CDNE_RHOMG
ID CDNE_RHOMG Reviewed; 288 AA.
AC G2SLH8;
DT 18-SEP-2019, integrated into UniProtKB/Swiss-Prot.
DT 16-NOV-2011, sequence version 1.
DT 03-AUG-2022, entry version 40.
DE RecName: Full=Cyclic UMP-AMP synthase {ECO:0000303|PubMed:30787435};
DE Short=cUMP-AMP synthase {ECO:0000303|PubMed:30787435};
DE EC=2.7.7.- {ECO:0000269|PubMed:30787435};
DE AltName: Full=3',3'-cUAMP synthase {ECO:0000305|PubMed:30787435};
DE AltName: Full=cGAS/DncV-like nucleotidyltransferase;
DE Short=CD-NTase;
GN Name=cdnE {ECO:0000303|PubMed:30787435};
GN ORFNames=Rhom172_2837 {ECO:0000312|EMBL:AEN74717.1};
OS Rhodothermus marinus (strain SG0.5JP17-172).
OG Plasmid pRHOM17201.
OC Bacteria; Bacteroidetes; Bacteroidetes Order II. Incertae sedis;
OC Rhodothermaceae; Rhodothermus.
OX NCBI_TaxID=762570;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SG0.5JP17-172; PLASMID=pRHOM17201;
RG US DOE Joint Genome Institute;
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Ovchinnikova G., Chertkov O., Detter J.C., Han C., Tapia R.,
RA Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Gladden J.,
RA Woyke T.;
RT "Complete sequence of plasmid 1 of Rhodothermus marinus SG0.5JP17-172.";
RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP CLASSIFICATION AND NOMENCLATURE.
RX PubMed=32839535; DOI=10.1038/s41564-020-0777-y;
RA Millman A., Melamed S., Amitai G., Sorek R.;
RT "Diversity and classification of cyclic-oligonucleotide-based anti-phage
RT signalling systems.";
RL Nat. Microbiol. 5:1608-1615(2020).
RN [3] {ECO:0007744|PDB:6E0K, ECO:0007744|PDB:6E0L}
RP X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF APOENZYME AND IN COMPLEX WITH
RP NON-HYDROLYSABLE ATP AND UTP AND MAGNESIUM, FUNCTION, CATALYTIC ACTIVITY,
RP COFACTOR, NOMENCLATURE, SIMILARITY, AND MUTAGENESIS OF ASN-166.
RX PubMed=30787435; DOI=10.1038/s41586-019-0953-5;
RA Whiteley A.T., Eaglesham J.B., de Oliveira Mann C.C., Morehouse B.R.,
RA Lowey B., Nieminen E.A., Danilchanka O., King D.S., Lee A.S.Y.,
RA Mekalanos J.J., Kranzusch P.J.;
RT "Bacterial cGAS-like enzymes synthesize diverse nucleotide signals.";
RL Nature 567:194-199(2019).
CC -!- FUNCTION: CBASS (cyclic oligonucleotide-based antiphage signaling
CC system) provides immunity against bacteriophage. The CD-NTase protein
CC synthesizes cyclic nucleotides in response to infection; these serve as
CC specific second messenger signals. The signals activate a diverse range
CC of effectors, leading to bacterial cell death and thus abortive phage
CC infection. A type I-B(UU) CBASS system (PubMed:32839535).
CC {ECO:0000303|PubMed:32839535, ECO:0000305}.
CC -!- FUNCTION: Cyclic dinucleotide synthase that catalyzes the synthesis of
CC 3'3'-cyclic UMP-AMP (cUMP-AMP) from UTP and ATP, a second messenger for
CC cell signal transduction. {ECO:0000269|PubMed:30787435}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + UTP = 3',3'-cUAMP + 2 diphosphate; Xref=Rhea:RHEA:60456,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:46398,
CC ChEBI:CHEBI:143809; Evidence={ECO:0000269|PubMed:30787435};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60457;
CC Evidence={ECO:0000305|PubMed:30787435};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:30787435};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000269|PubMed:30787435};
CC -!- SIMILARITY: Belongs to the CD-NTase family. E01 subfamily.
CC {ECO:0000305|PubMed:30787435}.
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DR EMBL; CP003030; AEN74717.1; -; Genomic_DNA.
DR PDB; 6E0K; X-ray; 1.60 A; A=1-288.
DR PDB; 6E0L; X-ray; 2.25 A; A=1-288.
DR PDBsum; 6E0K; -.
DR PDBsum; 6E0L; -.
DR AlphaFoldDB; G2SLH8; -.
DR SMR; G2SLH8; -.
DR EnsemblBacteria; AEN74717; AEN74717; Rhom172_2837.
DR KEGG; rmg:Rhom172_2837; -.
DR HOGENOM; CLU_080937_0_0_10; -.
DR Proteomes; UP000001280; Plasmid pRHOM17201.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016779; F:nucleotidyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-KW.
DR GO; GO:0009117; P:nucleotide metabolic process; IEA:UniProtKB-KW.
