ID   Q2SJM3_HAHCH            Unreviewed;       733 AA.
AC   Q2SJM3;
DT   24-JAN-2006, integrated into UniProtKB/TrEMBL.
DT   24-JAN-2006, sequence version 1.
DT   02-SEP-2026, entry version 93.
DE   SubName: Full=Adenylate cyclase, family 3 {ECO:0000313|EMBL:ABC29151.1};
GN   OrderedLocusNames=HCH_02328 {ECO:0000313|EMBL:ABC29151.1};
OS   Hahella chejuensis (strain KCTC 2396).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC   Oceanospirillales; Hahellaceae; Hahella.
OX   NCBI_TaxID=349521 {ECO:0000313|EMBL:ABC29151.1, ECO:0000313|Proteomes:UP000000238};
RN   [1] {ECO:0000313|EMBL:ABC29151.1, ECO:0000313|Proteomes:UP000000238}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KCTC 2396 {ECO:0000313|EMBL:ABC29151.1,
RC   ECO:0000313|Proteomes:UP000000238};
RX   PubMed=16352867; DOI=10.1093/nar/gki1016;
RA   Jeong H., Yim J.H., Lee C., Choi S.-H., Park Y.K., Yoon S.H., Hur C.-G.,
RA   Kang H.-Y., Kim D., Lee H.H., Park K.H., Park S.-H., Park H.-S., Lee H.K.,
RA   Oh T.K., Kim J.F.;
RT   "Genomic blueprint of Hahella chejuensis, a marine microbe producing an
RT   algicidal agent.";
RL   Nucleic Acids Res. 33:7066-7073(2005).
CC   -!- SIMILARITY: Belongs to the adenylyl cyclase class-4/guanylyl cyclase
CC       family. {ECO:0000256|PROSITE-ProRule:PRU00099}.
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DR   EMBL; CP000155; ABC29151.1; -; Genomic_DNA.
DR   RefSeq; WP_011396220.1; NC_007645.1.
DR   AlphaFoldDB; Q2SJM3; -.
DR   STRING; 349521.HCH_02328; -.
DR   KEGG; hch:HCH_02328; -.
DR   eggNOG; COG2114; Bacteria.
DR   eggNOG; COG4252; Bacteria.
DR   HOGENOM; CLU_000445_85_1_6; -.
DR   Proteomes; UP000000238; Chromosome.
DR   GO; GO:0004016; F:adenylate cyclase activity; IEA:UniProtKB-ARBA.
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; 3.30.70.1230; Nucleotide cyclase; 1.
DR   InterPro; IPR001054; A/G_cyclase.
DR   InterPro; IPR050697; Adenylyl/Guanylyl_Cyclase_3/4.
DR   InterPro; IPR007890; CHASE2.
DR   InterPro; IPR029787; Nucleotide_cyclase.
DR   PANTHER; PTHR43081:SF1; ADENYLATE CYCLASE, TERMINAL-DIFFERENTIATION SPECIFIC; 1.
DR   PANTHER; PTHR43081; ADENYLATE CYCLASE, TERMINAL-DIFFERENTIATION SPECIFIC-RELATED; 1.
DR   Pfam; PF05226; CHASE2; 1.
DR   Pfam; PF00211; Guanylate_cyc; 1.
DR   SMART; SM01080; CHASE2; 1.
DR   SMART; SM00044; CYCc; 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   Membrane {ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00099};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000238};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        6..26
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        359..380
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        386..407
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          478..610
FT                   /note="Guanylate cyclase"
FT                   /evidence="ECO:0000259|PROSITE:PS50125"
FT   BINDING         483
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         483
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         484
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         527
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         527
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   733 AA;  81589 MW;  C9CD74F5F6F64ED9 CRC64;
     MRTISGFLKH LPALLIAVVM IGWQLITQSG DRSLLNRLDY VFYDWRAQTA ALFTRAELYT
     DVVIVDIDEE SIQREGRWPW SRARVAALVE ALQESGAAVV AFDVVFSESE SNNFIESVAA
     SAGPDLSDEE RAALNRIAMS WRPDEQLAER LAEIDTVLGF FMHLDTSMQI GRLPNPLTSA
     PAGNVLINAS GYAAPLLELQ DEAAGSGFVT TFPDADGVIR RTPLFMSHDG SVYPSLALAA
     AMTYLLMDEV ELEFTPLGVV QAVSGMRLTD ALVRTDAVGR VMIPYRQGRG QFRYIPAWLA
     LAGGLAPQEL EGKLVFVGTS AIGLADLVST PFATVFPGVE VQALVAQGLL RGEFPYRPVW
     EPGAVLVFQL LLLLLLVWVL PGRRPLTMVL AAIMISLLLV AVNTLIWTRW RMDFPMISTL
     LLAQGVFGWY LVTEFIHEYA VERRVRGMFA QYVPPAHIDR MLDNPEQYSM AGESKELTVL
     FSDIRSFTTI SEQLSAAQLK ELLNLYFTPI TESIFRNDGT IDKYVGDMVM AFWGAPVDDP
     EHAEKAVKTA MEMQAITRRL SSELTAKGFP PIQIGVGINT GLMNVGDMGS QYRKAYTVLG
     DAVNLGSRLE GLTKFYGVDV LVGETTVKAT EGYAFRFCDR IQVKGKDIPV DAYEPLGEKG
     RLDAVTLNRL TRYQRAIECY RARQWEQADA IFQQLQLEDP SCRLYGLYRE RISGLRRQTL
     PENWDGVYRH TSK
//