ID   MOAC_METKA              Reviewed;         156 AA.
AC   Q8TXV5;
DT   19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   03-AUG-2022, entry version 90.
DE   RecName: Full=Probable 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=MK0554;
OS   Methanopyrus kandleri (strain AV19 / DSM 6324 / JCM 9639 / NBRC 100938).
OC   Archaea; Euryarchaeota; Methanopyri; Methanopyrales; Methanopyraceae;
OC   Methanopyrus.
OX   NCBI_TaxID=190192;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AV19 / DSM 6324 / JCM 9639 / NBRC 100938;
RX   PubMed=11930014; DOI=10.1073/pnas.032671499;
RA   Slesarev A.I., Mezhevaya K.V., Makarova K.S., Polushin N.N.,
RA   Shcherbinina O.V., Shakhova V.V., Belova G.I., Aravind L., Natale D.A.,
RA   Rogozin I.B., Tatusov R.L., Wolf Y.I., Stetter K.O., Malykh A.G.,
RA   Koonin E.V., Kozyavkin S.A.;
RT   "The complete genome of hyperthermophile Methanopyrus kandleri AV19 and
RT   monophyly of archaeal methanogens.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:4644-4649(2002).
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; AE009439; AAM01769.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q8TXV5; -.
DR   SMR; Q8TXV5; -.
DR   STRING; 190192.MK0554; -.
DR   EnsemblBacteria; AAM01769; AAM01769; MK0554.
DR   KEGG; mka:MK0554; -.
DR   PATRIC; fig|190192.8.peg.589; -.
DR   HOGENOM; CLU_074693_1_2_2; -.
DR   OMA; IWDMVKS; -.
DR   UniPathway; UPA00344; -.
DR   Proteomes; UP000001826; 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; cd01419; MoaC_A; 1.
DR   Gene3D; 3.30.70.640; -; 1.
DR   HAMAP; MF_01224_A; MoaC_A; 1.
DR   InterPro; IPR023047; Mo_CF_biosynth-C_arc.
DR   InterPro; IPR036522; MoaC_sf.
DR   InterPro; IPR002820; Mopterin_CF_biosynth-C_dom.
DR   Pfam; PF01967; MoaC; 1.
DR   SUPFAM; SSF55040; SSF55040; 1.
PE   3: Inferred from homology;
KW   Lyase; Molybdenum cofactor biosynthesis; Reference proteome.
FT   CHAIN           1..156
FT                   /note="Probable cyclic pyranopterin monophosphate synthase"
FT                   /id="PRO_0000097855"
FT   ACT_SITE        124
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01224"
FT   BINDING         109..110
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01224"
SQ   SEQUENCE   156 AA;  17004 MW;  936C82A4FEE5D965 CRC64;
     MTAGGRRMSM VDVTGKKEEI RIAEASGFLR LTEDGVNAVK SGESHPQGKG DPIEVAKVAA
     ILAVKKTPEL VPHCHPIKIT GVDVDVEVLE DGVKMSVRVK SEGKTGVEMD ALTGLVVGLV
     TLWDMVKYAE KDEEGQYPHT RIENVRVVEK IIKEKE