ID   MOAC_PYRHO              Reviewed;         159 AA.
AC   O59475;
DT   19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   03-AUG-2022, entry version 115.
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=PH1811;
OS   Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC
OS   100139 / OT-3).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Pyrococcus.
OX   NCBI_TaxID=70601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3;
RX   PubMed=9679194; DOI=10.1093/dnares/5.2.55;
RA   Kawarabayasi Y., Sawada M., Horikawa H., Haikawa Y., Hino Y., Yamamoto S.,
RA   Sekine M., Baba S., Kosugi H., Hosoyama A., Nagai Y., Sakai M., Ogura K.,
RA   Otsuka R., Nakazawa H., Takamiya M., Ohfuku Y., Funahashi T., Tanaka T.,
RA   Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K., Yoshizawa T.,
RA   Nakamura Y., Robb F.T., Horikoshi K., Masuchi Y., Shizuya H., Kikuchi H.;
RT   "Complete sequence and gene organization of the genome of a hyper-
RT   thermophilic archaebacterium, Pyrococcus horikoshii OT3.";
RL   DNA Res. 5:55-76(1998).
RN   [2]
RP   X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS).
RG   RIKEN structural genomics initiative (RSGI);
RT   "Structure of PH1811 protein from Pyrococcus horikoshii.";
RL   Submitted (JUL-2011) to the PDB data bank.
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; BA000001; BAA30930.1; -; Genomic_DNA.
DR   PIR; C71192; C71192.
DR   RefSeq; WP_010885871.1; NC_000961.1.
DR   PDB; 2EKN; X-ray; 2.05 A; A/B/C=1-159.
DR   PDBsum; 2EKN; -.
DR   AlphaFoldDB; O59475; -.
DR   SMR; O59475; -.
DR   STRING; 70601.3258247; -.
DR   EnsemblBacteria; BAA30930; BAA30930; BAA30930.
DR   GeneID; 1442653; -.
DR   KEGG; pho:PH1811; -.
DR   eggNOG; arCOG01530; Archaea.
DR   OMA; IWDMVKS; -.
DR   OrthoDB; 104538at2157; -.
DR   UniPathway; UPA00344; -.
DR   EvolutionaryTrace; O59475; -.
DR   Proteomes; UP000000752; 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.
FT   CHAIN           1..159
FT                   /note="Probable cyclic pyranopterin monophosphate synthase"
FT                   /id="PRO_0000097861"
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"
FT   STRAND          24..35
FT                   /evidence="ECO:0007829|PDB:2EKN"
FT   HELIX           38..46
FT                   /evidence="ECO:0007829|PDB:2EKN"
FT   HELIX           54..72
FT                   /evidence="ECO:0007829|PDB:2EKN"
FT   STRAND          81..90
FT                   /evidence="ECO:0007829|PDB:2EKN"
FT   STRAND          92..107
FT                   /evidence="ECO:0007829|PDB:2EKN"
FT   HELIX           110..132
FT                   /evidence="ECO:0007829|PDB:2EKN"
FT   STRAND          143..155
FT                   /evidence="ECO:0007829|PDB:2EKN"
SQ   SEQUENCE   159 AA;  17652 MW;  F202D4E875F026EA CRC64;
     MVGGLTHVDE KGVKMVEIGY KDVVFRKAVA KGRIKLKPET VKLIKEGKIE KGNVLATAQI
     AGILAVKRTP ELIPLCHPIP ITGVDITFDF GEDYIEVTCE VRAYYKTGVE MEALTGVTVA
     LLAIWDMVKA VEKDEKGQYP YTRIENVHVV EKVKTHNSQ