ID A0A160FAR6_9BACI Unreviewed; 162 AA.
AC A0A160FAR6;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE RecName: Full=Cyclic pyranopterin monophosphate synthase {ECO:0000256|ARBA:ARBA00012575, ECO:0000256|HAMAP-Rule:MF_01224};
DE EC=4.6.1.17 {ECO:0000256|ARBA:ARBA00012575, ECO:0000256|HAMAP-Rule:MF_01224};
DE AltName: Full=Molybdenum cofactor biosynthesis protein C {ECO:0000256|HAMAP-Rule:MF_01224};
GN Name=moaC {ECO:0000256|HAMAP-Rule:MF_01224,
GN ECO:0000313|EMBL:ANB63642.1};
GN ORFNames=GFC29_3070 {ECO:0000313|EMBL:ANB63642.1};
OS Anoxybacillus sp. B7M1.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Anoxybacillus.
OX NCBI_TaxID=1490057 {ECO:0000313|EMBL:ANB63642.1, ECO:0000313|Proteomes:UP000076753};
RN [1] {ECO:0000313|EMBL:ANB63642.1, ECO:0000313|Proteomes:UP000076753}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=b7m1 {ECO:0000313|Proteomes:UP000076753};
RA Evans L.H., Alamgir A., Owens N., Weber N.D., Virtaneva K., Barbian K.,
RA Babar A., Rosenke K.;
RL Submitted (APR-2016) 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:0000256|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:0000256|ARBA:ARBA00001637,
CC ECO:0000256|HAMAP-Rule:MF_01224};
CC -!- PATHWAY: Cofactor biosynthesis; molybdopterin biosynthesis.
CC {ECO:0000256|ARBA:ARBA00005046, ECO:0000256|HAMAP-Rule:MF_01224}.
CC -!- SUBUNIT: Homohexamer; trimer of dimers. {ECO:0000256|HAMAP-
CC Rule:MF_01224}.
CC -!- SIMILARITY: Belongs to the MoaC family. {ECO:0000256|HAMAP-
CC Rule:MF_01224}.
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DR EMBL; CP015436; ANB63642.1; -; Genomic_DNA.
DR RefSeq; WP_044743242.1; NZ_CP015436.1.
DR AlphaFoldDB; A0A160FAR6; -.
DR KEGG; anl:GFC29_3070; -.
DR PATRIC; fig|1490057.3.peg.3374; -.
DR OrthoDB; 9794429at2; -.
DR UniPathway; UPA00344; -.
DR Proteomes; UP000076753; 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; Molybdopterin cofactor biosynthesis C (MoaC) domain; 1.
DR HAMAP; MF_01224_B; MoaC_B; 1.
DR InterPro; IPR023045; MoaC.
DR InterPro; IPR047594; MoaC_bact/euk.
DR InterPro; IPR036522; MoaC_sf.
DR InterPro; IPR002820; Mopterin_CF_biosynth-C_dom.
DR NCBIfam; TIGR00581; moaC; 1.
DR Pfam; PF01967; MoaC; 1.
DR SUPFAM; SSF55040; Molybdenum cofactor biosynthesis protein C, MoaC; 1.
PE 3: Inferred from homology;
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_01224};
KW Molybdenum cofactor biosynthesis {ECO:0000256|ARBA:ARBA00023150,
KW ECO:0000256|HAMAP-Rule:MF_01224};
KW Reference proteome {ECO:0000313|Proteomes:UP000076753}.
FT DOMAIN 15..152
FT /note="Molybdopterin cofactor biosynthesis C (MoaC)"
FT /evidence="ECO:0000259|Pfam:PF01967"
FT ACT_SITE 130
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01224"
FT BINDING 75..77
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01224"
FT BINDING 115..116
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01224"
SQ SEQUENCE 162 AA; 17506 MW; 53849F767BF86671 CRC64;
MASFTHFNEQ GRAKMVDITE KADSVRVAVA RTSITVSQEI YEGIVSHSVK KGDVLAVAQV
AGIMAAKKTA DLIPMCHPLM LKGVDIQFEW RMHEQSCELI ITATVKTKGS TGVEMEALTA
ASVCALTVYD MCKALDKGMV IGPTYLVEKA GGKSGHYQRK AK
//
