ID CYA1_MYCBO Reviewed; 443 AA.
AC P0A4Y1; A0A1R3XYV0; O06142; O30820; X2BIV0;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 27-MAR-2024, entry version 111.
DE RecName: Full=Adenylate cyclase;
DE EC=4.6.1.1 {ECO:0000250|UniProtKB:P9WQ35};
DE AltName: Full=ATP pyrophosphate-lyase;
DE AltName: Full=Adenylyl cyclase;
GN Name=cya; OrderedLocusNames=BQ2027_MB1651C;
OS Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=233413;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-935 / AF2122/97;
RX PubMed=12788972; DOI=10.1073/pnas.1130426100;
RA Garnier T., Eiglmeier K., Camus J.-C., Medina N., Mansoor H., Pryor M.,
RA Duthoy S., Grondin S., Lacroix C., Monsempe C., Simon S., Harris B.,
RA Atkin R., Doggett J., Mayes R., Keating L., Wheeler P.R., Parkhill J.,
RA Barrell B.G., Cole S.T., Gordon S.V., Hewinson R.G.;
RT "The complete genome sequence of Mycobacterium bovis.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:7877-7882(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=ATCC BAA-935 / AF2122/97;
RX PubMed=28385856; DOI=10.1128/genomea.00157-17;
RA Malone K.M., Farrell D., Stuber T.P., Schubert O.T., Aebersold R.,
RA Robbe-Austerman S., Gordon S.V.;
RT "Updated reference genome sequence and annotation of Mycobacterium bovis
RT AF2122/97.";
RL Genome Announc. 5:E00157-E00157(2017).
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:0000250|UniProtKB:P9WQ35};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P9WQ35};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:P9WQ35};
CC Note=Binds 1 Mg(2+) ion per subunit. Is also active with manganese ions
CC (in vitro). {ECO:0000250|UniProtKB:P9WQ35};
CC -!- SUBUNIT: Homodimer. Can also exist as monomer.
CC {ECO:0000250|UniProtKB:P9WQ35}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P9WQ35};
CC Multi-pass membrane protein {ECO:0000250|UniProtKB:P9WQ35}.
CC -!- SIMILARITY: Belongs to the adenylyl cyclase class-4/guanylyl cyclase
CC family. {ECO:0000255|PROSITE-ProRule:PRU00099}.
CC -!- SEQUENCE CAUTION:
CC Sequence=SIU00255.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; LT708304; SIU00255.1; ALT_INIT; Genomic_DNA.
DR RefSeq; NP_855304.1; NC_002945.3.
DR RefSeq; WP_003408035.1; NC_002945.4.
DR AlphaFoldDB; P0A4Y1; -.
DR SMR; P0A4Y1; -.
DR GeneID; 45425593; -.
DR PATRIC; fig|233413.5.peg.1802; -.
DR Proteomes; UP000001419; Chromosome.
DR GO; GO:0005886; C:plasma membrane; 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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006171; P:cAMP biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR CDD; cd07302; CHD; 1.
DR Gene3D; 3.30.70.1230; Nucleotide cyclase; 1.
DR InterPro; IPR001054; A/G_cyclase.
DR InterPro; IPR018297; A/G_cyclase_CS.
DR InterPro; IPR048432; MASE7.
DR InterPro; IPR029787; Nucleotide_cyclase.
DR PANTHER; PTHR11920:SF335; GUANYLATE CYCLASE 32E; 1.
DR PANTHER; PTHR11920; GUANYLYL CYCLASE; 1.
DR Pfam; PF00211; Guanylate_cyc; 1.
DR Pfam; PF20967; MASE7; 1.
DR SMART; SM00044; CYCc; 1.
DR SUPFAM; SSF55073; Nucleotide cyclase; 1.
DR PROSITE; PS00452; GUANYLATE_CYCLASE_1; 1.
DR PROSITE; PS50125; GUANYLATE_CYCLASE_2; 1.
PE 3: Inferred from homology;
KW ATP-binding; cAMP biosynthesis; Cell membrane; Lyase; Magnesium; Manganese;
KW Membrane; Metal-binding; Nucleotide-binding; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..443
FT /note="Adenylate cyclase"
FT /id="PRO_0000195726"
FT TRANSMEM 47..69
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 74..93
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 98..120
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 124..143
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 148..167
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 180..202
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 203..443
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 251..378
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00099"
FT BINDING 256
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P9WQ35"
FT BINDING 300
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P9WQ35"
SQ SEQUENCE 443 AA; 47370 MW; 64B13168B4B792E2 CRC64;
MAARKCGAPP IAADGSTRRP DCVTAVRTQA RAPTQHYAES VARRQRVLTI TAWLAVVVTG
SFALMQLATG AGGWYIALIN VFTAVTFAIV PLLHRFGGLV APLTFIGTAY VAIFAIGWDV
GTDAGAQFFF LVAAALVVLL VGIEHTALAV GLAAVAAGLV IALEFLVPPD TGLQPPWAMS
VSFVLTTVSA CGVAVATVWF ALRDTARAEA VMEAEHDRSE ALLANMLPAS IAERLKEPER
NIIADKYDEA SVLFADIVGF TERASSTAPA DLVRFLDRLY SAFDELVDQH GLEKIKVSGD
SYMVVSGVPR PRPDHTQALA DFALDMTNVA AQLKDPRGNP VPLRVGLATG PVVAGVVGSR
RFFYDVWGDA VNVASRMEST DSVGQIQVPD EVYERLKDDF VLRERGHINV KGKGVMRTWY
LIGRKVAADP GEVRGAEPRT AGV
//
