ID A0A0J8YXH4_9GAMM Unreviewed; 495 AA.
AC A0A0J8YXH4;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE RecName: Full=Guanosine-5'-triphosphate,3'-diphosphate pyrophosphatase {ECO:0000256|HAMAP-Rule:MF_01550};
DE EC=3.6.1.40 {ECO:0000256|HAMAP-Rule:MF_01550};
DE AltName: Full=Guanosine pentaphosphate phosphohydrolase {ECO:0000256|HAMAP-Rule:MF_01550};
DE AltName: Full=pppGpp-5'-phosphohydrolase {ECO:0000256|HAMAP-Rule:MF_01550};
GN Name=gppA {ECO:0000256|HAMAP-Rule:MF_01550};
GN ORFNames=AI29_05960 {ECO:0000313|EMBL:KMV74316.1};
OS bacteria symbiont BFo2 of Frankliniella occidentalis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales.
OX NCBI_TaxID=1628856 {ECO:0000313|EMBL:KMV74316.1, ECO:0000313|Proteomes:UP000036794};
RN [1] {ECO:0000313|EMBL:KMV74316.1, ECO:0000313|Proteomes:UP000036794}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BFo2 {ECO:0000313|EMBL:KMV74316.1,
RC ECO:0000313|Proteomes:UP000036794};
RA Facey P.D., Hitchings M.D., Hegarty M.J., Pachebat J.A., Morgan L.V.,
RA Hoeppner J.E., Whitten M.A., Dyson P.J., Del Sol R.;
RT "The draft genomes, genome evolution and classification of BFo1 and BFo2
RT two insect symbionts isolated from Western Flower Thrips (Frankliniella
RT occidentalis [Pergande]).";
RL Submitted (MAY-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the conversion of pppGpp to ppGpp. Guanosine
CC pentaphosphate (pppGpp) is a cytoplasmic signaling molecule which
CC together with ppGpp controls the 'stringent response', an adaptive
CC process that allows bacteria to respond to amino acid starvation,
CC resulting in the coordinated regulation of numerous cellular
CC activities. {ECO:0000256|HAMAP-Rule:MF_01550}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=guanosine 3'-diphosphate 5'-triphosphate + H2O = guanosine
CC 3',5'-bis(diphosphate) + H(+) + phosphate; Xref=Rhea:RHEA:13073,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:77828, ChEBI:CHEBI:142410; EC=3.6.1.40;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01550};
CC -!- PATHWAY: Purine metabolism; ppGpp biosynthesis; ppGpp from GTP: step
CC 2/2. {ECO:0000256|HAMAP-Rule:MF_01550}.
CC -!- SIMILARITY: Belongs to the GppA/Ppx family. GppA subfamily.
CC {ECO:0000256|HAMAP-Rule:MF_01550}.
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:KMV74316.1}.
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DR EMBL; JMSP01000011; KMV74316.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0J8YXH4; -.
DR STRING; 1628856.WB67_08005; -.
DR PATRIC; fig|1628856.3.peg.1178; -.
DR UniPathway; UPA00908; UER00885.
DR Proteomes; UP000036794; Unassembled WGS sequence.
DR GO; GO:0008894; F:guanosine-5'-triphosphate,3'-diphosphate diphosphatase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0015974; P:guanosine pentaphosphate catabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0015970; P:guanosine tetraphosphate biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.30.420.40; -; 1.
DR Gene3D; 3.30.420.150; Exopolyphosphatase. Domain 2; 1.
DR Gene3D; 1.10.3210.10; Hypothetical protein af1432; 1.
DR HAMAP; MF_01550; GppA; 1.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR023709; Guo-5TP_3DP_PyrP.
DR InterPro; IPR048950; Ppx_GppA_C.
DR InterPro; IPR003695; Ppx_GppA_N.
DR InterPro; IPR030673; PyroPPase_GppA_Ppx.
DR PANTHER; PTHR30005; EXOPOLYPHOSPHATASE; 1.
DR PANTHER; PTHR30005:SF0; RETROGRADE REGULATION PROTEIN 2; 1.
DR Pfam; PF02541; Ppx-GppA; 1.
DR Pfam; PF21447; Ppx-GppA_III; 1.
DR PIRSF; PIRSF001267; Pyrophosphatase_GppA_Ppx; 1.
DR SUPFAM; SSF53067; Actin-like ATPase domain; 2.
DR SUPFAM; SSF109604; HD-domain/PDEase-like; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_01550, ECO:0000313|EMBL:KMV74316.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000036794}.
FT DOMAIN 22..300
FT /note="Ppx/GppA phosphatase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02541"
FT DOMAIN 308..480
FT /note="Ppx/GppA phosphatase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21447"
SQ SEQUENCE 495 AA; 54373 MW; EE9BE302ADF759CD CRC64;
MRSASSLHAA IDLGSNSFHL LVVREISGSL QTVARIKRKV RLAAGLNADN QLSEEAMQRG
LNCLALFAEQ LEHIPLSQIR AVATATLRIA TNADAFLCRA HDVLGLPIEV ISGEEEATLI
YQGVAQTTSG SDQRLVVDIG GGSTELVTGI GTDATALFSL SMGCVTWLER YFTDRYLTRE
NFDRAEAAAR AEISKVKATL LAKGWQICVG ASGTVQALQE IMVAQGMDEQ ITLAKLEQLK
QRAIQCGKLE ELEIEGLTLE RALVFPSGLS ILLAIFHELS ITRMSLAGGA LREGLIYGMI
TLPVDKDIRK RTLETTQQRF AVDLEQAERV KATCAVLVQQ VNDSWGLSEY CQQLLSSAAA
LHELGLAINY RHGAENSAYL IRQLELPGFT PAQKQLVAAI VMNQKGNIDL PSLSQQSALP
LQQAEQLCRL FRLAVILCST RSTSEMASFH LSAKGNHLAL QIDKQWAIHH PYRLELLQQE
EHLQSYVHWG FTLSY
//
