ID A0A0W7TWN0_9GAMM Unreviewed; 498 AA.
AC A0A0W7TWN0;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 43.
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=ATO46_11075 {ECO:0000313|EMBL:KUE78227.1};
OS Aeromonas schubertii.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Aeromonadales;
OC Aeromonadaceae; Aeromonas.
OX NCBI_TaxID=652 {ECO:0000313|EMBL:KUE78227.1, ECO:0000313|Proteomes:UP000054876};
RN [1] {ECO:0000313|EMBL:KUE78227.1, ECO:0000313|Proteomes:UP000054876}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43700 {ECO:0000313|EMBL:KUE78227.1,
RC ECO:0000313|Proteomes:UP000054876};
RA Liu L., Li Q., Zhang F., Shi B.;
RT "Complete genome sequence of Aeromonas schubertii strain ATCC43700.";
RL Submitted (DEC-2015) 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:KUE78227.1}.
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DR EMBL; LPUO01000056; KUE78227.1; -; Genomic_DNA.
DR RefSeq; WP_050665291.1; NZ_LPUO01000056.1.
DR AlphaFoldDB; A0A0W7TWN0; -.
DR STRING; 652.WL1483_2495; -.
DR OrthoDB; 9793035at2; -.
DR UniPathway; UPA00908; UER00885.
DR Proteomes; UP000054876; 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 CDD; cd00012; NBD_sugar-kinase_HSP70_actin; 1.
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:KUE78227.1}.
FT DOMAIN 20..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 498 AA; 55393 MW; 0A5C3AA7DB378E9E CRC64;
MSSTPLYAAI DLGSNSFHML VVREVAGALR TVAKVKRKVR LASGLDEHFR LSRTAMERGW
DCLRLFSEQL QDIPPENIRV VGTATLRLAT NVEEFLAEAE RVLNHGIEII SGEEEAKTIY
EGVSWTSAGE GNRLVIDIGG ASTELVIGEQ SEAKLLSSLH MGCVTWLSNH FGDGQLSTER
FAQAIDAAKA VLTEVAHDYR LLGWKSCVGA SGTVQALQEI MLAQGKSERV TLPKLQELMQ
QAIACGRLDQ LQLEGLTAER LTVFPSGLAI LIALFEVLGI ESMTLAGGAL REGLIYGLLG
NSHDCDARDR TANSLINRYQ LDREHAERVR DTAVEAFAQV QSAWRLSRRY GRPILRYAAL
LHEIGLCIEY KKAPQHAAYI IDNIDMPGFT PAQKKLLSAL LLNQRDDFKM EPLERQGAVT
ARQAIRLARL LRLSLILCMR RTQGTVPTFT LQAEEDALTL ALPKGWLDVH YLRASELRME
VERQQKMGWP TRLIEREA
//
