ID A0A1X0CZ82_9MYCO Unreviewed; 385 AA.
AC A0A1X0CZ82;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
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 ORFNames=BST26_18695 {ECO:0000313|EMBL:ORA65388.1};
OS Mycolicibacterium insubricum.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=444597 {ECO:0000313|EMBL:ORA65388.1, ECO:0000313|Proteomes:UP000192801};
RN [1] {ECO:0000313|EMBL:ORA65388.1, ECO:0000313|Proteomes:UP000192801}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45130 {ECO:0000313|EMBL:ORA65388.1,
RC ECO:0000313|Proteomes:UP000192801};
RA Tortoli E., Trovato A., Cirillo D.M.;
RT "The new phylogeny of genus Mycobacterium.";
RL Submitted (DEC-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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ORA65388.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; MVHS01000062; ORA65388.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1X0CZ82; -.
DR STRING; 444597.BST26_18695; -.
DR OrthoDB; 9794429at2; -.
DR UniPathway; UPA00344; -.
DR Proteomes; UP000192801; Unassembled WGS sequence.
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; cd00886; MogA_MoaB; 1.
DR Gene3D; 3.40.980.10; MoaB/Mog-like domain; 1.
DR Gene3D; 3.30.70.640; Molybdopterin cofactor biosynthesis C (MoaC) domain; 1.
DR HAMAP; MF_01224_B; MoaC_B; 1.
DR InterPro; IPR036425; MoaB/Mog-like_dom_sf.
DR InterPro; IPR001453; MoaB/Mog_dom.
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 PANTHER; PTHR43764; MOLYBDENUM COFACTOR BIOSYNTHESIS; 1.
DR PANTHER; PTHR43764:SF1; MOLYBDOPTERIN MOLYBDOTRANSFERASE; 1.
DR Pfam; PF01967; MoaC; 1.
DR Pfam; PF00994; MoCF_biosynth; 1.
DR SMART; SM00852; MoCF_biosynth; 1.
DR SUPFAM; SSF55040; Molybdenum cofactor biosynthesis protein C, MoaC; 1.
DR SUPFAM; SSF53218; Molybdenum cofactor biosynthesis proteins; 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:UP000192801}.
FT DOMAIN 177..319
FT /note="MoaB/Mog"
FT /evidence="ECO:0000259|SMART:SM00852"
FT REGION 327..385
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 128
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01224"
FT BINDING 77..79
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01224"
FT BINDING 113..114
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01224"
SQ SEQUENCE 385 AA; 38383 MW; 8CB622454DD96195 CRC64;
MAADELSHLR ADGTAAMVDV GGKPVTARVA VAGATFITTP AVLAAVTAGT VGKGDVLATA
RIAGIMAAKR TAELIPLCHP LPLDRVAVDF RLHADRIEVT ATTATTGRTG VEMEALTAVT
VAGLTLHDMV KAMDPAAVLT DIALREKTGG KHGHWTRPGA ETAPPPGRVA LADTGTAIVL
VSSTRIAAGE RTDKTGPVIA DWLRDRGFAV GDPRGVADAD FAAALAAALA ETPAVLISTG
GTGPTNDDRV PEATAARLTM PMPGIAEAMR ADGRRSTPFA ALSRGLAGLA GSTFVVNLPG
STGGVADGLA VLGPLLDHLV GLAGGSARPE EEAELAEPAE PALAGSDHWV GGGGASGASA
DGAEGKLGPP HVPGPGTPGG PREHR
//
