ID   MOAC_YERPP              Reviewed;         159 AA.
AC   A4TNP7;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   15-MAY-2007, sequence version 1.
DT   03-AUG-2022, entry version 78.
DE   RecName: Full=Cyclic pyranopterin monophosphate synthase {ECO:0000255|HAMAP-Rule:MF_01224};
DE            EC=4.6.1.17 {ECO:0000255|HAMAP-Rule:MF_01224};
DE   AltName: Full=Molybdenum cofactor biosynthesis protein C {ECO:0000255|HAMAP-Rule:MF_01224};
GN   Name=moaC {ECO:0000255|HAMAP-Rule:MF_01224}; OrderedLocusNames=YPDSF_2537;
OS   Yersinia pestis (strain Pestoides F).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=386656;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pestoides F;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Di Bartolo G., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Worsham P., Chu M., Bearden S., Garcia E.,
RA   Richardson P.;
RT   "Complete sequence of chromosome of Yersinia pestis Pestoides F.";
RL   Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the conversion of (8S)-3',8-cyclo-7,8-
CC       dihydroguanosine 5'-triphosphate to cyclic pyranopterin monophosphate
CC       (cPMP). {ECO:0000255|HAMAP-Rule:MF_01224}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate = cyclic
CC         pyranopterin phosphate + diphosphate; Xref=Rhea:RHEA:49580,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:59648, ChEBI:CHEBI:131766;
CC         EC=4.6.1.17; Evidence={ECO:0000255|HAMAP-Rule:MF_01224};
CC   -!- PATHWAY: Cofactor biosynthesis; molybdopterin biosynthesis.
CC       {ECO:0000255|HAMAP-Rule:MF_01224}.
CC   -!- SUBUNIT: Homohexamer; trimer of dimers. {ECO:0000255|HAMAP-
CC       Rule:MF_01224}.
CC   -!- SIMILARITY: Belongs to the MoaC family. {ECO:0000255|HAMAP-
CC       Rule:MF_01224}.
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DR   EMBL; CP000668; ABP40909.1; -; Genomic_DNA.
DR   RefSeq; WP_002210772.1; NZ_CP009715.1.
DR   AlphaFoldDB; A4TNP7; -.
DR   SMR; A4TNP7; -.
DR   GeneID; 57977299; -.
DR   KEGG; ypp:YPDSF_2537; -.
DR   PATRIC; fig|386656.14.peg.4054; -.
DR   OMA; IWDMVKS; -.
DR   UniPathway; UPA00344; -.
DR   GO; GO:0061799; F:cyclic pyranopterin monophosphate synthase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006777; P:Mo-molybdopterin cofactor biosynthetic process; IEA:UniProtKB-UniRule.
DR   CDD; cd01420; MoaC_PE; 1.
DR   Gene3D; 3.30.70.640; -; 1.
DR   HAMAP; MF_01224_B; MoaC_B; 1.
DR   InterPro; IPR023045; Mo_CF_biosynth-C.
DR   InterPro; IPR036522; MoaC_sf.
DR   InterPro; IPR002820; Mopterin_CF_biosynth-C_dom.
DR   Pfam; PF01967; MoaC; 1.
DR   SUPFAM; SSF55040; SSF55040; 1.
DR   TIGRFAMs; TIGR00581; moaC; 1.
PE   3: Inferred from homology;
KW   Lyase; Molybdenum cofactor biosynthesis.
FT   CHAIN           1..159
FT                   /note="Cyclic pyranopterin monophosphate synthase"
FT                   /id="PRO_1000054167"
FT   ACT_SITE        128
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01224"
FT   BINDING         75..77
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01224"
FT   BINDING         113..114
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01224"
SQ   SEQUENCE   159 AA;  17225 MW;  20CFE4A9A3E7ECDE CRC64;
     MTQLTHINTA GEAHMVDVSA KNETVREARA EAFVDMQAAT LAMIIDGSHH KGDVFATARI
     AGIQAAKKTW ELIPLCHPLL LTKVEVKLEA QPEHNRVRIE TCCRLTGKTG VEMEALTAAS
     VAALTIYDMC KAVQKDMIIG PVRLLTKSGG KSGDFKVDI