ID   MOACB_CHLTE             Reviewed;         312 AA.
AC   P59014;
DT   19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
DT   19-SEP-2002, sequence version 1.
DT   03-AUG-2022, entry version 107.
DE   RecName: Full=Molybdenum cofactor biosynthesis bifunctional protein;
DE   Includes:
DE     RecName: Full=Cyclic pyranopterin monophosphate synthase {ECO:0000250|UniProtKB:P0A738};
DE              EC=4.6.1.17 {ECO:0000250|UniProtKB:P0A738};
DE     AltName: Full=Molybdenum cofactor biosynthesis protein C {ECO:0000250|UniProtKB:P0A738};
DE   Includes:
DE     RecName: Full=Molybdenum cofactor biosynthesis protein B;
GN   Name=moaCB; OrderedLocusNames=CT1330;
OS   Chlorobaculum tepidum (strain ATCC 49652 / DSM 12025 / NBRC 103806 / TLS)
OS   (Chlorobium tepidum).
OC   Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae; Chlorobaculum.
OX   NCBI_TaxID=194439;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49652 / DSM 12025 / NBRC 103806 / TLS;
RX   PubMed=12093901; DOI=10.1073/pnas.132181499;
RA   Eisen J.A., Nelson K.E., Paulsen I.T., Heidelberg J.F., Wu M., Dodson R.J.,
RA   DeBoy R.T., Gwinn M.L., Nelson W.C., Haft D.H., Hickey E.K., Peterson J.D.,
RA   Durkin A.S., Kolonay J.F., Yang F., Holt I.E., Umayam L.A., Mason T.M.,
RA   Brenner M., Shea T.P., Parksey D.S., Nierman W.C., Feldblyum T.V.,
RA   Hansen C.L., Craven M.B., Radune D., Vamathevan J.J., Khouri H.M.,
RA   White O., Gruber T.M., Ketchum K.A., Venter J.C., Tettelin H., Bryant D.A.,
RA   Fraser C.M.;
RT   "The complete genome sequence of Chlorobium tepidum TLS, a photosynthetic,
RT   anaerobic, green-sulfur bacterium.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:9509-9514(2002).
CC   -!- FUNCTION: Catalyzes the conversion of (8S)-3',8-cyclo-7,8-
CC       dihydroguanosine 5'-triphosphate to cyclic pyranopterin monophosphate
CC       (cPMP). {ECO:0000250|UniProtKB:P0A738}.
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:0000250|UniProtKB:P0A738};
CC   -!- PATHWAY: Cofactor biosynthesis; molybdopterin biosynthesis.
CC       {ECO:0000250|UniProtKB:P0A738}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the MoaC family.
CC       {ECO:0000305}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the MoaB/Mog family.
CC       {ECO:0000305}.
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DR   EMBL; AE006470; AAM72559.1; -; Genomic_DNA.
DR   RefSeq; NP_662217.1; NC_002932.3.
DR   AlphaFoldDB; P59014; -.
DR   SMR; P59014; -.
DR   STRING; 194439.CT1330; -.
DR   EnsemblBacteria; AAM72559; AAM72559; CT1330.
DR   KEGG; cte:CT1330; -.
DR   PATRIC; fig|194439.7.peg.1210; -.
DR   eggNOG; COG0315; Bacteria.
DR   eggNOG; COG0521; Bacteria.
DR   HOGENOM; CLU_063423_1_1_10; -.
DR   OMA; TIYKTGV; -.
DR   OrthoDB; 1877633at2; -.
DR   UniPathway; UPA00344; -.
DR   Proteomes; UP000001007; 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   CDD; cd00886; MogA_MoaB; 1.
DR   Gene3D; 3.30.70.640; -; 1.
DR   Gene3D; 3.40.980.10; -; 1.
DR   HAMAP; MF_01224_B; MoaC_B; 1.
DR   InterPro; IPR023045; Mo_CF_biosynth-C.
DR   InterPro; IPR036425; MoaB/Mog-like_dom_sf.
DR   InterPro; IPR001453; MoaB/Mog_dom.
DR   InterPro; IPR012247; MoaC_MogA.
DR   InterPro; IPR036522; MoaC_sf.
DR   InterPro; IPR002820; Mopterin_CF_biosynth-C_dom.
DR   Pfam; PF01967; MoaC; 1.
DR   Pfam; PF00994; MoCF_biosynth; 1.
DR   PIRSF; PIRSF036594; MoaC_MogA; 1.
DR   SMART; SM00852; MoCF_biosynth; 1.
DR   SUPFAM; SSF53218; SSF53218; 1.
DR   SUPFAM; SSF55040; SSF55040; 1.
DR   TIGRFAMs; TIGR00581; moaC; 1.
DR   TIGRFAMs; TIGR00177; molyb_syn; 1.
PE   3: Inferred from homology;
KW   Lyase; Molybdenum cofactor biosynthesis; Reference proteome.
FT   CHAIN           1..312
FT                   /note="Molybdenum cofactor biosynthesis bifunctional
FT                   protein"
FT                   /id="PRO_0000097848"
FT   REGION          1..155
FT                   /note="Molybdenum cofactor biosynthesis protein C"
FT   REGION          156..312
FT                   /note="Molybdenum cofactor biosynthesis protein B"
FT   ACT_SITE        125
FT                   /evidence="ECO:0000250|UniProtKB:P0A738"
FT   BINDING         74..76
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P0A738"
FT   BINDING         110..111
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P0A738"
SQ   SEQUENCE   312 AA;  32916 MW;  7BBE7F9B9FAC907F CRC64;
     MEFTHLDENG MVRMADVSGK PPTRRKACAS GRIVMLPETI ALLRRKELPK GNVLAAAKIA
     GIQAAKQTST LIPLCHQLNL SWIDIEFEIG DDSIGIAATV ITRESTGVEM EALAAVSVAA
     LTIYDMCKAV DKTMEISAIR LDHKTGGKSS AAEYHPRTAI LVMSDSIAAG TATDHSGAIL
     REGLQKAGCA VEALTITPDE PVEIAATVEA WIGEGIEFIV TSGGTGLGPR DLAIDTLAPK
     FTRRLPGVEQ ELLRWGQTKT RTAMLSRLAA GVIGNTVVVC LPGSTSAAKD ALEVLVPAIF
     HAFPMLKGDG HA