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Database: UniProt
Entry: MOAC_COREF
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Original site: MOAC_COREF 
ID   MOAC_COREF              Reviewed;         155 AA.
AC   Q8FU35;
DT   30-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   24-JAN-2024, entry version 100.
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=CE0186;
OS   Corynebacterium efficiens (strain DSM 44549 / YS-314 / AJ 12310 / JCM 11189
OS   / NBRC 100395).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC   Corynebacteriaceae; Corynebacterium.
OX   NCBI_TaxID=196164;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44549 / YS-314 / AJ 12310 / JCM 11189 / NBRC 100395;
RX   PubMed=12840036; DOI=10.1101/gr.1285603;
RA   Nishio Y., Nakamura Y., Kawarabayasi Y., Usuda Y., Kimura E., Sugimoto S.,
RA   Matsui K., Yamagishi A., Kikuchi H., Ikeo K., Gojobori T.;
RT   "Comparative complete genome sequence analysis of the amino acid
RT   replacements responsible for the thermostability of Corynebacterium
RT   efficiens.";
RL   Genome Res. 13:1572-1579(2003).
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; BA000035; BAC16996.1; -; Genomic_DNA.
DR   RefSeq; WP_006768504.1; NZ_GG700684.1.
DR   AlphaFoldDB; Q8FU35; -.
DR   SMR; Q8FU35; -.
DR   STRING; 196164.gene:10740577; -.
DR   KEGG; cef:CE0186; -.
DR   eggNOG; COG0315; Bacteria.
DR   HOGENOM; CLU_074693_1_1_11; -.
DR   OMA; IWDMVKS; -.
DR   OrthoDB; 9794429at2; -.
DR   UniPathway; UPA00344; -.
DR   Proteomes; UP000001409; 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; Molybdopterin cofactor biosynthesis C (MoaC) domain; 1.
DR   HAMAP; MF_01224_B; MoaC_B; 1.
DR   InterPro; IPR023045; MoaC.
DR   InterPro; IPR047594; MoaC_bact/euk.
DR   InterPro; IPR036522; MoaC_sf.
DR   InterPro; IPR002820; Mopterin_CF_biosynth-C_dom.
DR   NCBIfam; TIGR00581; moaC; 1.
DR   Pfam; PF01967; MoaC; 1.
DR   SUPFAM; SSF55040; Molybdenum cofactor biosynthesis protein C, MoaC; 1.
PE   3: Inferred from homology;
KW   Lyase; Molybdenum cofactor biosynthesis; Reference proteome.
FT   CHAIN           1..155
FT                   /note="Cyclic pyranopterin monophosphate synthase"
FT                   /id="PRO_0000097795"
FT   ACT_SITE        126
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         111..112
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01224"
SQ   SEQUENCE   155 AA;  16341 MW;  C4D40A3D4A6333D8 CRC64;
     MSELTHVRAD GSAHMVDVTA KAETSRTAVA EGFVRTRADV VDKLFTADLP KGDALPVARV
     AGIMGAKKTP EIIPLCHPLP LGKITVDFER LPDGVRIEAS VKTRGVTGVE MEALTAVTTA
     ALTVYDMIKA VDKMAVIDGV RVLAKTGGKS GDWSV
//
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