ID   Q30S23_SULDN            Unreviewed;       796 AA.
AC   Q30S23;
DT   06-DEC-2005, integrated into UniProtKB/TrEMBL.
DT   06-DEC-2005, sequence version 1.
DT   27-MAR-2024, entry version 97.
DE   SubName: Full=Metal dependent phosphohydrolase {ECO:0000313|EMBL:ABB44208.1};
GN   OrderedLocusNames=Suden_0930 {ECO:0000313|EMBL:ABB44208.1};
OS   Sulfurimonas denitrificans (strain ATCC 33889 / DSM 1251) (Thiomicrospira
OS   denitrificans (strain ATCC 33889 / DSM 1251)).
OC   Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC   Sulfurimonadaceae; Sulfurimonas.
OX   NCBI_TaxID=326298 {ECO:0000313|EMBL:ABB44208.1, ECO:0000313|Proteomes:UP000002714};
RN   [1] {ECO:0000313|EMBL:ABB44208.1, ECO:0000313|Proteomes:UP000002714}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33889 / DSM 1251 {ECO:0000313|Proteomes:UP000002714};
RX   PubMed=18065616; DOI=10.1128/AEM.01844-07;
RA   Sievert S.M., Scott K.M., Klotz M.G., Chain P.S.G., Hauser L.J., Hemp J.,
RA   Huegler M., Land M., Lapidus A., Larimer F.W., Lucas S., Malfatti S.A.,
RA   Meyer F., Paulsen I.T., Ren Q., Simon J., Bailey K., Diaz E.,
RA   Fitzpatrick K.A., Glover B., Gwatney N., Korajkic A., Long A.,
RA   Mobberley J.M., Pantry S.N., Pazder G., Peterson S., Quintanilla J.D.,
RA   Sprinkle R., Stephens J., Thomas P., Vaughn R., Weber M.J., Wooten L.L.;
RT   "Genome of the epsilonproteobacterial chemolithoautotroph Sulfurimonas
RT   denitrificans.";
RL   Appl. Environ. Microbiol. 74:1145-1156(2008).
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DR   EMBL; CP000153; ABB44208.1; -; Genomic_DNA.
DR   RefSeq; WP_011372560.1; NC_007575.1.
DR   AlphaFoldDB; Q30S23; -.
DR   STRING; 326298.Suden_0930; -.
DR   KEGG; tdn:Suden_0930; -.
DR   eggNOG; COG1234; Bacteria.
DR   eggNOG; COG2203; Bacteria.
DR   eggNOG; COG2206; Bacteria.
DR   eggNOG; COG3437; Bacteria.
DR   HOGENOM; CLU_000445_92_13_7; -.
DR   OrthoDB; 9769359at2; -.
DR   Proteomes; UP000002714; Chromosome.
DR   GO; GO:0004115; F:3',5'-cyclic-AMP phosphodiesterase activity; IEA:InterPro.
DR   GO; GO:0006198; P:cAMP catabolic process; IEA:InterPro.
DR   CDD; cd07735; class_II_PDE_MBL-fold; 1.
DR   CDD; cd00077; HDc; 1.
DR   Gene3D; 3.30.450.40; -; 1.
DR   Gene3D; 1.10.3210.10; Hypothetical protein af1432; 2.
DR   Gene3D; 3.60.15.10; Ribonuclease Z/Hydroxyacylglutathione hydrolase-like; 1.
DR   InterPro; IPR003018; GAF.
DR   InterPro; IPR029016; GAF-like_dom_sf.
DR   InterPro; IPR003607; HD/PDEase_dom.
DR   InterPro; IPR037522; HD_GYP_dom.
DR   InterPro; IPR001279; Metallo-B-lactamas.
DR   InterPro; IPR000396; Pdiesterase2.
DR   InterPro; IPR036866; RibonucZ/Hydroxyglut_hydro.
DR   PANTHER; PTHR43155:SF2; CYCLIC DI-GMP PHOSPHODIESTERASE PA4108; 1.
DR   PANTHER; PTHR43155; CYCLIC DI-GMP PHOSPHODIESTERASE PA4108-RELATED; 1.
DR   Pfam; PF01590; GAF; 1.
DR   Pfam; PF13487; HD_5; 1.
DR   Pfam; PF02112; PDEase_II; 1.
DR   PRINTS; PR00388; PDIESTERASE2.
DR   SMART; SM00065; GAF; 1.
DR   SMART; SM00471; HDc; 1.
DR   SMART; SM00849; Lactamase_B; 1.
DR   SUPFAM; SSF55781; GAF domain-like; 1.
DR   SUPFAM; SSF109604; HD-domain/PDEase-like; 2.
DR   SUPFAM; SSF56281; Metallo-hydrolase/oxidoreductase; 1.
DR   PROSITE; PS51832; HD_GYP; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000313|EMBL:ABB44208.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002714}.
FT   DOMAIN          571..782
FT                   /note="HD-GYP"
FT                   /evidence="ECO:0000259|PROSITE:PS51832"
SQ   SEQUENCE   796 AA;  89559 MW;  7F672886A9CC5BE2 CRC64;
     MDTIKVLGAQ GGRSKDSFTT SIMVTKNTVI DAGNIMQALD RDAKNINKIF FSHSHLDHIV
     DSAFLIDNSF ATREEPLYLY GLPQTIKALK KHLFNSEIWP DFSEINLINT KTPSVVYVEL
     ELYKKYELEE GVSLTPLEAN HTVECCGYLI EGKKGSILFS GDTFKNPKLW DIINSNESIK
     ALIIDVSFPN KLTKIAQHSK HLTPHFLREE LELLKRKDVK IYINHLKPFY HEEIIEELFE
     IGISRDRVLN DSEEICFKNG LIKRVSMQYT TEQKIQKLNK IGTALSAETN IDALLEIIVT
     EAKILSNADA GTLYILEDKH LHFKVAQTDS LGIKMGGISG AITWPPLPLY LQDSTPNNKM
     VAATCALSDI VINIPDVYEA EGFSFDGTRK FDEGTGYRSK SMLVIPLKNH ESEIIGVLQL
     LNKYDDNNET IAFDKEDEEL TLSLASQAAI AITNTTLIQG LETLLEAFLQ SIIFAIGKKS
     PYTAGHIERM VKLTVMIAEA IDKDKGVFSA KSFSAQELKQ INFAALMHDI GKLATPEQVV
     DKSTKLETIF DRIEVVKGRI EIIKKALEIE LLNQKITLLQ SGKTLHVELE SEFSKKTDLL
     DSYFEVIQKS NRGTEFTNDE QIAIIQNIAS QNWEIDGKSY LILTENEAYN LSVQKGTLTS
     QERAIINEHA KISIDILNKL PFPKKYKEIP QISGNHHEKI NGKGYPLGLS GDEISFEARI
     LAVADVFEAL TASDRPYKKG NPLSSAMKIL YFMAKDDDLD RDIVKFFYNS GLYLQYAKKL
     LPKESIDEVT TDFSSL
//