ID A0A0Q4YGH3_9BURK Unreviewed; 763 AA.
AC A0A0Q4YGH3;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Guanosine-3',5'-bis(Diphosphate) 3'-pyrophosphohydrolase {ECO:0000313|EMBL:KQP23118.1};
GN ORFNames=ASF43_04335 {ECO:0000313|EMBL:KQP23118.1};
OS Pseudorhodoferax sp. Leaf267.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae.
OX NCBI_TaxID=1736316 {ECO:0000313|EMBL:KQP23118.1, ECO:0000313|Proteomes:UP000051560};
RN [1] {ECO:0000313|EMBL:KQP23118.1, ECO:0000313|Proteomes:UP000051560}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf267 {ECO:0000313|EMBL:KQP23118.1,
RC ECO:0000313|Proteomes:UP000051560};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQP23118.1, ECO:0000313|Proteomes:UP000051560}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf267 {ECO:0000313|EMBL:KQP23118.1,
RC ECO:0000313|Proteomes:UP000051560};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) 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 -!- 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:KQP23118.1}.
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DR EMBL; LMMV01000001; KQP23118.1; -; Genomic_DNA.
DR RefSeq; WP_056177078.1; NZ_LMMV01000001.1.
DR AlphaFoldDB; A0A0Q4YGH3; -.
DR STRING; 1736316.ASF43_04335; -.
DR OrthoDB; 9805041at2; -.
DR Proteomes; UP000051560; Unassembled WGS sequence.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0016779; F:nucleotidyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0015969; P:guanosine tetraphosphate metabolic process; IEA:InterPro.
DR CDD; cd04876; ACT_RelA-SpoT; 1.
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; 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 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; SSF55021; ACT-like; 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 ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Hydrolase {ECO:0000313|EMBL:KQP23118.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022840};
KW Reference proteome {ECO:0000313|Proteomes:UP000051560}.
FT DOMAIN 76..175
FT /note="HD"
FT /evidence="ECO:0000259|PROSITE:PS51831"
FT DOMAIN 417..478
FT /note="TGS"
FT /evidence="ECO:0000259|PROSITE:PS51880"
FT DOMAIN 680..755
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 763 AA; 83791 MW; 9B59F47F6736FDAD CRC64;
MNVELPSDTA VRTSPRKGPK AVEASPAAAN AAAASFAALT ASLDYLDAQS IEQVRQAYRF
ADEAHLGQLR SSGEPYITHP IAVAAQCAAW KLDAQALMAA LLHDAMEDCG VTKPDLIERF
GAPVAELVDG LTKLDKLQFN TREESQAESF RKMLLAMARD VRVILIKLAD RSHNMRTMGD
MPRSKWARIS SETLDIYAPI AHRLGLNVTY RELQELAFQH LMPWRHAVLA KAVAKARSRR
RDLVQKVQAE LEAAFANAGM KVRIAGREKT LYSIYRKMDD KHLSFAQVTD IYGFRVVVGS
VTDCYTALGI LHQLYKPVPG RFKDHIAIAK VNGYQSLHTT LVGPSGVNVE FQMRTDAMHV
VAESGVAAHW LYKANHPEGH ASDRMGAQWL QSLLDIQHET RDASEFWDHV KVDLFPDAVY
VFTPKSQIMA LPRGATVVDF AYAIHSNVGD RTVAARINGD QVPLRTELHN GDVIEIITAP
VSAPNPAWLG FVRTGRARSK IRHHLKGLAQ TESEGLGEKL LTQAVRAEGI ETLPGSDAEG
QPIWDKLLRF SGNRTRAELM TDIGLGKRIA SIVAKRLKVL VTERGAKADP LLMTRERYTA
HESVSQGGVV IDGSENASVQ YARCCRPVPG DEIVGYLGRG EGLFIHTADC ALAKRLQYKD
SERFIAVAWS DEPVRSFETG IVVTVNNGKG VLARVAASLA SAEVDIIHMD MGQEETQDAS
DLRFVISVRD RMHLEQALRT LKRTPAVLRA VRATAAAYAG GAG
//
