MOAC_CLOAB
ID MOAC_CLOAB Reviewed; 161 AA.
AC Q97HL9;
DT 19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 1.
DT 03-AUG-2022, entry version 103.
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=CA_C1992;
OS Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710
OS / VKM B-1787).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=272562;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787;
RX PubMed=11466286; DOI=10.1128/jb.183.16.4823-4838.2001;
RA Noelling J., Breton G., Omelchenko M.V., Makarova K.S., Zeng Q., Gibson R.,
RA Lee H.M., Dubois J., Qiu D., Hitti J., Wolf Y.I., Tatusov R.L., Sabathe F.,
RA Doucette-Stamm L.A., Soucaille P., Daly M.J., Bennett G.N., Koonin E.V.,
RA Smith D.R.;
RT "Genome sequence and comparative analysis of the solvent-producing
RT bacterium Clostridium acetobutylicum.";
RL J. Bacteriol. 183:4823-4838(2001).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE001437; AAK79951.1; -; Genomic_DNA.
DR PIR; D97145; D97145.
DR RefSeq; NP_348611.1; NC_003030.1.
DR RefSeq; WP_010965292.1; NC_003030.1.
DR AlphaFoldDB; Q97HL9; -.
DR SMR; Q97HL9; -.
DR STRING; 272562.CA_C1992; -.
DR EnsemblBacteria; AAK79951; AAK79951; CA_C1992.
DR GeneID; 44998480; -.
DR KEGG; cac:CA_C1992; -.
DR PATRIC; fig|272562.8.peg.2199; -.
DR eggNOG; COG0315; Bacteria.
DR HOGENOM; CLU_074693_1_1_9; -.
DR OMA; IWDMVKS; -.
DR OrthoDB; 1595361at2; -.
DR UniPathway; UPA00344; -.
DR Proteomes; UP000000814; 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; -; 1.
DR HAMAP; MF_01224_B; MoaC_B; 1.
DR InterPro; IPR023045; Mo_CF_biosynth-C.
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..161
FT /note="Cyclic pyranopterin monophosphate synthase"
FT /id="PRO_0000097793"
FT ACT_SITE 129
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01224"
FT BINDING 76..78
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01224"
FT BINDING 114..115
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01224"
SQ SEQUENCE 161 AA; 17481 MW; 7953EEE25809F6B9 CRC64;
MSEVFTHINE EGRARMVDVS EKDNTIRQAI ASGKISMEKD TLERIKEGTI SKGDVLAVAQ
VGGIMGAKST SQIIPMCHNI LISNCDINFK FDFENSEIEI VAMTKTVGKT GIEMEALTAV
SAAALTIYDM CKAIDREMVI SDIMLVKKSG GKSGDFERVG L
