MOAC_LIMF3
ID MOAC_LIMF3 Reviewed; 165 AA.
AC B2GCM0;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-JUN-2008, sequence version 1.
DT 03-AUG-2022, entry version 71.
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=LAF_1066;
OS Limosilactobacillus fermentum (strain NBRC 3956 / LMG 18251) (Lactobacillus
OS fermentum).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC Limosilactobacillus.
OX NCBI_TaxID=334390;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 3956 / LMG 18251;
RX PubMed=18487258; DOI=10.1093/dnares/dsn009;
RA Morita H., Toh H., Fukuda S., Horikawa H., Oshima K., Suzuki T.,
RA Murakami M., Hisamatsu S., Kato Y., Takizawa T., Fukuoka H., Yoshimura T.,
RA Itoh K., O'Sullivan D.J., McKay L.L., Ohno H., Kikuchi J., Masaoka T.,
RA Hattori M.;
RT "Comparative genome analysis of Lactobacillus reuteri and Lactobacillus
RT fermentum reveal a genomic island for reuterin and cobalamin production.";
RL DNA Res. 15:151-161(2008).
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}.
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DR EMBL; AP008937; BAG27402.1; -; Genomic_DNA.
DR AlphaFoldDB; B2GCM0; -.
DR SMR; B2GCM0; -.
DR EnsemblBacteria; BAG27402; BAG27402; LAF_1066.
DR KEGG; lfe:LAF_1066; -.
DR PATRIC; fig|334390.5.peg.1182; -.
DR eggNOG; COG0315; Bacteria.
DR HOGENOM; CLU_074693_1_1_9; -.
DR OMA; IWDMVKS; -.
DR UniPathway; UPA00344; -.
DR Proteomes; UP000001697; 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.
FT CHAIN 1..165
FT /note="Cyclic pyranopterin monophosphate synthase"
FT /id="PRO_1000139278"
FT ACT_SITE 128
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01224"
FT BINDING 76..78
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01224"
FT BINDING 113..114
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01224"
SQ SEQUENCE 165 AA; 17725 MW; A9A4B4CA10190E2D CRC64;
MSDPLTHFND QNRAKMVDVT AKQVTARTAT ATGTIRMQPA TLDRIHAGTM KKGDVLAVAQ
VAGIMAAKQT SNLIPMCHLI PLTGVDIHFT DNNQDTITAT ATVKTKHVTG VEIEALLAVQ
TTLLTIYDMC KAIDRGMVID NVHLVEKDGG KSGHFQFGEA PESQA
