(data stored in SCRATCH zone)

SWISSPROT: C5BBB1_EDWI9

ID   C5BBB1_EDWI9            Unreviewed;       500 AA.
AC   C5BBB1;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   08-MAY-2019, entry version 53.
DE   RecName: Full=Guanosine-5'-triphosphate,3'-diphosphate pyrophosphatase {ECO:0000256|HAMAP-Rule:MF_01550, ECO:0000256|SAAS:SAAS00336652};
DE            EC=3.6.1.40 {ECO:0000256|HAMAP-Rule:MF_01550, ECO:0000256|SAAS:SAAS00336644};
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   OrderedLocusNames=NT01EI_0086 {ECO:0000313|EMBL:ACR67346.1};
OS   Edwardsiella ictaluri (strain 93-146).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Hafniaceae; Edwardsiella.
OX   NCBI_TaxID=634503 {ECO:0000313|EMBL:ACR67346.1, ECO:0000313|Proteomes:UP000001485};
RN   [1] {ECO:0000313|Proteomes:UP000001485}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=93-146 {ECO:0000313|Proteomes:UP000001485};
RA   Williams M.L., Gillaspy A.F., Dyer D.W., Thune R.L., Waldbieser G.C.,
RA   Schuster S.C., Gipson J., Zaitshik J., Landry C., Lawrence M.L.;
RT   "Complete genome sequence of Edwardsiella ictaluri 93-146.";
RL   Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ACR67346.1, ECO:0000313|Proteomes:UP000001485}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=93-146 {ECO:0000313|EMBL:ACR67346.1,
RC   ECO:0000313|Proteomes:UP000001485};
RX   PubMed=22247535; DOI=10.1128/JB.06522-11;
RA   Williams M.L., Gillaspy A.F., Dyer D.W., Thune R.L., Waldbieser G.C.,
RA   Schuster S.C., Gipson J., Zaitshik J., Landry C., Banes M.M.,
RA   Lawrence M.L.;
RT   "Genome Sequence of Edwardsiella ictaluri 93-146, a Strain Associated
RT   with a Natural Channel Catfish Outbreak of Enteric Septicemia of
RT   Catfish.";
RL   J. Bacteriol. 194:740-741(2012).
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       ECO:0000256|SAAS:SAAS00890260}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=guanosine 3'-diphosphate 5'-triphosphate + H2O =
CC         guanosine 3',5'-bis(diphosphate) + H(+) + phosphate;
CC         Xref=Rhea:RHEA:13073, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:77828, ChEBI:CHEBI:142410;
CC         EC=3.6.1.40; Evidence={ECO:0000256|HAMAP-Rule:MF_01550,
CC         ECO:0000256|SAAS:SAAS01116876};
CC   -!- PATHWAY: Purine metabolism; ppGpp biosynthesis; ppGpp from GTP:
CC       step 2/2. {ECO:0000256|HAMAP-Rule:MF_01550,
CC       ECO:0000256|SAAS:SAAS00890257}.
CC   -!- SIMILARITY: Belongs to the GppA/Ppx family. GppA subfamily.
CC       {ECO:0000256|HAMAP-Rule:MF_01550, ECO:0000256|SAAS:SAAS00534370}.
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DR   EMBL; CP001600; ACR67346.1; -; Genomic_DNA.
DR   RefSeq; WP_015869567.1; NC_012779.2.
DR   EnsemblBacteria; ACR67346; ACR67346; NT01EI_0086.
DR   GeneID; 7959805; -.
DR   KEGG; eic:NT01EI_0086; -.
DR   PATRIC; fig|634503.3.peg.80; -.
DR   eggNOG; ENOG4105C9X; Bacteria.
DR   eggNOG; COG0248; LUCA.
DR   HOGENOM; HOG000258672; -.
DR   KO; K01524; -.
DR   OMA; WQICVGA; -.
DR   OrthoDB; 1862004at2; -.
DR   BioCyc; EICT634503:G1GVC-79-MONOMER; -.
DR   UniPathway; UPA00908; UER00885.
DR   Proteomes; UP000001485; 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   HAMAP; MF_01550; GppA; 1.
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.
PE   3: Inferred from homology;
DR   PRODOM; C5BBB1.
DR   SWISS-2DPAGE; C5BBB1.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001485};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_01550,
KW   ECO:0000256|SAAS:SAAS00181019};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001485}.
FT   DOMAIN       21    300       Ppx-GppA. {ECO:0000259|Pfam:PF02541}.
SQ   SEQUENCE   500 AA;  54976 MW;  1990142B5557F861 CRC64;
     MGKNAALYAA IDLGSNSFHM LVVREMAGGI QTLARIKRKV RLAAGLDADN TLSPDAMQRG
     WQCLRLFAER LQDIPIDHIR VVATATLRIA RNADAFIERA QEILGRPVRI ISGEEEARLI
     YQGVAHTTGG ARRRLVVDIG GGSTELACGE SAKADVLFSL QMGCVTWLER YFSDRHLTQA
     NFARAGDAAH AMIAPVHDTL LRHGWQACVG ASGTVQALQE IMVAQGMDER ITLDKLCQLR
     DRAIECGKLE ELEIEGLTLE RALVFPSGLA ILIALFEALH IDSMTLSGGA LREGLVYGML
     ALPGGCDVRT RTLHNIQRRF LIDEGQAERV WRLADSLSRQ LTTPWPQDSS ANMLLHAACL
     LHELGLSVDV RQAPQHTAYL IRHLDLPGFT PAQKKLLATL LANQSGPLNL ALFGQQNAVP
     LHTAQRLCRL LRLAIIFASQ RNDGTLPSLL TQVCEENTLR LILPTGWLAA HPLRAESLQQ
     ESLWQGYAHW PLQIVEATSD
//

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