ID A0A0J1H2S5_9GAMM Unreviewed; 855 AA.
AC A0A0J1H2S5;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 24-JAN-2024, entry version 21.
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:KLV06075.1};
GN ORFNames=ABT57_20160 {ECO:0000313|EMBL:KLV06075.1};
OS Photobacterium ganghwense.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Photobacterium.
OX NCBI_TaxID=320778 {ECO:0000313|EMBL:KLV06075.1, ECO:0000313|Proteomes:UP000035909};
RN [1] {ECO:0000313|EMBL:KLV06075.1, ECO:0000313|Proteomes:UP000035909}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22954 {ECO:0000313|EMBL:KLV06075.1,
RC ECO:0000313|Proteomes:UP000035909};
RA Machado H., Gram L.;
RT "Photobacterium galathea sp. nov.";
RL Submitted (MAY-2015) 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 -!- 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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KLV06075.1}.
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DR EMBL; LDOU01000023; KLV06075.1; -; Genomic_DNA.
DR RefSeq; WP_047887054.1; NZ_PYMI01000010.1.
DR AlphaFoldDB; A0A0J1H2S5; -.
DR STRING; 320778.ABT57_20160; -.
DR PATRIC; fig|320778.3.peg.4334; -.
DR OrthoDB; 5571448at2; -.
DR Proteomes; UP000035909; Unassembled WGS sequence.
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.
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:KLV06075.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000035909}.
FT DOMAIN 6..202
FT /note="Adenylate cyclase class-I N-terminal"
FT /evidence="ECO:0000259|Pfam:PF12633"
SQ SEQUENCE 855 AA; 97657 MW; D8555A288DA38464 CRC64;
MQNFITTLNS RLEQLNKIRL ERACGAMTAQ SEQVFNLLPV LLHYNHPAVP GYLDQTVPVG
IASFTASPMQ QQLIDDCALA CAATVTPPDA STRLPILGLY SMGSTASLGQ SLTSDLDIWV
VIRTDLPSDA RSALEAKCAL VSEWALVQGV EANFFLIDEN RFLDNFSEEM TGENCGSSQH
LLLLDEFYRS AVRLAGLSLL WFMVPPEMEE CYDDYIRYLE QGGFIRRDEW IDFGGLSRIP
AEEYFGSSLW QLYKSIDSPY KSVLKAILLE AYSWEYPHTQ LLSVDGKRRF FAIDRTEFCM
DAYYLMLEKV TRYLQRINDH RRLDLVRRCF YLKTHEKLTR QPASGSVPWR RKILEELTAN
WQWSEEVLLE LDSRRDWKVE QVKRAHNELL DALMLSYRNL IRFARRNNIT SAISPEDISI
LARKLYAAFE VLPGKVTLLN PQLSPDLHEQ DLTFIQVPAG RTNAAGWYLY KQSLDPVAIL
GRASLEHNRY LSKLVAWAYF NGLLTESTCL HSVVRTAAMD IDKLYQLVSD IRNTFPIRRP
QPSLQALSSP CEIRQLGLFI NLENDPTTEL KSRAVRFDFK NTDIFSYGPE QLCLVGSVDL
VYRNSWNEVR TLNFTGENAM LDALKTVLGK MHQDALPPES VDVFCYSKHM RGLIRNLVYQ
LVAECIEMRL KPVEQEKRRR FKAIRIGSQT HGLFFERRGV SVQKLENSVD FYSCISSNKL
IGSASLVMGK TDEPHPPEIV DAYASEGLIQ FFFEDCADGF NIYILDETNR IEVYRQCSGD
KDEMVHGVNR FYTSAHERFS YSANFINFNL PQFYDIVRGD NGETQVLPFK SGQQPTRRPA
PVMGGGAAVL NLSSR
//