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MOAC_PSEE4
ID   MOAC_PSEE4              Reviewed;         156 AA.
AC   Q1I574;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-JUN-2006, sequence version 1.
DT   03-AUG-2022, entry version 89.
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=PSEEN4530;
OS   Pseudomonas entomophila (strain L48).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=384676;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=L48;
RX   PubMed=16699499; DOI=10.1038/nbt1212;
RA   Vodovar N., Vallenet D., Cruveiller S., Rouy Z., Barbe V., Acosta C.,
RA   Cattolico L., Jubin C., Lajus A., Segurens B., Vacherie B., Wincker P.,
RA   Weissenbach J., Lemaitre B., Medigue C., Boccard F.;
RT   "Complete genome sequence of the entomopathogenic and metabolically
RT   versatile soil bacterium Pseudomonas entomophila.";
RL   Nat. Biotechnol. 24:673-679(2006).
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; CT573326; CAK17211.1; -; Genomic_DNA.
DR   RefSeq; WP_011535579.1; NC_008027.1.
DR   AlphaFoldDB; Q1I574; -.
DR   SMR; Q1I574; -.
DR   STRING; 384676.PSEEN4530; -.
DR   EnsemblBacteria; CAK17211; CAK17211; PSEEN4530.
DR   KEGG; pen:PSEEN4530; -.
DR   eggNOG; COG0315; Bacteria.
DR   HOGENOM; CLU_074693_1_1_6; -.
DR   OMA; IWDMVKS; -.
DR   OrthoDB; 1595361at2; -.
DR   UniPathway; UPA00344; -.
DR   Proteomes; UP000000658; Chromosome.
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..156
FT                   /note="Cyclic pyranopterin monophosphate synthase"
FT                   /id="PRO_1000054120"
FT   ACT_SITE        125
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01224"
FT   BINDING         73..75
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01224"
FT   BINDING         110..111
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01224"
SQ   SEQUENCE   156 AA;  16707 MW;  28CF452022892512 CRC64;
     MLTHLDSQGR ANMVDVTEKA VTAREAIAEA RVRMLPDTLR MIVDGQHPKG DVFAVARIAG
     IQAAKKTSDL IPLCHPLMLT GVKVELAAEG EDVVHIVARC KLAGQTGVEM EALTAASVTA
     LTIYDMCKAV DKGMVIEQVR LLEKTGGKSG HYKVEA
 
 
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