ID C7BQK4_PHOAA Unreviewed; 503 AA.
AC C7BQK4;
DT 22-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 22-SEP-2009, sequence version 1.
DT 27-MAR-2024, entry version 64.
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 ECO:0000313|EMBL:CAQ86234.1};
GN OrderedLocusNames=PAU_04146 {ECO:0000313|EMBL:CAQ86234.1};
OS Photorhabdus asymbiotica subsp. asymbiotica (strain ATCC 43949 / 3105-77)
OS (Xenorhabdus luminescens (strain 2)).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Morganellaceae; Photorhabdus.
OX NCBI_TaxID=553480 {ECO:0000313|EMBL:CAQ86234.1, ECO:0000313|Proteomes:UP000002747};
RN [1] {ECO:0000313|EMBL:CAQ86234.1, ECO:0000313|Proteomes:UP000002747}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43949 / 3105-77 {ECO:0000313|Proteomes:UP000002747};
RX PubMed=19583835; DOI=10.1186/1471-2164-10-302;
RA Wilkinson P., Waterfield N.R., Crossman L., Corton C.,
RA Sanchez-Contreras M., Vlisidou I., Barron A., Bignell A., Clark L.,
RA Ormond D., Mayho M., Bason N., Smith F., Simmonds M., Churcher C.,
RA Harris D., Thompson N.R., Quail M., Parkhill J., ffrench-Constant R.H.;
RT "Comparative genomics of the emerging human pathogen Photorhabdus
RT asymbiotica with the insect pathogen Photorhabdus luminescens.";
RL BMC Genomics 10:302-302(2009).
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; FM162591; CAQ86234.1; -; Genomic_DNA.
DR AlphaFoldDB; C7BQK4; -.
DR STRING; 291112.PAU_04146; -.
DR KEGG; pay:PAU_04146; -.
DR eggNOG; COG0248; Bacteria.
DR UniPathway; UPA00908; UER00885.
DR Proteomes; UP000002747; 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}.
FT DOMAIN 23..302
FT /note="Ppx/GppA phosphatase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02541"
FT DOMAIN 309..481
FT /note="Ppx/GppA phosphatase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21447"
SQ SEQUENCE 503 AA; 55898 MW; B6772A858F7D60D7 CRC64;
MMLSTSSLYA AIDLGSNSFH MLVVREISGS MQILARIKRK VRLAAGLDKN NYLSQQAMER
GWQCLRIFSE RLQGIPPSQI RVVATATLRI AGNSSEFVKK AAEILSCPVT VISGEDEARL
IYQGVAHTTG GPEKRLVVDI GGASTELVTG NGAKANQLSS LSMGCVTWLE CYFNDRSLTE
ENFAKAESAA HETMKPAVSK LIEQGWQICV GASGTVQALQ EIMIAQGMDE LITLPKLQEL
KHKAIECGKL EELEIEGLTL ERALVFPSGL AILIAIFQAL DIESMILAGG ALREGLVYGM
LDLPIEQDIR TRTLRNIQRR FQLEVEQSQR VKQLAEHFLQ QVAKPWALDS RCYELLLSAC
LIHEIGLSVD YRQAPSHAAY LISYLDLPGY TPAQKKLLAI LLRNQSATID LVSFSQQNAL
PLIQAQRLCR LLRLAIILAS HHRDDTFSAL HLKVSGEELM ITLPHGWLTQ YPLRAESLQQ
EILWQNHVQW PLVLQELDSS NLN
//
