ID A0A0J1H6L7_9GAMM Unreviewed; 496 AA.
AC A0A0J1H6L7;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 24-JAN-2024, entry version 30.
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=ABT56_04625 {ECO:0000313|EMBL:KLV07354.1};
OS Photobacterium aquae.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Photobacterium.
OX NCBI_TaxID=1195763 {ECO:0000313|EMBL:KLV07354.1, ECO:0000313|Proteomes:UP000036097};
RN [1] {ECO:0000313|EMBL:KLV07354.1, ECO:0000313|Proteomes:UP000036097}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.12159 {ECO:0000313|EMBL:KLV07354.1,
RC ECO:0000313|Proteomes:UP000036097};
RA Machado H., Gram L.;
RT "Photobacterium galathea sp. nov.";
RL Submitted (MAY-2015) 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:KLV07354.1}.
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DR EMBL; LDOT01000005; KLV07354.1; -; Genomic_DNA.
DR RefSeq; WP_047877874.1; NZ_LDOT01000005.1.
DR AlphaFoldDB; A0A0J1H6L7; -.
DR STRING; 1195763.ABT56_04625; -.
DR PATRIC; fig|1195763.3.peg.980; -.
DR OrthoDB; 9793035at2; -.
DR UniPathway; UPA00908; UER00885.
DR Proteomes; UP000036097; 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, ECO:0000313|EMBL:KLV07354.1}.
FT DOMAIN 23..302
FT /note="Ppx/GppA phosphatase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02541"
FT DOMAIN 309..479
FT /note="Ppx/GppA phosphatase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21447"
SQ SEQUENCE 496 AA; 54535 MW; F8D3CD132C011EEE CRC64;
MERTVSPLYA AIDLGSNSFH MWIVRDIAGT VQTLAKIKRK VRLAAGLNSN NELSLDAMQR
GWDCLSLFAE RLQDIPAANI RIVGTAALRT AVNANAFLSK AEKILGYPIQ IIPGEEEARI
IYQGVAHTSG GCGKRLVVDI GGASTEVIIG EGFDASALTS LKIGCVTWLE RYFKDRALTA
ANFDTAITAA KAAISPIVEQ YQTLGWTTCV GASGTVQALQ EIMLAQGMDE IITLAKLKRM
QRQAMQYERL EDLDIEGLTL ERALVFPSGL SILIAIFESL GIESMTLAGG ALREGMVYDM
MTQMRHHDVR ERTLASLQNR FQLDTGHAAE VTGTALNLLD ACQSAWQLEP QARYLLKACA
GLHEIGTMVE FKKSGEHAAY LIHHSDLPGF TRAQKHLIGE LLRRYREQLS SLPEQHALSA
PSATRLLRLL RLAVILCHRR DHCHQPPFTL DVTDNKLSLT LPASWLAANP LTDAELQQEA
NRQSDMGWPL TLIASE
//
