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Database: UniProt
Entry: F6CRU0_MARPP
LinkDB: F6CRU0_MARPP
Original site: F6CRU0_MARPP 
ID   F6CRU0_MARPP            Unreviewed;       162 AA.
AC   F6CRU0;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   27-JUL-2011, sequence version 1.
DT   24-JAN-2024, entry version 66.
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=Mar181_1905 {ECO:0000313|EMBL:AEF54943.1};
OS   Marinomonas posidonica (strain CECT 7376 / NCIMB 14433 / IVIA-Po-181).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC   Oceanospirillaceae; Marinomonas.
OX   NCBI_TaxID=491952 {ECO:0000313|EMBL:AEF54943.1, ECO:0000313|Proteomes:UP000009230};
RN   [1] {ECO:0000313|EMBL:AEF54943.1, ECO:0000313|Proteomes:UP000009230}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CECT 7376 / NCIMB 14433 / IVIA-Po-181
RC   {ECO:0000313|Proteomes:UP000009230};
RX   PubMed=23458837; DOI=10.4056/sigs.2976373;
RA   Lucas-Elio P., Goodwin L., Woyke T., Pitluck S., Nolan M., Kyrpides N.C.,
RA   Detter J.C., Copeland A., Lu M., Bruce D., Detter C., Tapia R., Han S.,
RA   Land M.L., Ivanova N., Mikhailova N., Johnston A.W., Sanchez-Amat A.;
RT   "Complete genome sequence of Marinomonas posidonica type strain (IVIA-Po-
RT   181(T)).";
RL   Stand. Genomic Sci. 7:31-43(2012).
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; CP002771; AEF54943.1; -; Genomic_DNA.
DR   RefSeq; WP_013796418.1; NC_015559.1.
DR   AlphaFoldDB; F6CRU0; -.
DR   STRING; 491952.Mar181_1905; -.
DR   KEGG; mpc:Mar181_1905; -.
DR   eggNOG; COG0315; Bacteria.
DR   HOGENOM; CLU_074693_1_1_6; -.
DR   OrthoDB; 9794429at2; -.
DR   UniPathway; UPA00344; -.
DR   Proteomes; UP000009230; 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}.
FT   DOMAIN          16..150
FT                   /note="Molybdopterin cofactor biosynthesis C (MoaC)"
FT                   /evidence="ECO:0000259|Pfam:PF01967"
FT   ACT_SITE        128
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01224"
FT   BINDING         76..78
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01224"
FT   BINDING         113..114
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01224"
SQ   SEQUENCE   162 AA;  17135 MW;  719DFD9095484B34 CRC64;
     MSDSLTHLDH RGHAHMVDVS DKAPTKRTAT ARGVLTMQPE TLTKILAGGF AKGDVLATAR
     IAGIQAAKKT SDLIPLCHPL MLTKVSVDIA QLNEHQLEVL CTCALSGKTG VEMEALTGVS
     VAALTLYDMC KAVDKGIVIE NVQLVEKTGG KSGDWSVTNE PD
//
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