ID   Y1264_MYCTO             Reviewed;         397 AA.
AC   P9WMU8; L0T7S0; Q11055;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   03-AUG-2022, entry version 35.
DE   RecName: Full=pH-sensitive adenylate cyclase MT1302;
DE            EC=4.6.1.1;
DE   AltName: Full=ATP pyrophosphate-lyase;
DE   AltName: Full=Adenylyl cyclase;
GN   OrderedLocusNames=MT1302;
OS   Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83331;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC 1551 / Oshkosh;
RX   PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA   Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA   Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA   Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA   Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA   Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT   "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT   laboratory strains.";
RL   J. Bacteriol. 184:5479-5490(2002).
CC   -!- FUNCTION: Catalyzes the formation of the second messenger cAMP.
CC       {ECO:0000250}.
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   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC       Note=The isolated catalytic domain prefers Mn(2+) over Mg(2+) as a
CC       cofactor. {ECO:0000250};
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the adenylyl cyclase class-4/guanylyl cyclase
CC       family. {ECO:0000255|PROSITE-ProRule:PRU00099}.
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DR   EMBL; AE000516; AAK45561.1; -; Genomic_DNA.
DR   PIR; H70753; H70753.
DR   RefSeq; WP_003406372.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WMU8; -.
DR   SMR; P9WMU8; -.
DR   EnsemblBacteria; AAK45561; AAK45561; MT1302.
DR   KEGG; mtc:MT1302; -.
DR   PATRIC; fig|83331.31.peg.1406; -.
DR   HOGENOM; CLU_043761_2_0_11; -.
DR   Proteomes; UP000001020; Chromosome.
DR   GO; GO:0004016; F:adenylate cyclase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0008289; F:lipid 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   Gene3D; 3.30.70.1230; -; 1.
DR   InterPro; IPR001054; A/G_cyclase.
DR   InterPro; IPR032026; Ad_Cy_reg.
DR   InterPro; IPR029787; Nucleotide_cyclase.
DR   Pfam; PF16701; Ad_Cy_reg; 1.
DR   Pfam; PF00211; Guanylate_cyc; 1.
DR   SMART; SM00044; CYCc; 1.
DR   SUPFAM; SSF55073; SSF55073; 1.
DR   PROSITE; PS50125; GUANYLATE_CYCLASE_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding; cAMP biosynthesis; Lipid-binding; Lyase; Magnesium; Manganese;
KW   Metal-binding; Nucleotide-binding.
FT   CHAIN           1..397
FT                   /note="pH-sensitive adenylate cyclase MT1302"
FT                   /id="PRO_0000427239"
FT   DOMAIN          217..325
FT                   /note="Guanylate cyclase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00099"
FT   REGION          1..191
FT                   /note="Regulatory domain"
FT                   /evidence="ECO:0000250"
FT   REGION          192..206
FT                   /note="Linker"
FT                   /evidence="ECO:0000250"
FT   REGION          211..397
FT                   /note="Catalytic domain"
FT                   /evidence="ECO:0000250"
FT   BINDING         222
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250|UniProtKB:P9WMU9"
FT   BINDING         261
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         265
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250|UniProtKB:P9WMU9"
FT   BINDING         298
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         312
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   397 AA;  42232 MW;  F6C212A181DB5AD3 CRC64;
     MTDHVREADD ANIDDLLGDL GGTARAERAK LVEWLLEQGI TPDEIRATNP PLLLATRHLV
     GDDGTYVSAR EISENYGVDL ELLQRVQRAV GLARVDDPDA VVHMRADGEA AARAQRFVEL
     GLNPDQVVLV VRVLAEGLSH AAEAMRYTAL EAIMRPGATE LDIAKGSQAL VSQIVPLLGP
     MIQDMLFMQL RHMMETEAVN AGERAAGKPL PGARQVTVAF ADLVGFTQLG EVVSAEELGH
     LAGRLAGLAR DLTAPPVWFI KTIGDAVMLV CPDPAPLLDT VLKLVEVVDT DNNFPRLRAG
     VASGMAVSRA GDWFGSPVNV ASRVTGVARP GAVLVADSVR EALGDAPEAD GFQWSFAGPR
     RLRGIRGDVR LFRVRRGATR TGSGGAAQDD DLAGSSP