MOACB_SYNE7
ID MOACB_SYNE7 Reviewed; 319 AA.
AC Q56208; Q31NQ4;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 110.
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=Synpcc7942_1285;
OS Synechococcus elongatus (strain PCC 7942 / FACHB-805) (Anacystis nidulans
OS R2).
OC Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus.
OX NCBI_TaxID=1140;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9495759; DOI=10.1128/jb.180.5.1200-1206.1998;
RA Rubio L.M., Flores E., Herrero A.;
RT "The narA locus of Synechococcus sp. strain PCC 7942 consists of a cluster
RT of molybdopterin biosynthesis genes.";
RL J. Bacteriol. 180:1200-1206(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7942 / FACHB-805;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Schmutz J., Larimer F., Land M.,
RA Kyrpides N., Lykidis A., Richardson P.;
RT "Complete sequence of chromosome 1 of Synechococcus elongatus PCC 7942.";
RL Submitted (AUG-2005) 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: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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABB57315.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; X99625; CAA67945.1; -; Genomic_DNA.
DR EMBL; CP000100; ABB57315.1; ALT_INIT; Genomic_DNA.
DR AlphaFoldDB; Q56208; -.
DR SMR; Q56208; -.
DR STRING; 1140.Synpcc7942_1285; -.
DR PRIDE; Q56208; -.
DR EnsemblBacteria; ABB57315; ABB57315; Synpcc7942_1285.
DR KEGG; syf:Synpcc7942_1285; -.
DR eggNOG; COG0315; Bacteria.
DR eggNOG; COG0521; Bacteria.
DR HOGENOM; CLU_063423_1_1_3; -.
DR BioCyc; SYNEL:SYNPCC7942_1285-MON; -.
DR UniPathway; UPA00344; -.
DR GO; GO:0061799; F:cyclic pyranopterin monophosphate synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0006777; P:Mo-molybdopterin cofactor biosynthetic process; IEA:UniProtKB-KW.
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 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; IPR008284; MoCF_biosynth_CS.
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.
DR PROSITE; PS01078; MOCF_BIOSYNTHESIS_1; 1.
PE 3: Inferred from homology;
KW Lyase; Molybdenum cofactor biosynthesis.
FT CHAIN 1..319
FT /note="Molybdenum cofactor biosynthesis bifunctional
FT protein"
FT /id="PRO_0000097849"
FT REGION 1..145
FT /note="Molybdenum cofactor biosynthesis protein C"
FT REGION 146..319
FT /note="Molybdenum cofactor biosynthesis protein B"
FT ACT_SITE 114
FT /evidence="ECO:0000250|UniProtKB:P0A738"
FT BINDING 61..63
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P0A738"
FT BINDING 99..100
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P0A738"
SQ SEQUENCE 319 AA; 32972 MW; 57A6E9E9A4FE000A CRC64;
MIDVGDKAVT ERTARAEGWI RLAPEVYQRV TQGQLPKGDG FLLAQVAGIQ GAKRTADLLP
LCHPLPIEGV KIDCQPLADS QTIRVEARVR TTGKTGVEME ALAAVSAALL CLYDLTKMFD
ATAEIGGIGL LEKTGGKSGH WQRPAIAPDV APTGALAGVF ATVITVSDRV AADQAEDRSG
PLIQNWLTDQ AATIATATCV ADEPALIQAA IQAAIAQGSA LILLTGGTGL GPRDRTPEAI
ADLGAIPVPG IGEALRQAGR SETVMTWLSR SGGWMLEGSF VIALPGSSRA VSSGLAMLQP
LLPHSLAILK GADHGTVKG
