ID C7NXC5_HALMD Unreviewed; 269 AA.
AC C7NXC5;
DT 13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT 13-OCT-2009, sequence version 1.
DT 27-MAR-2024, entry version 62.
DE RecName: Full=Diadenylate cyclase {ECO:0000256|HAMAP-Rule:MF_00840};
DE Short=DAC {ECO:0000256|HAMAP-Rule:MF_00840};
DE EC=2.7.7.85 {ECO:0000256|HAMAP-Rule:MF_00840};
DE AltName: Full=Cyclic-di-AMP synthase {ECO:0000256|HAMAP-Rule:MF_00840};
DE Short=c-di-AMP synthase {ECO:0000256|HAMAP-Rule:MF_00840};
GN Name=dacZ {ECO:0000256|HAMAP-Rule:MF_00840};
GN OrderedLocusNames=Hmuk_2246 {ECO:0000313|EMBL:ACV48359.1};
OS Halomicrobium mukohataei (strain ATCC 700874 / DSM 12286 / JCM 9738 / NCIMB
OS 13541) (Haloarcula mukohataei).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Haloarculaceae; Halomicrobium.
OX NCBI_TaxID=485914 {ECO:0000313|EMBL:ACV48359.1, ECO:0000313|Proteomes:UP000001746};
RN [1] {ECO:0000313|EMBL:ACV48359.1, ECO:0000313|Proteomes:UP000001746}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700874 / DSM 12286 / JCM 9738 / NCIMB 13541
RC {ECO:0000313|Proteomes:UP000001746};
RX PubMed=21304667; DOI=10.4056/sigs.42644;
RA Tindall B.J., Schneider S., Lapidus A., Copeland A., Glavina Del Rio T.,
RA Nolan M., Lucas S., Chen F., Tice H., Cheng J.F., Saunders E., Bruce D.,
RA Goodwin L., Pitluck S., Mikhailova N., Pati A., Ivanova N., Mavrommatis K.,
RA Chen A., Palaniappan K., Chain P., Land M., Hauser L., Chang Y.J.,
RA Jeffries C.D., Brettin T., Han C., Rohde M., Goker M., Bristow J.,
RA Eisen J.A., Markowitz V., Hugenholtz P., Klenk H.P., Kyrpides N.C.,
RA Detter J.C.;
RT "Complete genome sequence of Halomicrobium mukohataei type strain (arg-
RT 2).";
RL Stand. Genomic Sci. 1:270-277(2009).
CC -!- FUNCTION: Diadenylate cyclase that catalyzes the condensation of 2 ATP
CC molecules into cyclic di-AMP (c-di-AMP). c-di-AMP is a second messenger
CC for intracellular signal transduction involved in the control of
CC important regulatory processes such as osmoregulation.
CC {ECO:0000256|HAMAP-Rule:MF_00840}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 ATP = 3',3'-c-di-AMP + 2 diphosphate; Xref=Rhea:RHEA:35655,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:71500; EC=2.7.7.85;
CC Evidence={ECO:0000256|ARBA:ARBA00000877, ECO:0000256|HAMAP-
CC Rule:MF_00840};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00840};
CC -!- SIMILARITY: Belongs to the adenylate cyclase family. DacZ subfamily.
CC {ECO:0000256|HAMAP-Rule:MF_00840}.
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DR EMBL; CP001688; ACV48359.1; -; Genomic_DNA.
DR RefSeq; WP_015763201.1; NC_013202.1.
DR AlphaFoldDB; C7NXC5; -.
DR STRING; 485914.Hmuk_2246; -.
DR GeneID; 8411787; -.
DR KEGG; hmu:Hmuk_2246; -.
DR eggNOG; arCOG04453; Archaea.
DR HOGENOM; CLU_063222_0_0_2; -.
DR OrthoDB; 85944at2157; -.
DR Proteomes; UP000001746; Chromosome.
DR GO; GO:0004016; F:adenylate cyclase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0106408; F:diadenylate cyclase activity; IEA:UniProtKB-EC.
DR GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0019932; P:second-messenger-mediated signaling; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.1700.10; DNA integrity scanning protein, DisA, N-terminal domain; 1.
DR HAMAP; MF_00840; DacZ; 1.
DR InterPro; IPR014499; DAC_DacZ.
DR InterPro; IPR045586; DacZ_N.
DR InterPro; IPR036888; DNA_integrity_DisA_N_sf.
DR InterPro; IPR003390; DNA_integrity_scan_DisA_N.
DR NCBIfam; NF041371; Diadnylcyc_Halo; 1.
DR PANTHER; PTHR34185; DIADENYLATE CYCLASE; 1.
DR PANTHER; PTHR34185:SF1; DIADENYLATE CYCLASE; 1.
DR Pfam; PF02457; DAC; 1.
DR Pfam; PF19294; DACZ_N; 1.
DR PIRSF; PIRSF019073; UCP019073; 1.
DR SUPFAM; SSF143597; YojJ-like; 1.
DR PROSITE; PS51794; DAC; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_00840}; Manganese {ECO:0000256|HAMAP-Rule:MF_00840};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00840};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695, ECO:0000256|HAMAP-
KW Rule:MF_00840}; Reference proteome {ECO:0000313|Proteomes:UP000001746};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00840}.
FT DOMAIN 96..266
FT /note="DAC"
FT /evidence="ECO:0000259|PROSITE:PS51794"
SQ SEQUENCE 269 AA; 29102 MW; C585B12169BD5DC9 CRC64;
MSALREFLDD IVADTDAVFL FSPSASLYQS FEDDDTEVVV IAPENTVDAE TFVELPLEFT
NMADRIRFGV EGALEQEYVE EDADVVCIGD VFDDTPDSIV RVQVAEFSPS GVYGLFVNSR
AEPSVINDVL DVAIELGKKG QKGKPVGALF VVGDAGKVMN KSRPLSYNPF EKSHVHVGDP
IVNVMLKEFS RLDGAFVISD GGKIVSAYRY LEPSAEGVDI PKGLGARHMA AGAVTRDTNA
IAIVLSESDG LVRAFKSGEL ILEVDPEEY
//
