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
//