MOAC_THEKO
ID MOAC_THEKO Reviewed; 156 AA.
AC Q5JCX1;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 89.
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=TK0354;
OS Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)
OS (Pyrococcus kodakaraensis (strain KOD1)).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Thermococcus.
OX NCBI_TaxID=69014;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-918 / JCM 12380 / KOD1;
RX PubMed=15710748; DOI=10.1101/gr.3003105;
RA Fukui T., Atomi H., Kanai T., Matsumi R., Fujiwara S., Imanaka T.;
RT "Complete genome sequence of the hyperthermophilic archaeon Thermococcus
RT kodakaraensis KOD1 and comparison with Pyrococcus genomes.";
RL Genome Res. 15:352-363(2005).
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; AP006878; BAD84543.1; -; Genomic_DNA.
DR RefSeq; WP_011249309.1; NC_006624.1.
DR AlphaFoldDB; Q5JCX1; -.
DR SMR; Q5JCX1; -.
DR IntAct; Q5JCX1; 1.
DR MINT; Q5JCX1; -.
DR STRING; 69014.TK0354; -.
DR EnsemblBacteria; BAD84543; BAD84543; TK0354.
DR GeneID; 3234480; -.
DR KEGG; tko:TK0354; -.
DR PATRIC; fig|69014.16.peg.351; -.
DR eggNOG; arCOG01530; Archaea.
DR HOGENOM; CLU_074693_1_2_2; -.
DR InParanoid; Q5JCX1; -.
DR OMA; IWDMVKS; -.
DR OrthoDB; 104538at2157; -.
DR PhylomeDB; Q5JCX1; -.
DR UniPathway; UPA00344; -.
DR Proteomes; UP000000536; 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 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_0000097862"
FT ACT_SITE 125
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01224"
FT BINDING 74..76
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; 17295 MW; 26381E6B06B1FA27 CRC64;
MKDLTHVDEK GVKMVEVGHK DVVFRKAVAK GRIRLKPETI ELIKAGKTKK GNVIAAAQIA
GILAVKKTPE LIPLCHPIPL TGVDITFEFG DDYIEATCEV RAYYKTGVEM EALTGVSVAL
LTIWDMVKAV EKDENGQYPF TRIEDIRVVE KVKGEE
