ID   CYAB_AERHY              Reviewed;         191 AA.
AC   O69199;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 3.
DT   25-MAY-2022, entry version 69.
DE   RecName: Full=Adenylate cyclase CyaB;
DE            EC=4.6.1.1;
DE   AltName: Full=ATP pyrophosphate-lyase;
DE   AltName: Full=Adenylyl cyclase;
GN   Name=cyaB;
OS   Aeromonas hydrophila.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Aeromonadales;
OC   Aeromonadaceae; Aeromonas.
OX   NCBI_TaxID=644;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-6, FUNCTION,
RP   BIOPHYSICOCHEMICAL PROPERTIES, DISRUPTION PHENOTYPE, AND ACTIVITY
RP   REGULATION.
RC   STRAIN=strain 218;
RX   PubMed=9642185; DOI=10.1128/jb.180.13.3339-3344.1998;
RA   Sismeiro O., Trotot P., Biville F., Vivares C., Danchin A.;
RT   "Aeromonas hydrophila adenylyl cyclase 2: a new class of adenylyl cyclases
RT   with thermophilic properties and sequence similarities to proteins from
RT   hyperthermophilic archaebacteria.";
RL   J. Bacteriol. 180:3339-3344(1998).
RN   [2]
RP   FUNCTION AS A TRIPHOSPHATASE, AND CATALYTIC ACTIVITY.
RX   PubMed=22984449; DOI=10.1371/journal.pone.0043879;
RA   Kohn G., Delvaux D., Lakaye B., Servais A.C., Scholer G., Fillet M.,
RA   Elias B., Derochette J.M., Crommen J., Wins P., Bettendorff L.;
RT   "High inorganic triphosphatase activities in bacteria and mammalian cells:
RT   identification of the enzymes involved.";
RL   PLoS ONE 7:E43879-E43879(2012).
CC   -!- FUNCTION: In vitro, CyaB catalyzes the biosynthesis of cyclic AMP
CC       (cAMP) from ATP. It seems that under the physiological conditions CyaB
CC       has no function in cAMP processes. In vitro, it is also able to
CC       hydrolyze substrates such as thiamine triphosphate (ThTP) and inorganic
CC       triphosphate (PPPi) at a low rate. It has a slight preference for ThTP
CC       over ATP and PPPi in the presence of manganese ions. This PPPase
CC       activity is probably not of physiological importance.
CC       {ECO:0000269|PubMed:22984449, ECO:0000269|PubMed:9642185}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP = 3',5'-cyclic AMP + diphosphate; Xref=Rhea:RHEA:15389,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:58165; EC=4.6.1.1;
CC         Evidence={ECO:0000269|PubMed:22984449};
CC   -!- ACTIVITY REGULATION: Inhibited by GTP. {ECO:0000269|PubMed:9642185}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 9.5. {ECO:0000269|PubMed:9642185};
CC       Temperature dependence:
CC         Optimum temperature is 65 degrees Celsius.
CC         {ECO:0000269|PubMed:9642185};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- DISRUPTION PHENOTYPE: Cells lacking this gene show no impair of cAMP
CC       biosynthesis. {ECO:0000269|PubMed:9642185}.
CC   -!- SIMILARITY: Belongs to the adenylyl cyclase CyaB family. {ECO:0000305}.
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DR   EMBL; AJ223730; CAA11532.1; -; Genomic_DNA.
DR   AlphaFoldDB; O69199; -.
DR   SMR; O69199; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004016; F:adenylate cyclase activity; IDA:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0006171; P:cAMP biosynthetic process; IEA:UniProtKB-KW.
DR   CDD; cd07890; CYTH-like_AC_IV-like; 1.
DR   InterPro; IPR008173; Adenylyl_cyclase_CyaB.
DR   InterPro; IPR033469; CYTH-like_dom_sf.
DR   InterPro; IPR023577; CYTH_domain.
DR   PANTHER; PTHR21028; PTHR21028; 1.
DR   Pfam; PF01928; CYTH; 1.
DR   SMART; SM01118; CYTH; 1.
DR   SUPFAM; SSF55154; SSF55154; 1.
DR   TIGRFAMs; TIGR00318; cyaB; 1.
DR   PROSITE; PS51707; CYTH; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; cAMP biosynthesis; Cytoplasm; Direct protein sequencing;
KW   Lyase; Nucleotide-binding.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:9642185"
FT   CHAIN           2..191
FT                   /note="Adenylate cyclase CyaB"
FT                   /id="PRO_0000426738"
FT   DOMAIN          9..180
FT                   /note="CYTH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01044"
FT   ACT_SITE        46
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   191 AA;  21509 MW;  00E3A45E44323D4E CRC64;
     MSSQHFQGRF EVEFKYRLSD VDAFTCALAA LNPEVMLEDN QEQDSYFDTP EHSLAAEGKS
     LVIRTMQPSG IQLWIVKGPE ADRCEAVNIT DADKAASMLR TLGYRQVLAI SKRRSIYFVG
     PFHVTRDHLE GIGDFAELAI MTDDEALLPD YRQQLQDLAT RLGLSSAQLE TRSYRTLCEQ
     SLTLNSEKVP S