GPPA_VIBVY
ID GPPA_VIBVY Reviewed; 497 AA.
AC Q7MGP6;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 2.
DT 25-MAY-2022, entry version 99.
DE RecName: Full=Guanosine-5'-triphosphate,3'-diphosphate pyrophosphatase {ECO:0000255|HAMAP-Rule:MF_01550};
DE EC=3.6.1.40 {ECO:0000255|HAMAP-Rule:MF_01550};
DE AltName: Full=Guanosine pentaphosphate phosphohydrolase {ECO:0000255|HAMAP-Rule:MF_01550};
DE AltName: Full=pppGpp-5'-phosphohydrolase {ECO:0000255|HAMAP-Rule:MF_01550};
GN Name=gppA {ECO:0000255|HAMAP-Rule:MF_01550}; OrderedLocusNames=VV3184;
OS Vibrio vulnificus (strain YJ016).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=196600;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YJ016;
RX PubMed=14656965; DOI=10.1101/gr.1295503;
RA Chen C.-Y., Wu K.-M., Chang Y.-C., Chang C.-H., Tsai H.-C., Liao T.-L.,
RA Liu Y.-M., Chen H.-J., Shen A.B.-T., Li J.-C., Su T.-L., Shao C.-P.,
RA Lee C.-T., Hor L.-I., Tsai S.-F.;
RT "Comparative genome analysis of Vibrio vulnificus, a marine pathogen.";
RL Genome Res. 13:2577-2587(2003).
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:0000255|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:0000255|HAMAP-Rule:MF_01550};
CC -!- PATHWAY: Purine metabolism; ppGpp biosynthesis; ppGpp from GTP: step
CC 2/2. {ECO:0000255|HAMAP-Rule:MF_01550}.
CC -!- SIMILARITY: Belongs to the GppA/Ppx family. GppA subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_01550}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC95948.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; BA000037; BAC95948.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_011078989.1; NC_005139.1.
DR AlphaFoldDB; Q7MGP6; -.
DR SMR; Q7MGP6; -.
DR STRING; 672.VV93_v1c29050; -.
DR EnsemblBacteria; BAC95948; BAC95948; BAC95948.
DR KEGG; vvy:VV3184; -.
DR eggNOG; COG0248; Bacteria.
DR HOGENOM; CLU_025908_4_0_6; -.
DR OMA; WQICVGA; -.
DR OrthoDB; 1862004at2; -.
DR UniPathway; UPA00908; UER00885.
DR Proteomes; UP000002675; Chromosome I.
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 HAMAP; MF_01550; GppA; 1.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR023709; Guo-5TP_3DP_PyrP.
DR InterPro; IPR003695; Ppx_GppA.
DR InterPro; IPR030673; PyroPPase_GppA_Ppx.
DR Pfam; PF02541; Ppx-GppA; 1.
DR PIRSF; PIRSF001267; Pyrophosphatase_GppA_Ppx; 1.
DR SUPFAM; SSF53067; SSF53067; 2.
PE 3: Inferred from homology;
KW Hydrolase; Reference proteome.
FT CHAIN 1..497
FT /note="Guanosine-5'-triphosphate,3'-diphosphate
FT pyrophosphatase"
FT /id="PRO_0000194296"
SQ SEQUENCE 497 AA; 54755 MW; A4EB735219F4792C CRC64;
MSQAGNSPLY AAIDLGSNSF HMLVVRHIDG SVQTMAKIKR KVRLAAGLDE HNALSKEAMQ
RGWDCLSLFA ERLQDIPAEH IRIVGTATLR TATNVDLFLQ KANQILGHPI EVISGEEEAA
TIYKGVAHTS GGSGRRLVVD IGGASTELII GEGFEAKALT SLKMGCVTWL ENFFKDRQLS
ARNFEAAIEG AKQTLLPILE QYKSLGWDVC VGASGTVQAL QEIMLAQGMD EVITHAKLKR
LQKQAMLADH LEELEIEGLT LERALVFPSG LSILIAIFEL LEIDAMTLAG GALREGLAYE
MMSELRQDDI RARTIGSIQS RYQLDSQYGQ QVANLALKLL QQVGDVMWIP EPQGAMLLET
TAKLHEIGLT IDFKKGGEHS AYLMQHLDLP GFTRAQKFLM GEIARRYREG LTSLPEQHAL
SGNSGKRLLR LLRLAVILSH RRQPSLEPEV TLSAEGDKLT LAIDAQWLEN NPLTAAELEL
EANRQTDIGW PLVIESR