ID Q8E9H1_SHEON Unreviewed; 804 AA. AC Q8E9H1; DT 01-MAR-2003, integrated into UniProtKB/TrEMBL. DT 01-MAR-2003, sequence version 1. DT 27-MAR-2024, entry version 101. DE RecName: Full=Adenylate cyclase {ECO:0000256|ARBA:ARBA00021420}; DE EC=4.6.1.1 {ECO:0000256|ARBA:ARBA00012201}; DE AltName: Full=ATP pyrophosphate-lyase {ECO:0000256|ARBA:ARBA00032597}; DE AltName: Full=Adenylyl cyclase {ECO:0000256|ARBA:ARBA00032637}; GN Name=cyaA {ECO:0000313|EMBL:AAN57281.1}; GN OrderedLocusNames=SO_4312 {ECO:0000313|EMBL:AAN57281.1}; OS Shewanella oneidensis (strain MR-1). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales; OC Shewanellaceae; Shewanella. OX NCBI_TaxID=211586 {ECO:0000313|EMBL:AAN57281.1, ECO:0000313|Proteomes:UP000008186}; RN [1] {ECO:0000313|EMBL:AAN57281.1, ECO:0000313|Proteomes:UP000008186} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MR-1 {ECO:0000313|EMBL:AAN57281.1, RC ECO:0000313|Proteomes:UP000008186}; RX PubMed=12368813; DOI=10.1038/nbt749; RA Heidelberg J.F., Paulsen I.T., Nelson K.E., Gaidos E.J., Nelson W.C., RA Read T.D., Eisen J.A., Seshadri R., Ward N., Methe B., Clayton R.A., RA Meyer T., Tsapin A., Scott J., Beanan M., Brinkac L., Daugherty S., RA DeBoy R.T., Dodson R.J., Durkin A.S., Haft D.H., Kolonay J.F., Madupu R., RA Peterson J.D., Umayam L.A., White O., Wolf A.M., Vamathevan J., Weidman J., RA Impraim M., Lee K., Berry K., Lee C., Mueller J., Khouri H., Gill J., RA Utterback T.R., McDonald L.A., Feldblyum T.V., Smith H.O., Venter J.C., RA Nealson K.H., Fraser C.M.; RT "Genome sequence of the dissimilatory metal ion-reducing bacterium RT Shewanella oneidensis."; RL Nat. Biotechnol. 20:1118-1123(2002). 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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. CC -!- SIMILARITY: Belongs to the adenylyl cyclase class-1 family. CC {ECO:0000256|ARBA:ARBA00007901, ECO:0000256|RuleBase:RU004184}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AE014299; AAN57281.1; -; Genomic_DNA. DR RefSeq; NP_719837.1; NC_004347.2. DR RefSeq; WP_011073971.1; NZ_CP053946.1. DR AlphaFoldDB; Q8E9H1; -. DR STRING; 211586.SO_4312; -. DR PaxDb; 211586-SO_4312; -. DR KEGG; son:SO_4312; -. DR PATRIC; fig|211586.12.peg.4175; -. DR eggNOG; COG3072; Bacteria. DR HOGENOM; CLU_013280_0_0_6; -. DR OrthoDB; 5571448at2; -. DR PhylomeDB; Q8E9H1; -. DR BioCyc; SONE211586:G1GMP-3983-MONOMER; -. DR Proteomes; UP000008186; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004016; F:adenylate cyclase activity; IBA:GO_Central. 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; 2. DR PROSITE; PS01092; ADENYLATE_CYCLASE_1_1; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|ARBA:ARBA00022840}; KW cAMP biosynthesis {ECO:0000256|ARBA:ARBA00022998}; KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490}; KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000313|EMBL:AAN57281.1}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}; KW Reference proteome {ECO:0000313|Proteomes:UP000008186}. FT DOMAIN 10..202 FT /note="Adenylate cyclase class-I N-terminal" FT /evidence="ECO:0000259|Pfam:PF12633" SQ SEQUENCE 804 AA; 92445 MW; 2CA3C230F766B7C3 CRC64; MDQQGHFPDI AERLNQVRIA RALALLSPLQ KHLFRLIPFL IQQNSVQYPG FVDPNTPCGI YGYKAGSLEA QACDVFKLPF IATEVDFYAF EGVYAMGSTA SFGQNAKSDV DVWLVHHADL CDDDLALIKL KTERLTAWFA EYQFEVNFYL VHPLQFCGDM SQRTVCQSSM AHEHSGSTQH WLLLEEFYRS QIRLAGKIIA WWPDAKLNPE LLSLGNVHEL PASEYFGASL WQLYKGLNKP HKALIKVLLL EAYASEYPHS QLLCDRLWQK TLAGDFSTAN DAYYAIYEVI EAYLLKQNDS RRLEIVRRCF YLKCGVFLSL SNQGKDWRYA KMQKLVQEWQ WPNSLITTLD DCEHWHSGQL NWFNEQLNEL LLASYQTLLR FASTHELNEG LKIEELGMLT RKLHTYFSQD EDQIAKLNLL WSRSVAEAEV TMVSSTKENQ YYLYRQGPKP LNLLGDSAIC KGKSPSALMI WACLNGVSTP ETKWYEFGQS KVKSQRLTDA SKRLLNFIDH DWRVSKLDLC QPWHFRKLIF ILNLDCDPTI GWRGQEMMVD VMNANVFSLG RKQENMLGAL DAICLNSWGE WQCHRFEGET AVLQALAFVT PGLRRATHPV DMDVISCSQR LRPQLKLAVK NLLKQTVRLC QQVQQSSTLV QPLQISHTRY GIFFNPLGMA YQDLSDAKSF YQQLARSHLV QLPRPELGDD PFSSMPNIIQ NFAAKGAIQY FLRQRTDSLD VFILDEENQL SHYVQSGSDM SELVNKVSHH YVFDEFYASK ARFNIPQFFH LVRVAGELTV RPFGVDMNNA NVEF //