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 27-MAR-2024, entry version 41.
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; Actinomycetota; Actinomycetes; Mycobacteriales; 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 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 CDD; cd07556; Nucleotidyl_cyc_III; 1.
DR Gene3D; 3.30.70.1230; Nucleotide cyclase; 1.
DR InterPro; IPR001054; A/G_cyclase.
DR InterPro; IPR032026; Ad_Cy_reg.
DR InterPro; IPR029787; Nucleotide_cyclase.
DR PANTHER; PTHR43081; ADENYLATE CYCLASE, TERMINAL-DIFFERENTIATION SPECIFIC-RELATED; 1.
DR PANTHER; PTHR43081:SF1; PH-SENSITIVE ADENYLATE CYCLASE RV1264; 1.
DR Pfam; PF16701; Ad_Cy_reg; 1.
DR Pfam; PF00211; Guanylate_cyc; 1.
DR SMART; SM00044; CYCc; 1.
DR SUPFAM; SSF55073; Nucleotide cyclase; 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; Reference proteome.
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
//
