ID S6HMI7_9GAMM Unreviewed; 702 AA.
AC S6HMI7;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=guanosine-3',5'-bis(diphosphate) 3'-diphosphatase {ECO:0000256|ARBA:ARBA00024387};
DE EC=3.1.7.2 {ECO:0000256|ARBA:ARBA00024387};
GN ORFNames=OFPI_18970 {ECO:0000313|EMBL:EPJ50843.1};
OS Osedax symbiont Rs2.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Oceanospirillaceae.
OX NCBI_TaxID=1330035 {ECO:0000313|EMBL:EPJ50843.1, ECO:0000313|Proteomes:UP000014830};
RN [1] {ECO:0000313|EMBL:EPJ50843.1, ECO:0000313|Proteomes:UP000014830}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Rs2 {ECO:0000313|Proteomes:UP000014830};
RA Yi H., Goffredi S.;
RT "Comparative genomics of two novel heterotrophic symbionts of deep-sea
RT Osedax worms: functional variation and environmental selection.";
RL Submitted (MAY-2013) to the EMBL/GenBank/DDBJ databases.
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 {ECO:0000256|RuleBase:RU003847}.
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 Evidence={ECO:0000256|ARBA:ARBA00024273};
CC -!- PATHWAY: Purine metabolism; ppGpp biosynthesis; ppGpp from GDP: step
CC 1/1. {ECO:0000256|ARBA:ARBA00024329}.
CC -!- SIMILARITY: Belongs to the relA/spoT family.
CC {ECO:0000256|RuleBase:RU003847}.
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:EPJ50843.1}.
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DR EMBL; ASZI01000136; EPJ50843.1; -; Genomic_DNA.
DR AlphaFoldDB; S6HMI7; -.
DR PATRIC; fig|1330035.3.peg.1805; -.
DR UniPathway; UPA00908; UER00886.
DR Proteomes; UP000014830; Unassembled WGS sequence.
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; 3.30.70.260; -; 1.
DR Gene3D; 3.30.460.10; Beta Polymerase, domain 2; 1.
DR Gene3D; 1.10.3210.10; Hypothetical protein af1432; 1.
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 NCBIfam; TIGR00691; spoT_relA; 1.
DR PANTHER; PTHR21262:SF31; BIFUNCTIONAL (P)PPGPP SYNTHASE_HYDROLASE SPOT; 1.
DR PANTHER; PTHR21262; GUANOSINE-3',5'-BIS DIPHOSPHATE 3'-PYROPHOSPHOHYDROLASE; 1.
DR Pfam; PF13291; ACT_4; 1.
DR Pfam; PF13328; HD_4; 1.
DR Pfam; PF19296; RelA_AH_RIS; 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; SSF109604; HD-domain/PDEase-like; 1.
DR SUPFAM; SSF81301; Nucleotidyltransferase; 1.
DR SUPFAM; SSF81271; TGS-like; 1.
DR PROSITE; PS51671; ACT; 1.
DR PROSITE; PS51831; HD; 1.
DR PROSITE; PS51880; TGS; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000014830}.
FT DOMAIN 45..144
FT /note="HD"
FT /evidence="ECO:0000259|PROSITE:PS51831"
FT DOMAIN 388..449
FT /note="TGS"
FT /evidence="ECO:0000259|PROSITE:PS51880"
FT DOMAIN 630..702
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
SQ SEQUENCE 702 AA; 79292 MW; 2DC634A68C4BAB85 CRC64;
MPTIDALSDR LVDYLDPQMV HQVRRAYFYA EQAHEGQWRK SGEPYVTHPL AVSSILATMH
MDHQSLMAAM LHDVIEDTEV DFPGIEGQFG IAVATIVEGV SKLTHLEVET KAEAQAENFQ
KMVMAMAEDI RVILVKLADR LHNMRTLGAM PAHKRRRIAK ETLDIYAPIA ARLGVRNIQI
ELQELSFFSY YPMRASRIRQ AVIKARGQRK DLITEIEASI QARLQQENLK GIVFGREKHL
YSIYLKMKSQ RKQFVDIMDV FAFRIVTETV DECYRVLGSV HNLYKPVHGR FKDYIAIPKG
NGYQSLHTEL FGAKDITIEV QIRTREMDAV AMQGIAEHSY YKGNGSSDIA VSSFTRARKW
VQDMLEMQKR AGDSMEFIDN VKKDLFPDEV YVFTPKGRIY ELPPGATSVD FAYAIHTDVG
NSCISCRVNR RLVPLSEPLE SGQTVEIIRT PSAKPNMAWL NFVVTGKARS SIRHFLKNQQ
RDESVQMGRR LLNQFLGQFG INTDQVDAVK MENLLEEASF KSVDELLQDI GVGNRMAYVV
ARKLKPDREQ SEAKLSHKPL AIEGTEGVVI QYAKCCQPIP GDSIVGYTSS GRGFVVHRIN
CKNIKSMKDD PEKCIYLEWS DDLEDEFSVG LRLEVASERG IVAHLATTAA ANGANILAID
LGEKEGLLYS VNMELGVKGR IHLARTIKKL RALRTVNRVV RI
//
