese; Reference proteome.
FT CHAIN 1..760
FT /note="Probable guanosine-3',5'-bis(diphosphate) 3'-
FT pyrophosphohydrolase"
FT /id="PRO_0000166576"
FT DOMAIN 76..175
FT /note="HD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01175"
FT DOMAIN 421..482
FT /note="TGS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01228"
FT DOMAIN 685..759
FT /note="ACT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01007"
FT REGION 585..614
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 585..599
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 760 AA; 86569 MW; CA276EA2286358F7 CRC64;
MNAVAALPTP TIHTTCAQDI HDIELPQWLE DCLQQWQREI EQGQDETTAP HCLICRAFCF
AYDLHAQQRR KSGEPYIAHP VAVAGLLRDL GGDEAMIAAG FLHDVVEDTD ISIEQIEALF
GEETASLVEG VTKLSKFNFS STTEHQAENF RRMFLAMAKD IRVIVVKLAD RLHNMRTLDA
LSPEKQRRIA RETKDIFAPL ANRLGIWRFK WELEDLSFKY LEPDSYRKIQ SLVVEKRGDR
ESRLETVKDM LRFRLRDEGI EHFELQGRPK HLYGIYYKMT SQDKAFEEIY DIAALRIIVE
SKGECYRALS VVHDVFKPIP GRFKDYIGLP KPNRYQSLHT TVLGLTSRPL EIQIRTEEMH
HVAEYGIAAH WKYKESGGSE NATLTSTDEK FTWLRQLLDW QSDLKDAQEY VENLKQNLFD
DDVYVFTPKG EVISLARGAT PVDFAYRIHT EVGHHMKGAR VNGQWLGVDT RLKNGDIVEI
VTQKNSHPSL DWLNFVVTPS ARHRIRQWFK RSRRDENILR GRELLEKELG KTGLEALLKS
EPMQKTAERC NYQNVEDLLA GLGYGEITSN SVVNRLRENN VNNVKNSQSS QEVTLASSPQ
VHPPTPPATG KDNSPIAGIE GLLYHIAGCC HPLPGEPIMG VVTRGARGIS IHRQGCHNLE
QMDGDRLIPV RWNPNTNNHQ TYPVDIVIEA IDRVGVLKDI LSRLSDNHIN VRNADVKTHL
GRPAIISLKI DIHDYQQLLG IMAKIKNMSD VMDLRRVISG