DR CDD; cd05400; NT_2-5OAS_ClassI-CCAase; 1.
DR Gene3D; 3.30.460.10; -; 1.
DR InterPro; IPR006116; NT_2-5OAS_ClassI-CCAase.
DR InterPro; IPR043519; NT_sf.
DR SUPFAM; SSF81301; SSF81301; 1.
DR PROSITE; PS50152; 25A_SYNTH_3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antiviral defense; ATP-binding; Magnesium; Metal-binding;
KW Nucleotide metabolism; Nucleotide-binding; Nucleotidyltransferase; Plasmid;
KW Transferase.
FT CHAIN 1..288
FT /note="Cyclic UMP-AMP synthase"
FT /id="PRO_0000447701"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 46..48
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:30787435"
FT BINDING 46
FT /ligand="UTP"
FT /ligand_id="ChEBI:CHEBI:46398"
FT /evidence="ECO:0000269|PubMed:30787435"
FT BINDING 60
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:30787435"
FT BINDING 62
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:30787435"
FT BINDING 62
FT /ligand="UTP"
FT /ligand_id="ChEBI:CHEBI:46398"
FT /evidence="ECO:0000269|PubMed:30787435"
FT BINDING 116..120
FT /ligand="UTP"
FT /ligand_id="ChEBI:CHEBI:46398"
FT /evidence="ECO:0000269|PubMed:30787435"
FT BINDING 129
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:30787435"
FT BINDING 166
FT /ligand="UTP"
FT /ligand_id="ChEBI:CHEBI:46398"
FT /evidence="ECO:0000269|PubMed:30787435"
FT BINDING 194
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:30787435"
FT BINDING 212
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:30787435"
FT BINDING 265
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:30787435"
FT MUTAGEN 166
FT /note="N->S: Loses pyrimidine specificity as this mutant
FT incorporates almost no UTP and instead predominantly
FT synthesizes c-di-AMP."
FT /evidence="ECO:0000269|PubMed:30787435"
FT HELIX 5..11
FT /evidence="ECO:0007829|PDB:6E0K"
FT HELIX 18..32
FT /evidence="ECO:0007829|PDB:6E0K"
FT STRAND 42..45
FT /evidence="ECO:0007829|PDB:6E0K"
FT HELIX 47..50
FT /evidence="ECO:0007829|PDB:6E0K"
FT STRAND 57..59
FT /evidence="ECO:0007829|PDB:6E0K"
FT STRAND 61..73
FT /evidence="ECO:0007829|PDB:6E0K"
FT HELIX 77..82
FT /evidence="ECO:0007829|PDB:6E0K"
FT HELIX 92..107
FT /evidence="ECO:0007829|PDB:6E0K"
FT HELIX 109..111
FT /evidence="ECO:0007829|PDB:6E0K"
FT STRAND 112..114
FT /evidence="ECO:0007829|PDB:6E0K"
FT STRAND 116..122
FT /evidence="ECO:0007829|PDB:6E0K"
FT STRAND 124..138
FT /evidence="ECO:0007829|PDB:6E0K"
FT STRAND 141..143
FT /evidence="ECO:0007829|PDB:6E0K"
FT STRAND 150..156
FT /evidence="ECO:0007829|PDB:6E0K"
FT TURN 158..160
FT /evidence="ECO:0007829|PDB:6E0K"
FT STRAND 163..166
FT /evidence="ECO:0007829|PDB:6E0K"
FT HELIX 168..181
FT /evidence="ECO:0007829|PDB:6E0K"
FT TURN 182..184
FT /evidence="ECO:0007829|PDB:6E0K"
FT HELIX 186..202
FT /evidence="ECO:0007829|PDB:6E0K"
FT HELIX 212..220
FT /evidence="ECO:0007829|PDB:6E0K"
FT HELIX 224..226
FT /evidence="ECO:0007829|PDB:6E0K"
FT HELIX 231..244
FT /evidence="ECO:0007829|PDB:6E0K"
FT HELIX 247..249
FT /evidence="ECO:0007829|PDB:6E0K"
FT STRAND 255..263
FT /evidence="ECO:0007829|PDB:6E0K"
FT HELIX 269..285
FT /evidence="ECO:0007829|PDB:6E0K"
SQ SEQUENCE 288 AA; 33874 MW; AC41551CECD2B115 CRC64;
MPVPESQLER WSHQGATTTA KKTHESIRAA LDRYKWPKGK PEVYLQGSYK NSTNIRGDSD
VDVVVQLNSV FMNNLTAEQK RRFGFVKSDY TWNDFYSDVE RALTDYYGAS KVRRGRKTLK
VETTYLPADV VVCIQYRKYP PNRKSEDDYI EGMTFYVPSE DRWVVNYPKL HYENGAAKNQ
QTNEWYKPTI RMFKNARTYL IEQGAPQDLA PSYFLECLLY NVPDSKFGGT FKDTFCSVIN
WLKRADLSKF RCQNGQDDLF GEFPEQWSEE KARRFLRYMD DLWTGWGQ
