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Database: UniProt
Entry: D7DL15_METV0
LinkDB: D7DL15_METV0
Original site: D7DL15_METV0 
ID   D7DL15_METV0            Unreviewed;       162 AA.
AC   D7DL15;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   24-JAN-2024, entry version 75.
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   OrderedLocusNames=M301_0239 {ECO:0000313|EMBL:ADI28626.1};
OS   Methylotenera versatilis (strain 301).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC   Methylophilaceae; Methylotenera.
OX   NCBI_TaxID=666681 {ECO:0000313|EMBL:ADI28626.1, ECO:0000313|Proteomes:UP000000383};
RN   [1] {ECO:0000313|Proteomes:UP000000383}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=301 {ECO:0000313|Proteomes:UP000000383};
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., Clum A., Land M., Hauser L., Kyrpides N., Ivanova N.,
RA   Chistoservova L., Kalyuzhnaya M., Woyke T.;
RT   "Complete sequence of Methylotenera sp. 301.";
RL   Submitted (MAY-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ADI28626.1, ECO:0000313|Proteomes:UP000000383}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=301 {ECO:0000313|EMBL:ADI28626.1,
RC   ECO:0000313|Proteomes:UP000000383};
RX   PubMed=21622745; DOI=10.1128/JB.00404-11;
RA   Lapidus A., Clum A., Labutti K., Kaluzhnaya M.G., Lim S., Beck D.A.,
RA   Glavina Del Rio T., Nolan M., Mavromatis K., Huntemann M., Lucas S.,
RA   Lidstrom M.E., Ivanova N., Chistoserdova L.;
RT   "Genomes of three methylotrophs from a single niche uncover genetic and
RT   metabolic divergence of Methylophilaceae.";
RL   J. Bacteriol. 193:3757-3764(2011).
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}.
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DR   EMBL; CP002056; ADI28626.1; -; Genomic_DNA.
DR   RefSeq; WP_013146943.1; NC_014207.1.
DR   AlphaFoldDB; D7DL15; -.
DR   STRING; 666681.M301_0239; -.
DR   KEGG; meh:M301_0239; -.
DR   eggNOG; COG0315; Bacteria.
DR   HOGENOM; CLU_074693_1_1_4; -.
DR   OrthoDB; 9794429at2; -.
DR   UniPathway; UPA00344; -.
DR   Proteomes; UP000000383; 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; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000383}.
FT   DOMAIN          19..154
FT                   /note="Molybdopterin cofactor biosynthesis C (MoaC)"
FT                   /evidence="ECO:0000259|Pfam:PF01967"
FT   ACT_SITE        132
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01224"
FT   BINDING         79..81
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01224"
FT   BINDING         117..118
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01224"
SQ   SEQUENCE   162 AA;  16925 MW;  96643DF67762C139 CRC64;
     MTDAANTLTH FDNSGQAHMV DVGDKAHTKR IAIASGVITM QTSTLALIKS GDSKKGDVLG
     IARIAAIQGS KRTSDLIPLC HPIGLTKVAV TFEIDDKNTS VICTATTETA GQTGVEMEAL
     TAVSVGLLTI YDMCKAVDRG MTISGIKLLE KHGGKSGEWV AP
//
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