ID G5H478_9FIRM Unreviewed; 160 AA.
AC G5H478;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE RecName: Full=Cyclic pyranopterin monophosphate synthase {ECO:0000256|ARBA:ARBA00012575, ECO:0000256|HAMAP-Rule:MF_01224};
DE EC=4.6.1.17 {ECO:0000256|ARBA:ARBA00012575, ECO:0000256|HAMAP-Rule:MF_01224};
DE AltName: Full=Molybdenum cofactor biosynthesis protein C {ECO:0000256|HAMAP-Rule:MF_01224};
GN Name=moaC {ECO:0000256|HAMAP-Rule:MF_01224};
GN ORFNames=HMPREF9432_01725 {ECO:0000313|EMBL:EHG24051.1};
OS Selenomonas noxia F0398.
OC Bacteria; Bacillota; Negativicutes; Selenomonadales; Selenomonadaceae;
OC Selenomonas.
OX NCBI_TaxID=702437 {ECO:0000313|EMBL:EHG24051.1, ECO:0000313|Proteomes:UP000003175};
RN [1] {ECO:0000313|EMBL:EHG24051.1, ECO:0000313|Proteomes:UP000003175}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0398 {ECO:0000313|EMBL:EHG24051.1,
RC ECO:0000313|Proteomes:UP000003175};
RG The Broad Institute Genome Sequencing Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Izard J., Ganesan A.,
RA Blanton J.M., Baranova O.V., Tanner A.C., Dewhirst F.E., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C.,
RA Freedman E., Gearin G., Gellesch M., Goldberg J., Griggs A., Gujja S.,
RA Heiman D., Howarth C., Larson L., Lui A., MacDonald P.J.P., Montmayeur A.,
RA Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T.,
RA Shenoy N., Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Selenomonas noxia F0398.";
RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the conversion of (8S)-3',8-cyclo-7,8-
CC dihydroguanosine 5'-triphosphate to cyclic pyranopterin monophosphate
CC (cPMP). {ECO:0000256|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:0000256|ARBA:ARBA00001637,
CC ECO:0000256|HAMAP-Rule:MF_01224};
CC -!- PATHWAY: Cofactor biosynthesis; molybdopterin biosynthesis.
CC {ECO:0000256|ARBA:ARBA00005046, ECO:0000256|HAMAP-Rule:MF_01224}.
CC -!- SUBUNIT: Homohexamer; trimer of dimers. {ECO:0000256|HAMAP-
CC Rule:MF_01224}.
CC -!- SIMILARITY: Belongs to the MoaC family. {ECO:0000256|HAMAP-
CC Rule:MF_01224}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EHG24051.1}.
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DR EMBL; ADGH01000016; EHG24051.1; -; Genomic_DNA.
DR RefSeq; WP_006696923.1; NZ_JH376860.1.
DR AlphaFoldDB; G5H478; -.
DR STRING; 702437.HMPREF9432_01725; -.
DR GeneID; 84787913; -.
DR PATRIC; fig|702437.3.peg.1758; -.
DR eggNOG; COG0315; Bacteria.
DR HOGENOM; CLU_074693_1_1_9; -.
DR UniPathway; UPA00344; -.
DR Proteomes; UP000003175; Unassembled WGS sequence.
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; Molybdopterin cofactor biosynthesis C (MoaC) domain; 1.
DR HAMAP; MF_01224_B; MoaC_B; 1.
DR InterPro; IPR023045; MoaC.
DR InterPro; IPR047594; MoaC_bact/euk.
DR InterPro; IPR036522; MoaC_sf.
DR InterPro; IPR002820; Mopterin_CF_biosynth-C_dom.
DR NCBIfam; TIGR00581; moaC; 1.
DR Pfam; PF01967; MoaC; 1.
DR SUPFAM; SSF55040; Molybdenum cofactor biosynthesis protein C, MoaC; 1.
PE 3: Inferred from homology;
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_01224};
KW Molybdenum cofactor biosynthesis {ECO:0000256|ARBA:ARBA00023150,
KW ECO:0000256|HAMAP-Rule:MF_01224}.
FT DOMAIN 17..153
FT /note="Molybdopterin cofactor biosynthesis C (MoaC)"
FT /evidence="ECO:0000259|Pfam:PF01967"
FT ACT_SITE 131
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01224"
FT BINDING 77..79
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01224"
FT BINDING 116..117
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01224"
SQ SEQUENCE 160 AA; 16879 MW; BCF7DF24F8653864 CRC64;
MPNLGLTHFD AGGAAVMVDV SGKEKTHREA VASGRIYVSE PVYDAIAGGA AAKGDVLGVA
RIAGIMAAKR TSDMIPLCHP LPLAKCTLNF ALEEVPRRAV RAEAAVKVTG ETGVEMEALH
AVSTALLTIY DMCKAIDKRM EIGDIRLERK SGGKSGTFVR
//
