ID A0A443IFD8_9GAMM Unreviewed; 494 AA.
AC A0A443IFD8;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 12.
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=ED28_06505 {ECO:0000313|EMBL:RWR02779.1};
OS [Pantoea] beijingensis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Erwinia.
OX NCBI_TaxID=1324864 {ECO:0000313|EMBL:RWR02779.1, ECO:0000313|Proteomes:UP000288794};
RN [1] {ECO:0000313|EMBL:RWR02779.1, ECO:0000313|Proteomes:UP000288794}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 27579 {ECO:0000313|EMBL:RWR02779.1,
RC ECO:0000313|Proteomes:UP000288794};
RA Xu F., Liu Y., Wang S., Yin Y., Ma Y., Zhao S., Rong C.;
RT "Draft genome sequence of Pantoea beijingensis strain LMG 27579, an
RT emerging pathogen to Pleurotus eryngii with potential industrial
RT application.";
RL Submitted (APR-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:RWR02779.1}.
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DR EMBL; JMEE01000008; RWR02779.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A443IFD8; -.
DR UniPathway; UPA00908; UER00885.
DR Proteomes; UP000288794; 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:RWR02779.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000288794}.
FT DOMAIN 21..301
FT /note="Ppx/GppA phosphatase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02541"
FT DOMAIN 308..481
FT /note="Ppx/GppA phosphatase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21447"
SQ SEQUENCE 494 AA; 54777 MW; A7FDA6FAEE2C52F0 CRC64;
MLSASSLYAA IDLGSNSFHM LVVREVAGSI QTVARIKRKV RLAAGLDNAN HLSDEAMARG
WQCLRLFSEQ LQDIPLEQIR VVATATLRLA ANADIFLSKA QHILGSTINV ISGEEEARLI
YQGVAHTTGG SDKRLVVDIG GGSTELVTGD GAHATSLFSL PMGCVTWLER YFTDRHLGKA
NFEQAEQAAR AMIQPVAAAL RTQGWQICVG ASGTVQALQE IMVAQGMDEQ ITLSKLQQLK
QRAIQCGKLE ELEIEGLTLE RALVFPSGLS ILIAIFNELG IESMTLAGGA LREGLVYGML
HLPVDRDIRS RTLQNVQRRF TIDTEQAERV RQLAESFARQ VKQNWKLDER CCELLENASL
IHEIGLSVDF KQAPQHAAYL IRHLAMPGFT PAQKKLLATL LQNQGNNIDL GLLSQQNAVP
QRMAERLCRL LRLAIIFASR RRDDTLPAVR LHADDETLSL TLPTDWLEAH PLRAELLEQE
SHWQSYVHWP LIIS
//
