MOAC_HELPY
ID MOAC_HELPY Reviewed; 158 AA.
AC Q48260; Q05188;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 119.
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=HP_0798;
OS Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=85962;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700392 / 26695;
RX PubMed=9252185; DOI=10.1038/41483;
RA Tomb J.-F., White O., Kerlavage A.R., Clayton R.A., Sutton G.G.,
RA Fleischmann R.D., Ketchum K.A., Klenk H.-P., Gill S.R., Dougherty B.A.,
RA Nelson K.E., Quackenbush J., Zhou L., Kirkness E.F., Peterson S.N.,
RA Loftus B.J., Richardson D.L., Dodson R.J., Khalak H.G., Glodek A.,
RA McKenney K., FitzGerald L.M., Lee N., Adams M.D., Hickey E.K., Berg D.E.,
RA Gocayne J.D., Utterback T.R., Peterson J.D., Kelley J.M., Cotton M.D.,
RA Weidman J.F., Fujii C., Bowman C., Watthey L., Wallin E., Hayes W.S.,
RA Borodovsky M., Karp P.D., Smith H.O., Fraser C.M., Venter J.C.;
RT "The complete genome sequence of the gastric pathogen Helicobacter
RT pylori.";
RL Nature 388:539-547(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 14-158.
RC STRAIN=ATCC 43504 / NCTC 11637 / JCM 7653 / RPH 13487;
RX PubMed=9287032; DOI=10.1128/jb.179.17.5643-5647.1997;
RA Jones A.C., Logan R.P., Foynes S., Cockayne A., Wren B.W., Penn C.W.;
RT "A flagellar sheath protein of Helicobacter pylori is identical to HpaA, a
RT putative N-acetylneuraminyllactose-binding hemagglutinin, but is not an
RT adhesin for AGS cells.";
RL J. Bacteriol. 179:5643-5647(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 8-126.
RC STRAIN=8826;
RX PubMed=7678592; DOI=10.1128/jb.175.3.674-683.1993;
RA Evans D.G., Karjalainen T.K., Evans D.J. Jr., Graham D.Y., Lee C.-H.;
RT "Cloning, nucleotide sequence, and expression of a gene encoding an adhesin
RT subunit protein of Helicobacter pylori.";
RL J. Bacteriol. 175:674-683(1993).
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; AE000511; AAD07848.1; -; Genomic_DNA.
DR EMBL; X92502; CAA63245.1; -; Genomic_DNA.
DR EMBL; X61574; CAA43772.1; -; Genomic_DNA.
DR PIR; F64619; F64619.
DR RefSeq; NP_207591.1; NC_000915.1.
DR RefSeq; WP_001131513.1; NC_018939.1.
DR AlphaFoldDB; Q48260; -.
DR SMR; Q48260; -.
DR DIP; DIP-3520N; -.
DR IntAct; Q48260; 2.
DR MINT; Q48260; -.
DR STRING; 85962.C694_04090; -.
DR PaxDb; Q48260; -.
DR EnsemblBacteria; AAD07848; AAD07848; HP_0798.
DR KEGG; hpy:HP_0798; -.
DR PATRIC; fig|85962.47.peg.850; -.
DR eggNOG; COG0315; Bacteria.
DR OMA; IWDMVKS; -.
DR PhylomeDB; Q48260; -.
DR UniPathway; UPA00344; -.
DR Proteomes; UP000000429; 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..158
FT /note="Cyclic pyranopterin monophosphate synthase"
FT /id="PRO_0000097804"
FT ACT_SITE 127
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01224"
FT BINDING 74..76
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01224"
FT BINDING 112..113
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01224"
FT CONFLICT 47
FT /note="C -> G (in Ref. 2 and 3)"
FT /evidence="ECO:0000305"
FT CONFLICT 64
FT /note="G -> A (in Ref. 3; CAA43772)"
FT /evidence="ECO:0000305"
FT CONFLICT 108
FT /note="T -> S (in Ref. 3; CAA43772)"
FT /evidence="ECO:0000305"
FT CONFLICT 114..126
FT /note="ALMSVSIGLLTIY -> GANECERRAFNHL (in Ref. 3)"
FT /evidence="ECO:0000305"
FT CONFLICT 120
FT /note="I -> V (in Ref. 2; CAA63245)"
FT /evidence="ECO:0000305"
FT CONFLICT 145
FT /note="H -> Y (in Ref. 2; CAA63245)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 158 AA; 17271 MW; 95813DE88C069A7D CRC64;
MPLTHLNEEN QPKMVDIGDK ETTERIALAS GRISMNKEAY DAIINHCVKK GPVLQTAIIA
GIMGAKKTSE LIPMCHPIML NGVDIDILEE KETCSFKLYA RVKTQAKTGV EMEALMSVSI
GLLTIYDMVK AIDKSMTISG VMLEHKSGGK SGDYNAKK
