ID   Q5LP73_RUEPO            Unreviewed;       329 AA.
AC   Q5LP73;
DT   01-FEB-2005, integrated into UniProtKB/TrEMBL.
DT   01-FEB-2005, sequence version 1.
DT   04-NOV-2026, entry version 92.
DE   SubName: Full=Adenylate/guanylate cyclase {ECO:0000313|EMBL:AAV96215.1};
GN   OrderedLocusNames=SPO2977 {ECO:0000313|EMBL:AAV96215.1};
OS   Ruegeria pomeroyi (strain ATCC 700808 / DSM 15171 / DSS-3) (Silicibacter
OS   pomeroyi).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
OC   Rhodobacterales; Roseobacteraceae; Ruegeria.
OX   NCBI_TaxID=246200 {ECO:0000313|EMBL:AAV96215.1, ECO:0000313|Proteomes:UP000001023};
RN   [1] {ECO:0000313|EMBL:AAV96215.1, ECO:0000313|Proteomes:UP000001023}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700808 / DSM 15171 / DSS-3
RC   {ECO:0000313|Proteomes:UP000001023};
RX   PubMed=15602564; DOI=10.1038/nature03170;
RA   Moran M.A., Buchan A., Gonzalez J.M., Heidelberg J.F., Whitman W.B.,
RA   Kiene R.P., Henriksen J.R., King G.M., Belas R., Fuqua C., Brinkac L.,
RA   Lewis M., Johri S., Weaver B., Pai G., Eisen J.A., Rahe E., Sheldon W.M.,
RA   Ye W., Miller T.R., Carlton J., Rasko D.A., Paulsen I.T., Ren Q.,
RA   Daugherty S.C., Deboy R.T., Dodson R.J., Durkin A.S., Madupu R.,
RA   Nelson W.C., Sullivan S.A., Rosovitz M.J., Haft D.H., Selengut J., Ward N.;
RT   "Genome sequence of Silicibacter pomeroyi reveals adaptations to the marine
RT   environment.";
RL   Nature 432:910-913(2004).
RN   [2] {ECO:0000313|EMBL:AAV96215.1, ECO:0000313|Proteomes:UP000001023}
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 700808 / DSM 15171 / DSS-3
RC   {ECO:0000313|Proteomes:UP000001023};
RX   PubMed=25780504; DOI=10.1186/1944-3277-9-11;
RA   Rivers A.R., Smith C.B., Moran M.A.;
RT   "An updated genome annotation for the model marine bacterium Ruegeria
RT   pomeroyi DSS-3.";
RL   Stand. Genomic Sci. 9:11-11(2014).
CC   -!- SIMILARITY: Belongs to the adenylyl cyclase class-4/guanylyl cyclase
CC       family. {ECO:0000256|PROSITE-ProRule:PRU00099}.
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DR   EMBL; CP000031; AAV96215.1; -; Genomic_DNA.
DR   RefSeq; WP_011048673.1; NC_003911.12.
DR   AlphaFoldDB; Q5LP73; -.
DR   SMR; Q5LP73; -.
DR   STRING; 246200.SPO2977; -.
DR   PaxDb; 246200-SPO2977; -.
DR   DNASU; 3195656; -.
DR   KEGG; sil:SPO2977; -.
DR   eggNOG; COG2114; Bacteria.
DR   HOGENOM; CLU_844367_0_0_5; -.
DR   Proteomes; UP000001023; Chromosome.
DR   GO; GO:0004016; F:adenylate cyclase activity; IEA:UniProtKB-ARBA.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006171; P:cAMP biosynthetic process; IEA:TreeGrafter.
DR   GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR   CDD; cd07302; CHD; 1.
DR   Gene3D; 3.10.450.50; -; 1.
DR   Gene3D; 3.30.70.1230; Nucleotide cyclase; 1.
DR   InterPro; IPR001054; A/G_cyclase.
DR   InterPro; IPR050697; Adenylyl/Guanylyl_Cyclase_3/4.
DR   InterPro; IPR032710; NTF2-like_dom_sf.
DR   InterPro; IPR029787; Nucleotide_cyclase.
DR   InterPro; IPR037401; SnoaL-like.
DR   PANTHER; PTHR43081; ADENYLATE CYCLASE, TERMINAL-DIFFERENTIATION SPECIFIC-RELATED; 1.
DR   PANTHER; PTHR43081:SF19; PH-SENSITIVE ADENYLATE CYCLASE RV1264; 1.
DR   Pfam; PF00211; Guanylate_cyc; 1.
DR   Pfam; PF13474; SnoaL_3; 1.
DR   SMART; SM00044; CYCc; 1.
DR   SUPFAM; SSF54427; NTF2-like; 1.
DR   SUPFAM; SSF55073; Nucleotide cyclase; 1.
DR   PROSITE; PS50125; GUANYLATE_CYCLASE_2; 1.
PE   3: Inferred from homology;
KW   Magnesium {ECO:0000256|PROSITE-ProRule:PRU00099};
KW   Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00099};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001023}.
FT   DOMAIN          169..279
FT                   /note="Guanylate cyclase"
FT                   /evidence="ECO:0000259|PROSITE:PS50125"
FT   BINDING         174
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00099"
FT   BINDING         174
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00099"
FT   BINDING         175
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00099"
FT   BINDING         218
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00099"
FT   BINDING         218
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00099"
SQ   SEQUENCE   329 AA;  36032 MW;  11F44B19B9E6852E CRC64;
     MGETWMSAVT PSPELLAFAR RWIDAIPNRR PNDLRNMMTE KEHLLFVGTG EDEIWAGSSV
     REGIGDFFGE IPEFLRHEEV FAEAYEHNGT GWACLCHEIV FARQPDRVFQ VRSTLIFTLE
     DGAWKIVHRH GSVPIPNMDF TGAAQTAIAD LVAAAKQGFS LDQREGFASV MFTDIVNSSR
     LASAMGDRLW SSEVARHFNS LREIIEARGG QFVKSLGDGT MSSFPSPEQG LRAAQAILRA
     TEASDGPAIA LRIGIHTGEV IQTREDFFGT VVNKAARIAA VAAPGEIVIS GDTRDLAGAV
     EGLIIHPPAD ISLKGFDGLH RVHRLEWKA
//