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Database: UniProt
Entry: I4N1I5_9PSED
LinkDB: I4N1I5_9PSED
Original site: I4N1I5_9PSED 
ID   I4N1I5_9PSED            Unreviewed;       157 AA.
AC   I4N1I5;
DT   05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT   05-SEP-2012, sequence version 1.
DT   24-JAN-2024, entry version 50.
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   ECO:0000313|EMBL:EIK95325.1};
GN   ORFNames=PMM47T1_17560 {ECO:0000313|EMBL:EIK95325.1};
OS   Pseudomonas sp. M47T1.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=1179778 {ECO:0000313|EMBL:EIK95325.1, ECO:0000313|Proteomes:UP000004339};
RN   [1] {ECO:0000313|EMBL:EIK95325.1, ECO:0000313|Proteomes:UP000004339}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M47T1 {ECO:0000313|EMBL:EIK95325.1,
RC   ECO:0000313|Proteomes:UP000004339};
RX   PubMed=22887683; DOI=10.1128/JB.01116-12;
RA   Proenca D.N., Espirito Santo C., Grass G., Morais P.V.;
RT   "Draft Genome Sequence of Pseudomonas sp. Strain M47T1, Carried by
RT   Bursaphelenchus xylophilus Isolated from Pinus pinaster.";
RL   J. Bacteriol. 194:4789-4790(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}.
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:EIK95325.1}.
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DR   EMBL; AJWX01000016; EIK95325.1; -; Genomic_DNA.
DR   RefSeq; WP_008371292.1; NZ_AJWX01000016.1.
DR   AlphaFoldDB; I4N1I5; -.
DR   STRING; 1179778.PMM47T1_17560; -.
DR   PATRIC; fig|1179778.3.peg.3512; -.
DR   eggNOG; COG0315; Bacteria.
DR   OrthoDB; 9794429at2; -.
DR   UniPathway; UPA00344; -.
DR   Proteomes; UP000004339; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000004339}.
FT   DOMAIN          13..147
FT                   /note="Molybdopterin cofactor biosynthesis C (MoaC)"
FT                   /evidence="ECO:0000259|Pfam:PF01967"
FT   ACT_SITE        125
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01224"
FT   BINDING         73..75
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01224"
FT   BINDING         110..111
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01224"
SQ   SEQUENCE   157 AA;  16547 MW;  9F3F4A308E2865A3 CRC64;
     MLTHLDSQGR ANMVDVTEKA VTSREAVAEA RVRMLPQTLQ MIVDGGHPKG DVFAVARIAG
     IQAAKKTSDL IPLCHPLMLT SVKVELSADG ADAVRIVARC KLAGQTGVEM EALTAASVAA
     LTLYDMCKAV DKGMIIESVR LLEKTGGKSG DYQAVPA
//
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