ID A0A1Y4DLS7_9ACTN Unreviewed; 450 AA.
AC A0A1Y4DLS7;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 24-JAN-2024, entry version 23.
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=B5F74_07445 {ECO:0000313|EMBL:OUO60034.1};
OS Collinsella sp. An271.
OC Bacteria; Actinomycetota; Coriobacteriia; Coriobacteriales;
OC Coriobacteriaceae; Collinsella.
OX NCBI_TaxID=1965616 {ECO:0000313|EMBL:OUO60034.1, ECO:0000313|Proteomes:UP000195889};
RN [1] {ECO:0000313|Proteomes:UP000195889}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=An271 {ECO:0000313|Proteomes:UP000195889};
RA Medvecky M., Cejkova D., Polansky O., Karasova D., Kubasova T., Cizek A.,
RA Rychlik I.;
RT "Function of individual gut microbiota members based on whole genome
RT sequencing of pure cultures obtained from chicken caecum.";
RL Submitted (APR-2017) 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:OUO60034.1}.
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DR EMBL; NFJE01000007; OUO60034.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y4DLS7; -.
DR OrthoDB; 9794429at2; -.
DR UniPathway; UPA00344; -.
DR Proteomes; UP000195889; Unassembled WGS sequence.
DR GO; GO:0061799; F:cyclic pyranopterin monophosphate synthase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0005525; F:GTP binding; IEA:InterPro.
DR GO; GO:0006777; P:Mo-molybdopterin cofactor biosynthetic process; IEA:UniProtKB-UniRule.
DR CDD; cd01420; MoaC_PE; 1.
DR CDD; cd03116; MobB; 1.
DR Gene3D; 3.30.70.640; Molybdopterin cofactor biosynthesis C (MoaC) domain; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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; IPR004435; MobB_dom.
DR InterPro; IPR002820; Mopterin_CF_biosynth-C_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR NCBIfam; TIGR00581; moaC; 1.
DR NCBIfam; TIGR00176; mobB; 1.
DR PANTHER; PTHR40072:SF1; MOLYBDOPTERIN-GUANINE DINUCLEOTIDE BIOSYNTHESIS ADAPTER PROTEIN; 1.
DR PANTHER; PTHR40072; MOLYBDOPTERIN-GUANINE DINUCLEOTIDE BIOSYNTHESIS ADAPTER PROTEIN-RELATED; 1.
DR Pfam; PF01967; MoaC; 1.
DR Pfam; PF03205; MobB; 1.
DR SUPFAM; SSF55040; Molybdenum cofactor biosynthesis protein C, MoaC; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 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:UP000195889}.
FT DOMAIN 66..210
FT /note="Molybdopterin cofactor biosynthesis C (MoaC)"
FT /evidence="ECO:0000259|Pfam:PF01967"
FT DOMAIN 270..384
FT /note="Molybdopterin-guanine dinucleotide biosynthesis
FT protein B (MobB)"
FT /evidence="ECO:0000259|Pfam:PF03205"
FT REGION 1..49
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 221..262
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 188
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01224"
FT BINDING 126..128
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01224"
FT BINDING 173..174
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01224"
SQ SEQUENCE 450 AA; 47812 MW; B28D60CC21F88EE4 CRC64;
MIKRATGEKY PTAVVETDGP GQQGAPDAPT ADGHQDAGNT DAAASPARDA YRDTLTHVDE
KGDVRMVDVS DKAVTQRLAV AEGSILMHPE TQTMVLEDRA KKGDVLACAR VAGIMASKRT
SDLIPMCHPL MITKSKVDIE PIPAQGDGAR ADGRVGFRVT STLGVTGVTG IEMEALTATS
VACLTIYDMC KAVDRGMEIV DVRLLHKEGG RSGVWERAEQ ADASAVAPAT DTAPATDAVP
DSAETADPVE PEPASPLPGG PGAKAAAPAI AFIGYQNSGK TTLVEKIIKR LTQRGLRVGS
IKHHGHKGFD IDQPGKDSWR HAQAGSRHVG LVAPGQYAEY AYTENEVPVG DLLTHYTDVD
IVIVEGYKTA GLPNIVVTRS GVDRLRGDTS YDLIDENTLA IACNDVVERN FRARAAREAE
QADAVRELPP FISINDAAAL VNFILRRLGR
//
