ID A0A1Y0D0C9_9GAMM Unreviewed; 497 AA.
AC A0A1Y0D0C9;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 24-JAN-2024, entry version 21.
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=CBP12_11550 {ECO:0000313|EMBL:ART80704.1};
OS Oceanisphaera avium.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Aeromonadales;
OC Aeromonadaceae; Oceanisphaera.
OX NCBI_TaxID=1903694 {ECO:0000313|EMBL:ART80704.1, ECO:0000313|Proteomes:UP000243793};
RN [1] {ECO:0000313|Proteomes:UP000243793}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AMac2203 {ECO:0000313|Proteomes:UP000243793};
RA Sung H.;
RL Submitted (MAY-2017) 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}.
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DR EMBL; CP021376; ART80704.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y0D0C9; -.
DR KEGG; ocm:CBP12_11550; -.
DR OrthoDB; 9793035at2; -.
DR UniPathway; UPA00908; UER00885.
DR Proteomes; UP000243793; Chromosome.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000243793}.
FT DOMAIN 21..302
FT /note="Ppx/GppA phosphatase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02541"
FT DOMAIN 308..479
FT /note="Ppx/GppA phosphatase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21447"
SQ SEQUENCE 497 AA; 54579 MW; 25004702F74BA5CE CRC64;
MKNSALYAAI DLGSNSFHML VVNEVAGASR TLAKIKRKVR LAAGLQEDGS LDHAAMERGW
DCLQLFAEQL QDVPAENIRI VGTATLRLAS NIQVFLDQAH AILGHPIRII SGEEEAALIY
EGVAWTSSGT GRRLAIDIGG ASTELVIGEG TSALLLNSLD MGCVTWLKRY FNDGNLSETN
FEQAIAAARQ VLVPNASAYL KLGWQGCIGA SGTIQAIQEI MINLGEDERI TLPKLQALKN
AAIDCKTLAQ LHLPGLKAER VSVFPSGLAI LIALFDMLAI DDMVLAGGAL REGLMYGMLG
QHQDRDARVR SLDSLMDRYQ LDRTQGERVR NTALLAFKQV NERQPLEDAS DDILGWAAMM
YELGLCIEYK RAPEHGAYIL SHIDLPGFTV AQKQLLAALL LNQRDDFQLA ALEQQSATSY
EQAILLTRLL RISIILCLRR TKGTVPDFHV SAQGIELTLT LPPNWSQTHH LRASELQQEA
QRQTELGWPL VIKQGEE
//
