ID   MOAC_SULTO              Reviewed;         151 AA.
AC   Q975D5;
DT   19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   03-AUG-2022, entry version 104.
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=STK_04720;
OS   Sulfurisphaera tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7)
OS   (Sulfolobus tokodaii).
OC   Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Sulfurisphaera.
OX   NCBI_TaxID=273063;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 16993 / JCM 10545 / NBRC 100140 / 7;
RX   PubMed=11572479; DOI=10.1093/dnares/8.4.123;
RA   Kawarabayasi Y., Hino Y., Horikawa H., Jin-no K., Takahashi M., Sekine M.,
RA   Baba S., Ankai A., Kosugi H., Hosoyama A., Fukui S., Nagai Y.,
RA   Nishijima K., Otsuka R., Nakazawa H., Takamiya M., Kato Y., Yoshizawa T.,
RA   Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K.,
RA   Masuda S., Yanagii M., Nishimura M., Yamagishi A., Oshima T., Kikuchi H.;
RT   "Complete genome sequence of an aerobic thermoacidophilic Crenarchaeon,
RT   Sulfolobus tokodaii strain7.";
RL   DNA Res. 8:123-140(2001).
RN   [2]
RP   X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS), AND SUBUNIT.
RX   PubMed=18607082; DOI=10.1107/s174430910801590x;
RA   Yoshida H., Yamada M., Kuramitsu S., Kamitori S.;
RT   "Structure of a putative molybdenum-cofactor biosynthesis protein C (MoaC)
RT   from Sulfolobus tokodaii (ST0472).";
RL   Acta Crystallogr. F 64:589-592(2008).
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, ECO:0000305|PubMed:18607082}.
CC   -!- SIMILARITY: Belongs to the MoaC family. {ECO:0000255|HAMAP-
CC       Rule:MF_01224}.
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DR   EMBL; BA000023; BAB65466.1; -; Genomic_DNA.
DR   RefSeq; WP_010978449.1; NC_003106.2.
DR   PDB; 2OHD; X-ray; 2.20 A; A/B/C/D/E/F=1-151.
DR   PDBsum; 2OHD; -.
DR   AlphaFoldDB; Q975D5; -.
DR   SMR; Q975D5; -.
DR   STRING; 273063.STK_04720; -.
DR   EnsemblBacteria; BAB65466; BAB65466; STK_04720.
DR   GeneID; 1458415; -.
DR   KEGG; sto:STK_04720; -.
DR   PATRIC; fig|273063.9.peg.547; -.
DR   eggNOG; arCOG01530; Archaea.
DR   OMA; IWDMVKS; -.
DR   OrthoDB; 104538at2157; -.
DR   BRENDA; 4.6.1.17; 15396.
DR   UniPathway; UPA00344; -.
DR   EvolutionaryTrace; Q975D5; -.
DR   Proteomes; UP000001015; 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; IPR023045; Mo_CF_biosynth-C.
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.
DR   TIGRFAMs; TIGR00581; moaC; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Lyase; Molybdenum cofactor biosynthesis; Reference proteome.
FT   CHAIN           1..151
FT                   /note="Probable cyclic pyranopterin monophosphate synthase"
FT                   /id="PRO_0000097865"
FT   ACT_SITE        117
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01224"
FT   BINDING         66..68
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01224"
FT   BINDING         102..103
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01224"
FT   STRAND          15..26
FT                   /evidence="ECO:0007829|PDB:2OHD"
FT   HELIX           29..36
FT                   /evidence="ECO:0007829|PDB:2OHD"
FT   HELIX           45..63
FT                   /evidence="ECO:0007829|PDB:2OHD"
FT   STRAND          74..82
FT                   /evidence="ECO:0007829|PDB:2OHD"
FT   STRAND          85..98
FT                   /evidence="ECO:0007829|PDB:2OHD"
FT   HELIX           101..118
FT                   /evidence="ECO:0007829|PDB:2OHD"
FT   HELIX           120..123
FT                   /evidence="ECO:0007829|PDB:2OHD"
FT   STRAND          134..143
FT                   /evidence="ECO:0007829|PDB:2OHD"
SQ   SEQUENCE   151 AA;  17125 MW;  A475C519B6ADDE27 CRC64;
     MTEAKIVDIS SKDIVLREAV VEGYIKLRKE TIEKIKNKEV EKGDVITVAK TAGILAAKKT
     PELIPMCHPI PLEFVDVEIK IEEEGLRVIS TVKAHYKTGV EMEALTATSV ALLTIWDMVK
     KYEKDENGQY PYTEIKSIRV INKIKTYDDM K