MOAC_RHOBA
ID MOAC_RHOBA Reviewed; 175 AA.
AC Q7UP45;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 07-MAR-2006, sequence version 2.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Cyclic pyranopterin monophosphate synthase {ECO:0000255|HAMAP-Rule:MF_01224};
DE EC=4.6.1.17 {ECO:0000255|HAMAP-Rule:MF_01224};
DE AltName: Full=Molybdenum cofactor biosynthesis protein C {ECO:0000255|HAMAP-Rule:MF_01224};
GN Name=moaC {ECO:0000255|HAMAP-Rule:MF_01224}; OrderedLocusNames=RB7175;
OS Rhodopirellula baltica (strain DSM 10527 / NCIMB 13988 / SH1).
OC Bacteria; Planctomycetes; Planctomycetia; Pirellulales; Pirellulaceae;
OC Rhodopirellula.
OX NCBI_TaxID=243090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 10527 / NCIMB 13988 / SH1;
RX PubMed=12835416; DOI=10.1073/pnas.1431443100;
RA Gloeckner F.O., Kube M., Bauer M., Teeling H., Lombardot T., Ludwig W.,
RA Gade D., Beck A., Borzym K., Heitmann K., Rabus R., Schlesner H., Amann R.,
RA Reinhardt R.;
RT "Complete genome sequence of the marine planctomycete Pirellula sp. strain
RT 1.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:8298-8303(2003).
CC -!- FUNCTION: Catalyzes the conversion of (8S)-3',8-cyclo-7,8-
CC dihydroguanosine 5'-triphosphate to cyclic pyranopterin monophosphate
CC (cPMP). {ECO:0000255|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:0000255|HAMAP-Rule:MF_01224};
CC -!- PATHWAY: Cofactor biosynthesis; molybdopterin biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_01224}.
CC -!- SUBUNIT: Homohexamer; trimer of dimers. {ECO:0000255|HAMAP-
CC Rule:MF_01224}.
CC -!- SIMILARITY: Belongs to the MoaC family. {ECO:0000255|HAMAP-
CC Rule:MF_01224}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAD75220.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; BX294145; CAD75220.1; ALT_INIT; Genomic_DNA.
DR RefSeq; NP_867673.1; NC_005027.1.
DR AlphaFoldDB; Q7UP45; -.
DR SMR; Q7UP45; -.
DR STRING; 243090.RB7175; -.
DR EnsemblBacteria; CAD75220; CAD75220; RB7175.
DR KEGG; rba:RB7175; -.
DR PATRIC; fig|243090.15.peg.3474; -.
DR eggNOG; COG0315; Bacteria.
DR HOGENOM; CLU_074693_1_1_0; -.
DR InParanoid; Q7UP45; -.
DR OrthoDB; 1595361at2; -.
DR UniPathway; UPA00344; -.
DR Proteomes; UP000001025; 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; -; 1.
DR HAMAP; MF_01224_B; MoaC_B; 1.
DR InterPro; IPR023045; Mo_CF_biosynth-C.
DR InterPro; IPR036522; MoaC_sf.
DR InterPro; IPR002820; Mopterin_CF_biosynth-C_dom.
DR Pfam; PF01967; MoaC; 1.
DR SUPFAM; SSF55040; SSF55040; 1.
DR TIGRFAMs; TIGR00581; moaC; 1.
PE 3: Inferred from homology;
KW Lyase; Molybdenum cofactor biosynthesis; Reference proteome.
FT CHAIN 1..175
FT /note="Cyclic pyranopterin monophosphate synthase"
FT /id="PRO_0000227027"
FT ACT_SITE 140
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01224"
FT BINDING 78..80
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01224"
FT BINDING 125..126
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01224"
SQ SEQUENCE 175 AA; 18656 MW; B8828D0D1C6CBFBA CRC64;
MKPDPRSTHF NAAGEVHMVD VTGKDITVRE AVASARIHMS ADAAEAIRRG DTKKGDVLAV
ARLAGIAGAK WTSHLIPLCH AIPIEAVSID FDWVDESDSD DDAVANQTLR CTATARTTAK
TGIEMESLTA ASTAALTVYD MLKSVDRAMV IDQVRLESKS GGKSGDFRRD TGDKA
