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Database: UniProt
Entry: F2JU31_MARM1
LinkDB: F2JU31_MARM1
Original site: F2JU31_MARM1 
ID   F2JU31_MARM1            Unreviewed;       168 AA.
AC   F2JU31;
DT   31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   31-MAY-2011, sequence version 1.
DT   27-MAR-2024, entry version 71.
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=Marme_2302 {ECO:0000313|EMBL:ADZ91543.1};
OS   Marinomonas mediterranea (strain ATCC 700492 / JCM 21426 / NBRC 103028 /
OS   MMB-1).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC   Oceanospirillaceae; Marinomonas.
OX   NCBI_TaxID=717774 {ECO:0000313|EMBL:ADZ91543.1, ECO:0000313|Proteomes:UP000001062};
RN   [1] {ECO:0000313|EMBL:ADZ91543.1, ECO:0000313|Proteomes:UP000001062}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700492 / JCM 21426 / NBRC 103028 / MMB-1
RC   {ECO:0000313|Proteomes:UP000001062};
RX   PubMed=22675599; DOI=10.4056/sigs.2545743;
RA   Lucas-Elio P., Goodwin L., Woyke T., Pitluck S., Nolan M., Kyrpides N.C.,
RA   Detter J.C., Copeland A., Teshima H., Bruce D., Detter C., Tapia R.,
RA   Han S., Land M.L., Ivanova N., Mikhailova N., Johnston A.W.,
RA   Sanchez-Amat A.;
RT   "Complete genome sequence of the melanogenic marine bacterium Marinomonas
RT   mediterranea type strain (MMB-1(T)).";
RL   Stand. Genomic Sci. 6:63-73(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; CP002583; ADZ91543.1; -; Genomic_DNA.
DR   RefSeq; WP_013661448.1; NZ_CP047696.1.
DR   AlphaFoldDB; F2JU31; -.
DR   STRING; 717774.Marme_2302; -.
DR   KEGG; mme:Marme_2302; -.
DR   PATRIC; fig|717774.3.peg.2372; -.
DR   eggNOG; COG0315; Bacteria.
DR   HOGENOM; CLU_074693_1_1_6; -.
DR   OrthoDB; 9794429at2; -.
DR   UniPathway; UPA00344; -.
DR   Proteomes; UP000001062; 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:UP000001062}.
FT   DOMAIN          21..155
FT                   /note="Molybdopterin cofactor biosynthesis C (MoaC)"
FT                   /evidence="ECO:0000259|Pfam:PF01967"
FT   ACT_SITE        133
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01224"
FT   BINDING         81..83
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01224"
FT   BINDING         118..119
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01224"
SQ   SEQUENCE   168 AA;  17757 MW;  4D382FEB36A523D9 CRC64;
     MSTEIGTESL THLDAKGNAH MVDVGNKQIT ERSATARALV EMKPETLAKV IAGGLPKGDV
     LATVRIAGIQ AAKKTPDLIP LCHPLMLTKI TLDIEPINES QIEIRCTCKL SGKTGVEMEA
     LTGASVAALT LYDMCKAVDK GITIKETGLL TKTGGKSGNW NIDQEGSK
//
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