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Database: UniProt
Entry: A0A1Y2SPB7_9GAMM
LinkDB: A0A1Y2SPB7_9GAMM
Original site: A0A1Y2SPB7_9GAMM 
ID   A0A1Y2SPB7_9GAMM        Unreviewed;       866 AA.
AC   A0A1Y2SPB7;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   24-JAN-2024, entry version 17.
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   ORFNames=Xbed_00899 {ECO:0000313|EMBL:OTA20922.1};
OS   Xenorhabdus beddingii.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Morganellaceae; Xenorhabdus.
OX   NCBI_TaxID=40578 {ECO:0000313|EMBL:OTA20922.1, ECO:0000313|Proteomes:UP000194204};
RN   [1] {ECO:0000313|EMBL:OTA20922.1, ECO:0000313|Proteomes:UP000194204}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 4764 {ECO:0000313|EMBL:OTA20922.1,
RC   ECO:0000313|Proteomes:UP000194204};
RA   Tobias N.J., Wolff H., Djahanschiri B., Ebersberger I., Bode H.B.;
RT   "Deconstructing symbiosis and pathogenesis requirements using a combined
RT   genomic-metabolomic approach.";
RL   Submitted (JAN-2017) 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}.
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:OTA20922.1}.
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DR   EMBL; MUBK01000005; OTA20922.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y2SPB7; -.
DR   STRING; 40578.Xbed_00899; -.
DR   OrthoDB; 5571448at2; -.
DR   Proteomes; UP000194204; 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.
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   866 AA;  99787 MW;  07390CFC96F3E0E0 CRC64;
     MYLYIETLKQ RLDAINQLRL ERATSSMSDA FKQVYSLIPV LLHYHHPMMP GYIKGNAPHG
     VCFFTPDESQ QFWINDLENQ LAGALSQTSN GELPITGIYS MGSTSSIGQS YSSDVDIWVC
     HQSWLDNDEK VLLEQKCTLI EQWAATLGIE VTFFLIDENR FRHNASGSLN GEDCGSTQHI
     LLLDEFYRTA VCMAGKRLLW AMVPVEEEAH YDEYVLSLYA QGVLTPNEWL DLGGLSELSA
     EEYFGASLWQ LYKSVDSPYK AVLKSLLLEA YSWEYPNGKL LAMEMKQYFH DGSIVSFGLD
     AYSMMLERVT RYLTATNDLT RLDLARRCFY LKVCEKLLDS RDDRGCTGWR RQVMSQLVHE
     WGWDGNKLAM LDNRSAWKIE QVREAHNELL DTMMQSYRNL IRFARRNNLS VSASPQDIGV
     LTRKLYAAFE ALPGKVTLVN PQISPDLSEQ DLTFIYVPPG RINRSGWYLY NRAPTIESII
     GYQPLEYNRY LNKLVSWTYF NGLLTKETRI HIHHGKSQCD RNKLCDLVND IATHFPIRLP
     APTPKALYSP CEIRHLAIIV NLEEDPTVAF SNQLVHFDLR KLNVFSFGEL QQCLVGSIDL
     LYRNSWNEVR TLHFSGEQSV LEALKTILGK MHQDAAPPSD VEVFCYSQHL SGLICTRIRQ
     LVSECIELRL SSNRQNPNRF KALRISGQTW GLFFERLNVS VQKLENAVEF YGAISNTKLH
     GLPVKIDTKE KHLPPVIDGF ACEGMIQFFF EDIENEQGFN IYILDESNRV EIYSHCEGSK
     EELVRDISRF YSSSHDRFTY GSSFINFNLP QFYQIIKKGE RTHVTPFVEG TFPLDEMETN
     NTRFHLDGRF EEPSRAHESY RSLYHY
//
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