MOAC_VIBPA
ID MOAC_VIBPA Reviewed; 159 AA.
AC Q87MY2;
DT 25-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 98.
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=VP2094;
OS Vibrio parahaemolyticus serotype O3:K6 (strain RIMD 2210633).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=223926;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RIMD 2210633;
RX PubMed=12620739; DOI=10.1016/s0140-6736(03)12659-1;
RA Makino K., Oshima K., Kurokawa K., Yokoyama K., Uda T., Tagomori K.,
RA Iijima Y., Najima M., Nakano M., Yamashita A., Kubota Y., Kimura S.,
RA Yasunaga T., Honda T., Shinagawa H., Hattori M., Iida T.;
RT "Genome sequence of Vibrio parahaemolyticus: a pathogenic mechanism
RT distinct from that of V. cholerae.";
RL Lancet 361:743-749(2003).
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; BA000031; BAC60357.1; -; Genomic_DNA.
DR RefSeq; NP_798473.1; NC_004603.1.
DR RefSeq; WP_005461493.1; NC_004603.1.
DR AlphaFoldDB; Q87MY2; -.
DR SMR; Q87MY2; -.
DR STRING; 223926.28807087; -.
DR EnsemblBacteria; BAC60357; BAC60357; BAC60357.
DR GeneID; 1189605; -.
DR KEGG; vpa:VP2094; -.
DR PATRIC; fig|223926.6.peg.2005; -.
DR eggNOG; COG0315; Bacteria.
DR HOGENOM; CLU_074693_1_1_6; -.
DR OMA; IWDMVKS; -.
DR UniPathway; UPA00344; -.
DR Proteomes; UP000002493; Chromosome 1.
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..159
FT /note="Cyclic pyranopterin monophosphate synthase"
FT /id="PRO_0000097842"
FT ACT_SITE 128
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 113..114
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01224"
SQ SEQUENCE 159 AA; 17126 MW; A9C62522F68EC407 CRC64;
MTQFTHINAS GEANMVDVSA KAETVREARA EAFVHMAPET LQLIVSGQHH KGDVFATARI
AGIQAAKKTW DLIPLCHPLL LSKVEVQLEA IEAENKVRIE SVCKLAGKTG VEMEALTAAS
VAALTIYDMC KAVQKDMVIG QVRLLEKTGG KSGHFKAES
