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Database: UniProt
Entry: E6XRP3_SHEP2
LinkDB: E6XRP3_SHEP2
Original site: E6XRP3_SHEP2 
ID   E6XRP3_SHEP2            Unreviewed;       158 AA.
AC   E6XRP3;
DT   08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT   08-MAR-2011, sequence version 1.
DT   24-JAN-2024, entry version 68.
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=Sput200_0249 {ECO:0000313|EMBL:ADV52737.1};
OS   Shewanella putrefaciens (strain 200).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=399804 {ECO:0000313|EMBL:ADV52737.1, ECO:0000313|Proteomes:UP000008209};
RN   [1] {ECO:0000313|EMBL:ADV52737.1, ECO:0000313|Proteomes:UP000008209}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=200 {ECO:0000313|EMBL:ADV52737.1,
RC   ECO:0000313|Proteomes:UP000008209};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., Munk A.C., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA   Chang Y.-J., Jeffries C., Kyrpides N., Ivanova N., Mikhailova N.,
RA   Kolker E., Lawrence C., McCue L.A., DiChristina T., Nealson K.,
RA   Fredrickson J.K., Woyke T.;
RT   "Complete sequence of Shewanella putrefaciens 200.";
RL   Submitted (JAN-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}.
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DR   EMBL; CP002457; ADV52737.1; -; Genomic_DNA.
DR   AlphaFoldDB; E6XRP3; -.
DR   SMR; E6XRP3; -.
DR   KEGG; shp:Sput200_0249; -.
DR   PATRIC; fig|399804.5.peg.251; -.
DR   HOGENOM; CLU_074693_1_1_6; -.
DR   OMA; IWDMVKS; -.
DR   OrthoDB; 9794429at2; -.
DR   UniPathway; UPA00344; -.
DR   Proteomes; UP000008209; 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..151
FT                   /note="Molybdopterin cofactor biosynthesis C (MoaC)"
FT                   /evidence="ECO:0000259|Pfam:PF01967"
FT   ACT_SITE        129
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         114..115
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01224"
SQ   SEQUENCE   158 AA;  17179 MW;  52371550D786D8A4 CRC64;
     MSNVFTHINA DGNAHMVDVT EKAVTEREAR AEAFIEMAST TLEMIMSGSH HKGDVFATAR
     IAGIQAAKKT SDLIPLCHPL MLTKVEVDLE AQPEHNRVRI TSLCKLSGKT GVEMEALTAA
     SVAALTIYDM CKAVQKDMVI SQVRLLEKRG GKSGHFKV
//
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