ID A0A2N7D5V8_9VIBR Unreviewed; 498 AA.
AC A0A2N7D5V8;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 24-JAN-2024, entry version 16.
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=BCU70_15425 {ECO:0000313|EMBL:PMH37463.1};
OS Vibrio sp. 10N.286.49.C2.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=1880856 {ECO:0000313|EMBL:PMH37463.1, ECO:0000313|Proteomes:UP000235640};
RN [1] {ECO:0000313|Proteomes:UP000235640}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=10N.286.49.C2 {ECO:0000313|Proteomes:UP000235640};
RA Kauffman K., Hussain F., Yang J., Arevalo P., Brown J., Cutler M.,
RA Kelly L., Polz M.F.;
RT "Nontailed viruses are major unrecognized killers of bacteria in the
RT ocean.";
RL Submitted (JUL-2016) 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:PMH37463.1}.
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DR EMBL; MCUT01000042; PMH37463.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2N7D5V8; -.
DR OrthoDB; 9793035at2; -.
DR UniPathway; UPA00908; UER00885.
DR Proteomes; UP000235640; 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}.
FT DOMAIN 24..304
FT /note="Ppx/GppA phosphatase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02541"
FT DOMAIN 311..483
FT /note="Ppx/GppA phosphatase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21447"
SQ SEQUENCE 498 AA; 54667 MW; 27B4CC3B7B15FE5B CRC64;
MSQAVNSSPL YAAIDLGSNS FHMLVVRHVD GSIQTMAKIK RKVRLAAGLN STMALSPEAM
QRGWDCLSLF AERLQDIPQD NIRIVGTATL RTATNVDIFL DKANEILGYP IQVISGEEEA
ATIYKGVAHT SGGTGRRLVV DIGGASTELI IGEGFEPKAL TSLKMGCVTW LERHFKDRQL
NKKNFDCAIN AAKDTLTPIL KQYQELGWDT CVGASGTVQA LQEIMLAQGM DEVITHAKLK
RLQKQAMQAD HLEELDIEGL TLERALVFPS GLSILIAVFE LLNLDYMTLA GGALREGMVY
DMVSELQQDD IRARTIGSLQ SRCQLDVSYG EQVATTASQL LSACGGTTCI HEPHGETLLT
TAAKLHEVGL TFDFKKAGEH GAYLLQNIDL PGFTRAQKHF LAEVVRRYKD QLSPLPPQHA
VSAQSATRTL RLLRLAVIIT HRRQSSLQPN VSLTSQDDNL ILTLDKQWLD NNPLTAAELE
IESNRQSDLG WPLTINAV
//
