GPPA_VIBC1
ID GPPA_VIBC1 Reviewed; 497 AA.
AC A7MXT2;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 02-OCT-2007, sequence version 1.
DT 03-AUG-2022, entry version 76.
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};
GN OrderedLocusNames=VIBHAR_00339;
OS Vibrio campbellii (strain ATCC BAA-1116).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=2902295;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1116 / BB120;
RG The Vibrio harveyi Genome Sequencing Project;
RA Bassler B., Clifton S.W., Fulton L., Delehaunty K., Fronick C.,
RA Harrison M., Markivic C., Fulton R., Tin-Wollam A.-M., Shah N., Pepin K.,
RA Nash W., Thiruvilangam P., Bhonagiri V., Waters C., Tu K.C., Irgon J.,
RA Wilson R.K.;
RL Submitted (AUG-2007) 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: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}.
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DR EMBL; CP000789; ABU69361.1; -; Genomic_DNA.
DR RefSeq; WP_012126604.1; NC_022269.1.
DR AlphaFoldDB; A7MXT2; -.
DR SMR; A7MXT2; -.
DR EnsemblBacteria; ABU69361; ABU69361; VIBHAR_00339.
DR KEGG; vha:VIBHAR_00339; -.
DR PATRIC; fig|338187.25.peg.2240; -.
DR OMA; WQICVGA; -.
DR OrthoDB; 1862004at2; -.
DR UniPathway; UPA00908; UER00885.
DR Proteomes; UP000008152; 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.
FT CHAIN 1..497
FT /note="Guanosine-5'-triphosphate,3'-diphosphate
FT pyrophosphatase"
FT /id="PRO_0000314501"
SQ SEQUENCE 497 AA; 54724 MW; 5C50888DBAB586EF CRC64;
MSQAGSSPLY AAIDLGSNSF HMLVVRHIDG SVQTMAKIKR KVRLAAGLDE HNSLSMEAMQ
RGWDCLSLFA ERLQDIPKQN IRIVGTATLR TATNVDVFLE KANQILGQPI EVITGEEEAA
TIYKGVAHTS GGSGRRLVVD IGGASTELII GEGFEAKALT SLKMGCVTWL ENFFKDRQLN
ARNFDAAIEG AKQTLMPILG QYTDLGWDVC VGASGTVQAL QEIMLAQGMD EVITHSKLKR
LQKQAMLADH LEELDIEGLT LERALVFPSG LSILIAIFEQ LEIDAMTLAG GALREGLVYE
MVDELRQNDI RARTIRSVQN RYQLDCQYGE QVAKLAGKLL EQVGGEAWVA EPQGKVLLKT
TAKLHEIGLT IDFKKGGEHS AYLLQHLDLP GYTRAQKFFI GEIARRYREQ LTSLPEQHAL
SGTSGKRVLR LLRLAVLLSH RRNPDLEPCV TLTAEGDKLT LSIDAKWLEA NPLTAAELEI
ESNRQTDIGW PLSIVTC