(data stored in SCRATCH zone)

SWISSPROT: D3VIK5_XENNA

ID   D3VIK5_XENNA            Unreviewed;       176 AA.
AC   D3VIK5;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   08-MAY-2019, entry version 49.
DE   RecName: Full=Inorganic pyrophosphatase {ECO:0000256|HAMAP-Rule:MF_00209};
DE            EC=3.6.1.1 {ECO:0000256|HAMAP-Rule:MF_00209};
DE   AltName: Full=Pyrophosphate phospho-hydrolase {ECO:0000256|HAMAP-Rule:MF_00209};
DE            Short=PPase {ECO:0000256|HAMAP-Rule:MF_00209};
GN   Name=ppa {ECO:0000256|HAMAP-Rule:MF_00209,
GN   ECO:0000313|EMBL:CBJ88555.1};
GN   OrderedLocusNames=XNC1_0481 {ECO:0000313|EMBL:CBJ88555.1};
OS   Xenorhabdus nematophila (strain ATCC 19061 / DSM 3370 / LMG 1036 /
OS   NCIB 9965 / AN6).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Morganellaceae; Xenorhabdus.
OX   NCBI_TaxID=406817 {ECO:0000313|EMBL:CBJ88555.1, ECO:0000313|Proteomes:UP000008075};
RN   [1] {ECO:0000313|Proteomes:UP000008075}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 19061 / DSM 3370 / LMG 1036 / NCIB 9965 / AN6
RC   {ECO:0000313|Proteomes:UP000008075};
RA   Goodrich-Blair H., Barbazuk B., Bode H.B., Darby C., Du Z., Forst S.,
RA   Gaudriault S., Goldman B.S., Goodner B., Henkhaus J., Latreille P.,
RA   Medigue C., Miller N., Norton S., Ogier J.C., Rouy Z., Slater S.,
RA   Suen G.;
RT   "Complete genome sequence of Xenorhabdus nematophila (strain ATCC
RT   19061 / DSM 3370 / LMG 1036 / NCIB 9965 / AN6).";
RL   Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:CBJ88555.1, ECO:0000313|Proteomes:UP000008075}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 19061 / DSM 3370 / LMG 1036 / NCIB 9965 / AN6
RC   {ECO:0000313|Proteomes:UP000008075};
RX   PubMed=22125637; DOI=10.1371/journal.pone.0027909;
RA   Chaston J.M., Suen G., Tucker S.L., Andersen A.W., Bhasin A., Bode E.,
RA   Bode H.B., Brachmann A.O., Cowles C.E., Cowles K.N., Darby C.,
RA   de Leon L., Drace K., Du Z., Givaudan A., Herbert Tran E.E.,
RA   Jewell K.A., Knack J.J., Krasomil-Osterfeld K.C., Kukor R., Lanois A.,
RA   Latreille P., Leimgruber N.K., Lipke C.M., Liu R., Lu X.,
RA   Martens E.C., Marri P.R., Medigue C., Menard M.L., Miller N.M.,
RA   Morales-Soto N., Norton S., Ogier J.C., Orchard S.S., Park D.,
RA   Park Y., Qurollo B.A., Sugar D.R., Richards G.R., Rouy Z.,
RA   Slominski B., Slominski K., Snyder H., Tjaden B.C., van der Hoeven R.,
RA   Welch R.D., Wheeler C., Xiang B., Barbazuk B., Gaudriault S.,
RA   Goodner B., Slater S.C., Forst S., Goldman B.S., Goodrich-Blair H.;
RT   "The entomopathogenic bacterial endosymbionts xenorhabdus and
RT   photorhabdus: convergent lifestyles from divergent genomes.";
RL   PLoS ONE 6:e27909-e27909(2011).
CC   -!- FUNCTION: Catalyzes the hydrolysis of inorganic pyrophosphate
CC       (PPi) forming two phosphate ions. {ECO:0000256|HAMAP-
CC       Rule:MF_00209}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=diphosphate + H2O = H(+) + 2 phosphate;
CC         Xref=Rhea:RHEA:24576, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:43474; EC=3.6.1.1;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00209};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00209};
CC   -!- SUBUNIT: Homohexamer. {ECO:0000256|HAMAP-Rule:MF_00209}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00209}.
CC   -!- SIMILARITY: Belongs to the PPase family. {ECO:0000256|HAMAP-
CC       Rule:MF_00209}.
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DR   EMBL; FN667742; CBJ88555.1; -; Genomic_DNA.
DR   RefSeq; WP_010845228.1; NC_014228.1.
DR   STRING; 406817.XNC1_0481; -.
DR   EnsemblBacteria; CBJ88555; CBJ88555; XNC1_0481.
DR   KEGG; xne:XNC1_0481; -.
DR   eggNOG; ENOG4105F0N; Bacteria.
DR   eggNOG; COG0221; LUCA.
DR   HOGENOM; HOG000236473; -.
DR   KO; K01507; -.
DR   OMA; DEPTFPG; -.
DR   Proteomes; UP000008075; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004427; F:inorganic diphosphatase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006796; P:phosphate-containing compound metabolic process; IEA:InterPro.
DR   CDD; cd00412; pyrophosphatase; 1.
DR   Gene3D; 3.90.80.10; -; 1.
DR   HAMAP; MF_00209; Inorganic_PPase; 1.
DR   InterPro; IPR008162; Pyrophosphatase.
DR   InterPro; IPR036649; Pyrophosphatase_sf.
DR   PANTHER; PTHR10286; PTHR10286; 1.
DR   Pfam; PF00719; Pyrophosphatase; 1.
DR   SUPFAM; SSF50324; SSF50324; 1.
DR   PROSITE; PS00387; PPASE; 1.
PE   3: Inferred from homology;
DR   PRODOM; D3VIK5.
DR   SWISS-2DPAGE; D3VIK5.
KW   Complete proteome {ECO:0000313|Proteomes:UP000008075};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00209};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_00209,
KW   ECO:0000313|EMBL:CBJ88555.1};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00209};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00209};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008075}.
FT   METAL        66     66       Magnesium 1. {ECO:0000256|HAMAP-Rule:
FT                                MF_00209}.
FT   METAL        71     71       Magnesium 1. {ECO:0000256|HAMAP-Rule:
FT                                MF_00209}.
FT   METAL        71     71       Magnesium 2. {ECO:0000256|HAMAP-Rule:
FT                                MF_00209}.
FT   METAL       103    103       Magnesium 1. {ECO:0000256|HAMAP-Rule:
FT                                MF_00209}.
FT   BINDING      30     30       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00209}.
FT   BINDING      44     44       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00209}.
FT   BINDING      56     56       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00209}.
FT   BINDING     142    142       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00209}.
SQ   SEQUENCE   176 AA;  19757 MW;  5B5ED6F6305A853F CRC64;
     MSLNNVPAGK ELPEDIYVII EIPANADPIK YEVDKESGAL FVDRFMSTAM FYPCNYGYIN
     NTLSLDGDPV DVLVPTPYPL QPGSVIRCRP VGVLKMTDES GEDAKLVAVP HTKLSKEYDH
     IKDVNDLPEL LRAQITHFFE HYKDLEKGKW VKVDGWDNVE AAKAEIVSSF ERAAKK
//

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