ID   A8G849_SERP5            Unreviewed;       850 AA.
AC   A8G849;
DT   13-NOV-2007, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2007, sequence version 1.
DT   27-MAR-2024, entry version 74.
DE   RecName: Full=Adenylate cyclase {ECO:0000256|ARBA:ARBA00021420, ECO:0000256|RuleBase:RU000604};
DE            EC=4.6.1.1 {ECO:0000256|ARBA:ARBA00012201, ECO:0000256|RuleBase:RU000604};
GN   OrderedLocusNames=Spro_0179 {ECO:0000313|EMBL:ABV39289.1};
OS   Serratia proteamaculans (strain 568).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Serratia.
OX   NCBI_TaxID=399741 {ECO:0000313|EMBL:ABV39289.1};
RN   [1] {ECO:0000313|EMBL:ABV39289.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=568 {ECO:0000313|EMBL:ABV39289.1};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Taghavi S., Newman L.,
RA   Vangronsveld J., van der Lelie D., Richardson P.;
RT   "Complete sequence of chromosome of Serratia proteamaculans 568.";
RL   Submitted (SEP-2007) to the EMBL/GenBank/DDBJ databases.
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:0000256|ARBA:ARBA00001593,
CC         ECO:0000256|RuleBase:RU000604};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC       ECO:0000256|RuleBase:RU000604}.
CC   -!- SIMILARITY: Belongs to the adenylyl cyclase class-1 family.
CC       {ECO:0000256|ARBA:ARBA00007901, ECO:0000256|RuleBase:RU004184}.
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DR   EMBL; CP000826; ABV39289.1; -; Genomic_DNA.
DR   AlphaFoldDB; A8G849; -.
DR   STRING; 399741.Spro_0179; -.
DR   KEGG; spe:Spro_0179; -.
DR   eggNOG; COG3072; Bacteria.
DR   HOGENOM; CLU_013280_0_0_6; -.
DR   OrthoDB; 5571448at2; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004016; F:adenylate cyclase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0006171; P:cAMP biosynthetic process; IEA:UniProtKB-KW.
DR   InterPro; IPR000274; Adenylate_cyclase_1.
DR   InterPro; IPR024686; Adenylate_cyclase_1_CS.
DR   InterPro; IPR024685; Adenylate_cyclase_1_N.
DR   PANTHER; PTHR38760; ADENYLATE CYCLASE; 1.
DR   PANTHER; PTHR38760:SF1; ADENYLATE CYCLASE; 1.
DR   Pfam; PF12633; Adenyl_cycl_N; 1.
DR   Pfam; PF01295; Adenylate_cycl; 1.
DR   PIRSF; PIRSF001444; Adenylate_cycl; 1.
DR   PROSITE; PS01092; ADENYLATE_CYCLASE_1_1; 1.
DR   PROSITE; PS01093; ADENYLATE_CYCLASE_1_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   cAMP biosynthesis {ECO:0000256|ARBA:ARBA00022998,
KW   ECO:0000256|RuleBase:RU000604}; Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU000604};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}.
FT   DOMAIN          5..200
FT                   /note="Adenylate cyclase class-I N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF12633"
SQ   SEQUENCE   850 AA;  97164 MW;  520B8FCCA14CE5EC CRC64;
     MYLYIETLKQ RLDAINQLRI DRALAAMKPA FQRVYSLLPT LLHHHHPLMP GYLNGNVPHG
     VCIYTPDETQ QEYLNDLEDK WGSPFDKPAS GELPITGVYS MGSTSSIGQS CSSDLDIWVC
     HQSWLDNEER NRLQQKCSLL EKWAASMGVE VSFFLIDENR FRHNESGSLG GEDCGSTQHI
     LLLDEFYRTA VRLAGKRILW NMVPGDEESH YDEYVLSLYS QGALTPNEWL DLGGLGTLSA
     EEYFGASLWQ LYKSIDSPYK AVLKTLLLEA YSWEYPNTQL LAMDIKQRLH QGEIVCFGLD
     AYCMMLERVT HYLNAINDTT RLDLVRRCFY LKVCEKLSRA NACVGWRREI LSQLVSEWGW
     DEERLAILDN RANWKIARVR EAHNELLDAM MQSYRNLIRF ARRNNLSVSA SPQDIGVLTR
     KLYAAFEALP GKVTLVNPQI SPDLSEDDLT FIHVPIGRAN RTGWYLYNQA PAMDSIVSHQ
     PLEYNRYLNK LVAWAYFNGL LTPKTRLHIK SGNLCDTAKL QELVADVSHH FPLRLAAPTP
     KALYSPCEIR HLAIIVNLEN DPTAAFRNQV VHFDFRKLDV FSFGQQQQCL VGSIDLLYRN
     SWNEVRTLHF SGEQSVLEAL KTILGKMHQD AAPPESVEVF CYSQHLRGLI RTRIQQLVSE
     CIELRLSSTR LEPGRFKAVR VAGQTWGLFF ERLSVSVQKL ENAVEFYGAI SNNKLHGLSI
     KVETDQVHLP PVVDGFASEG IIQFFFEDTS DDKGFNIYIL DESNRVEVYH HCEGSKEELV
     RDVSRFYSSS HDRFTYGSSF INFNLPQFYQ IVQLDGRTQV IPFRSNVLSS LCVPLTDGAA
     QPLKQQFQLH
//