ID   PYCC_MICEH              Reviewed;         305 AA.
AC   A0A1C5G2V9;
DT   25-MAY-2022, integrated into UniProtKB/Swiss-Prot.
DT   02-NOV-2016, sequence version 1.
DT   03-AUG-2022, entry version 10.
DE   RecName: Full=Uridylate cyclase {ECO:0000303|PubMed:34644530};
DE            EC=4.6.1.- {ECO:0000269|PubMed:34644530};
DE            EC=4.6.1.2 {ECO:0000269|PubMed:34644530};
DE   AltName: Full=Cyclic UMP synthase;
DE            Short=cUMP synthase {ECO:0000303|PubMed:34644530};
DE   AltName: Full=MePycC {ECO:0000303|PubMed:34644530};
GN   Name=pycC {ECO:0000303|PubMed:34644530};
GN   ORFNames=GA0070610_0182 {ECO:0000303|Ref.1};
OS   Micromonospora echinofusca.
OC   Bacteria; Actinobacteria; Micromonosporales; Micromonosporaceae;
OC   Micromonospora.
OX   NCBI_TaxID=47858;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 43913 / CIP 108946 / JCM 3327 / NBRC 14267 / 71-m68;
RA   Varghese N.;
RL   Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, AND CLASSIFICATION.
RC   STRAIN=DSM 43913 / CIP 108946 / JCM 3327 / NBRC 14267 / 71-m68;
RX   PubMed=34644530; DOI=10.1016/j.cell.2021.09.031;
RA   Tal N., Morehouse B.R., Millman A., Stokar-Avihail A., Avraham C.,
RA   Fedorenko T., Yirmiya E., Herbst E., Brandis A., Mehlman T.,
RA   Oppenheimer-Shaanan Y., Keszei A.F.A., Shao S., Amitai G., Kranzusch P.J.,
RA   Sorek R.;
RT   "Cyclic CMP and cyclic UMP mediate bacterial immunity against phages.";
RL   Cell 0:0-0(2021).
CC   -!- FUNCTION: Pycsar (pyrimidine cyclase system for antiphage resistance)
CC       provides immunity against bacteriophage. The pyrimidine cyclase (PycC)
CC       synthesizes cyclic nucleotides in response to infection; these serve as
CC       specific second messenger signals. The signals activate the adjacent
CC       effector, leading to bacterial cell death and abortive phage infection.
CC       A clade D Pycsar system. {ECO:0000305|PubMed:34644530}.
CC   -!- FUNCTION: The pyrimidine cyclase gene of a two-gene Pycsar system,
CC       generates cyclic UMP (cUMP) from UTP as well as cGMP from GTP to a
CC       lesser extent, has little to no activity on ATP or CTP
CC       (PubMed:34644530). Expression of this and adjacent effector MePycTM (AC
CC       A0A1C5G2D0) probably confers resistance to bacteriophage. The genes are
CC       probably only expressed in response to bacteriophage infection
CC       (Probable). {ECO:0000269|PubMed:34644530, ECO:0000305|PubMed:34644530}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=GTP = 3',5'-cyclic GMP + diphosphate; Xref=Rhea:RHEA:13665,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:37565, ChEBI:CHEBI:57746; EC=4.6.1.2;
CC         Evidence={ECO:0000269|PubMed:34644530};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=UTP = 3',5'-cyclic UMP + diphosphate; Xref=Rhea:RHEA:69603,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:46398, ChEBI:CHEBI:184387;
CC         Evidence={ECO:0000269|PubMed:34644530};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000250|UniProtKB:P0DV24};
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:A0A0J5ZXG5}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the adenylyl cyclase class-4/guanylyl cyclase
CC       family. Pyrimidine cyclase subfamily. {ECO:0000305|PubMed:34644530}.
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DR   EMBL; LT607733; SCG13990.1; -; Genomic_DNA.
DR   EnsemblBacteria; SCG13990; SCG13990; GA0070610_0182.
DR   Proteomes; UP000198251; Chromosome i.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR   GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.70.1230; -; 1.
DR   InterPro; IPR029787; Nucleotide_cyclase.
DR   SUPFAM; SSF55073; SSF55073; 1.
PE   1: Evidence at protein level;
KW   Antiviral defense; Cytoplasm; Lyase; Manganese; Metal-binding;
KW   Nucleotide-binding; Reference proteome.
FT   CHAIN           1..305
FT                   /note="Uridylate cyclase"
FT                   /id="PRO_0000455223"
FT   BINDING         58
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000305|PubMed:34644530"
FT   BINDING         58
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000305|PubMed:34644530"
FT   BINDING         102
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000305|PubMed:34644530"
FT   BINDING         102
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000305|PubMed:34644530"
SQ   SEQUENCE   305 AA;  33529 MW;  803427EE52AF3442 CRC64;
     MTEVDLKALL ADVDGDVATE LASKPEVIDK GHELDISTLP IQARKWHKLR DAVAVVADLK
     SSTQLGLNKH AASTASIYEA ATGGVVQIFD EFDANFVAIQ GDGAFALFWG DKRRQRAVCA
     GITIKTFSFK HLVPRLEKKW DGLPETGLKV GLGSSPLLVK RVGVPRTEHQ EPVWAGRAVN
     YAAKAAQQAD RHEMVVTGTI WDWVSDNDFL AVTCSCSNPN PDLWSNITIE KIPDGDGDRE
     GKRLTSSWCD VHGPEYCAAV LEGKKRRADV TTQRTSALAA EMKSWVRNKA AQDRKNRLAR
     YQGLH